Spectrin beta chain [Melipona quadrifasciata]
Protein Classification
List of domain hits
| Name | Accession | Description | Interval | E-value | ||||||||||
| VPS10 super family | cl33391 | VPS10 domain; |
2428-3031 | 1.58e-128 | ||||||||||
VPS10 domain; The actual alignment was detected with superfamily member smart00602: Pssm-ID: 214740 [Multi-domain] Cd Length: 612 Bit Score: 419.89 E-value: 1.58e-128
|
||||||||||||||
| CH_SPTB-like_rpt1 | cd21246 | first calponin homology (CH) domain found in the beta-I spectrin-like subfamily; The beta-I ... |
36-152 | 2.06e-82 | ||||||||||
first calponin homology (CH) domain found in the beta-I spectrin-like subfamily; The beta-I spectrin-like family includes beta-I, -II, -III and -IV spectrins. Spectrin is an actin crosslinking and molecular scaffold protein that links the plasma membrane to the actin cytoskeleton, and functions in the determination of cell shape, arrangement of transmembrane proteins, and organization of organelles. It is composed of two antiparallel dimers of alpha- and beta- subunits. Beta-I spectrin, also called spectrin beta chain, erythrocytic (SPTB), may be involved in anaemia pathogenesis. Beta-II spectrin, also called spectrin beta chain, non-erythrocytic 1 (SPTBN1), or fodrin beta chain, is a component of fodrin, which is the general spectrin-like protein that seems to be involved in secretion. Fodrin interacts with calmodulin in a calcium-dependent manner and is thus a candidate for the calcium-dependent movement of the cytoskeleton at the membrane. Beta-III spectrin, also called spectrin beta chain, non-erythrocytic 2 (SPTBN2), or spinocerebellar ataxia 5 protein (SCA5), may play a crucial role as a longer actin-membrane cross-linker or fulfill the need for greater extensible flexibility than can be provided by the other smaller conventional spectrins. Beta-IV spectrin is also called spectrin, non-erythroid beta chain 3 (SPTBN3) or spectrin beta chain, non-erythrocytic 4 (SPTBN4). Its mutation associates with congenital myopathy, neuropathy, and central deafness. Members of this subfamily contain two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs. : Pssm-ID: 409095 Cd Length: 117 Bit Score: 266.54 E-value: 2.06e-82
|
||||||||||||||
| CH_SPTB_like_rpt2 | cd21248 | second calponin homology (CH) domain found in the beta-I spectrin-like subfamily; The beta-I ... |
169-273 | 2.12e-78 | ||||||||||
second calponin homology (CH) domain found in the beta-I spectrin-like subfamily; The beta-I spectrin-like family includes beta-I, -II, -III and -IV spectrins. Spectrin is an actin crosslinking and molecular scaffold protein that links the plasma membrane to the actin cytoskeleton, and functions in the determination of cell shape, arrangement of transmembrane proteins, and organization of organelles. It is composed of two antiparallel dimers of alpha- and beta- subunits. Beta-I spectrin, also called spectrin beta chain, erythrocytic (SPTB), may be involved in anaemia pathogenesis. Beta-II spectrin, also called spectrin beta chain, non-erythrocytic 1 (SPTBN1), or fodrin beta chain, is a component of fodrin, which is the general spectrin-like protein that seems to be involved in secretion. Fodrin interacts with calmodulin in a calcium-dependent manner and is thus a candidate for the calcium-dependent movement of the cytoskeleton at the membrane. Beta-III spectrin, also called spectrin beta chain, non-erythrocytic 2 (SPTBN2), or spinocerebellar ataxia 5 protein (SCA5), may play a crucial role as a longer actin-membrane cross-linker or fulfill the need for greater extensible flexibility than can be provided by the other smaller conventional spectrins. Beta-IV spectrin is also called spectrin, non-erythroid beta chain 3 (SPTBN3) or spectrin beta chain, non-erythrocytic 4 (SPTBN4). Its mutation associates with congenital myopathy, neuropathy, and central deafness. Members of this subfamily contain two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs. : Pssm-ID: 409097 Cd Length: 105 Bit Score: 254.63 E-value: 2.12e-78
|
||||||||||||||
| SPEC | cd00176 | Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
638-845 | 9.08e-50 | ||||||||||
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here : Pssm-ID: 238103 [Multi-domain] Cd Length: 213 Bit Score: 177.25 E-value: 9.08e-50
|
||||||||||||||
| SPEC | cd00176 | Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
525-740 | 2.07e-48 | ||||||||||
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here : Pssm-ID: 238103 [Multi-domain] Cd Length: 213 Bit Score: 173.40 E-value: 2.07e-48
|
||||||||||||||
| SPEC | cd00176 | Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
1546-1758 | 2.83e-48 | ||||||||||
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here : Pssm-ID: 238103 [Multi-domain] Cd Length: 213 Bit Score: 173.02 E-value: 2.83e-48
|
||||||||||||||
| SPEC | cd00176 | Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
1759-1967 | 4.30e-45 | ||||||||||
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here : Pssm-ID: 238103 [Multi-domain] Cd Length: 213 Bit Score: 163.77 E-value: 4.30e-45
|
||||||||||||||
| PH_beta_spectrin | cd10571 | Beta-spectrin pleckstrin homology (PH) domain; Beta spectrin binds actin and functions as a ... |
2195-2290 | 6.86e-45 | ||||||||||
Beta-spectrin pleckstrin homology (PH) domain; Beta spectrin binds actin and functions as a major component of the cytoskeleton underlying cellular membranes. Beta spectrin consists of multiple spectrin repeats followed by a PH domain, which binds to inositol-1,4,5-trisphosphate. The PH domain of beta-spectrin is thought to play a role in the association of spectrin with the plasma membrane of cells. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes. : Pssm-ID: 269975 Cd Length: 106 Bit Score: 158.93 E-value: 6.86e-45
|
||||||||||||||
| SPEC | cd00176 | Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
954-1167 | 1.15e-44 | ||||||||||
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here : Pssm-ID: 238103 [Multi-domain] Cd Length: 213 Bit Score: 162.62 E-value: 1.15e-44
|
||||||||||||||
| SPEC | cd00176 | Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
1338-1543 | 4.28e-44 | ||||||||||
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here : Pssm-ID: 238103 [Multi-domain] Cd Length: 213 Bit Score: 161.07 E-value: 4.28e-44
|
||||||||||||||
| SPEC | cd00176 | Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
847-1057 | 8.32e-42 | ||||||||||
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here : Pssm-ID: 238103 [Multi-domain] Cd Length: 213 Bit Score: 154.53 E-value: 8.32e-42
|
||||||||||||||
| SPEC | cd00176 | Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
1169-1436 | 4.11e-33 | ||||||||||
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here : Pssm-ID: 238103 [Multi-domain] Cd Length: 213 Bit Score: 129.49 E-value: 4.11e-33
|
||||||||||||||
| SPEC | smart00150 | Spectrin repeats; |
422-521 | 3.99e-20 | ||||||||||
Spectrin repeats; : Pssm-ID: 197544 [Multi-domain] Cd Length: 101 Bit Score: 88.16 E-value: 3.99e-20
|
||||||||||||||
| LDLa | cd00112 | Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central ... |
3441-3475 | 2.75e-16 | ||||||||||
Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central role in mammalian cholesterol metabolism; the receptor protein binds LDL and transports it into cells by endocytosis; 7 successive cysteine-rich repeats of about 40 amino acids are present in the N-terminal of this multidomain membrane protein; other homologous domains occur in related receptors, including the very low-density lipoprotein receptor and the LDL receptor-related protein/alpha 2-macroglobulin receptor, and in proteins which are functionally unrelated, such as the C9 component of complement; the binding of calcium is required for in vitro formation of the native disulfide isomer and is necessary in establishing and maintaining the modular structure : Pssm-ID: 238060 Cd Length: 35 Bit Score: 74.94 E-value: 2.75e-16
|
||||||||||||||
| LDLa | cd00112 | Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central ... |
3363-3397 | 6.06e-16 | ||||||||||
Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central role in mammalian cholesterol metabolism; the receptor protein binds LDL and transports it into cells by endocytosis; 7 successive cysteine-rich repeats of about 40 amino acids are present in the N-terminal of this multidomain membrane protein; other homologous domains occur in related receptors, including the very low-density lipoprotein receptor and the LDL receptor-related protein/alpha 2-macroglobulin receptor, and in proteins which are functionally unrelated, such as the C9 component of complement; the binding of calcium is required for in vitro formation of the native disulfide isomer and is necessary in establishing and maintaining the modular structure : Pssm-ID: 238060 Cd Length: 35 Bit Score: 73.78 E-value: 6.06e-16
|
||||||||||||||
| LDLa | cd00112 | Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central ... |
3484-3518 | 3.40e-14 | ||||||||||
Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central role in mammalian cholesterol metabolism; the receptor protein binds LDL and transports it into cells by endocytosis; 7 successive cysteine-rich repeats of about 40 amino acids are present in the N-terminal of this multidomain membrane protein; other homologous domains occur in related receptors, including the very low-density lipoprotein receptor and the LDL receptor-related protein/alpha 2-macroglobulin receptor, and in proteins which are functionally unrelated, such as the C9 component of complement; the binding of calcium is required for in vitro formation of the native disulfide isomer and is necessary in establishing and maintaining the modular structure : Pssm-ID: 238060 Cd Length: 35 Bit Score: 69.16 E-value: 3.40e-14
|
||||||||||||||
| FN3 super family | cl27307 | Fibronectin type 3 domain [General function prediction only]; |
3766-4135 | 1.20e-13 | ||||||||||
Fibronectin type 3 domain [General function prediction only]; The actual alignment was detected with superfamily member COG3401: Pssm-ID: 442628 [Multi-domain] Cd Length: 603 Bit Score: 77.35 E-value: 1.20e-13
|
||||||||||||||
| Spectrin | pfam00435 | Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ... |
1970-2029 | 3.14e-13 | ||||||||||
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in cytoskeletal structure. These include spectrin, alpha-actinin and dystrophin. The sequence repeat used in this family is taken from the structural repeat in reference. The spectrin domain- repeat forms a three helix bundle. The second helix is interrupted by proline in some sequences. The repeats are defined by a characteriztic tryptophan (W) residue at position 17 in helix A and a leucine (L) at 2 residues from the carboxyl end of helix C. Although the domain occurs in multiple repeats along sequences, the domains are actually stable on their own - ie they act, biophysically, like domains rather than repeats that along function when aggregated. : Pssm-ID: 395348 [Multi-domain] Cd Length: 105 Bit Score: 68.50 E-value: 3.14e-13
|
||||||||||||||
| LDLa | cd00112 | Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central ... |
3633-3667 | 4.26e-13 | ||||||||||
Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central role in mammalian cholesterol metabolism; the receptor protein binds LDL and transports it into cells by endocytosis; 7 successive cysteine-rich repeats of about 40 amino acids are present in the N-terminal of this multidomain membrane protein; other homologous domains occur in related receptors, including the very low-density lipoprotein receptor and the LDL receptor-related protein/alpha 2-macroglobulin receptor, and in proteins which are functionally unrelated, such as the C9 component of complement; the binding of calcium is required for in vitro formation of the native disulfide isomer and is necessary in establishing and maintaining the modular structure : Pssm-ID: 238060 Cd Length: 35 Bit Score: 65.69 E-value: 4.26e-13
|
||||||||||||||
| LDLa | cd00112 | Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central ... |
3523-3561 | 7.44e-12 | ||||||||||
Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central role in mammalian cholesterol metabolism; the receptor protein binds LDL and transports it into cells by endocytosis; 7 successive cysteine-rich repeats of about 40 amino acids are present in the N-terminal of this multidomain membrane protein; other homologous domains occur in related receptors, including the very low-density lipoprotein receptor and the LDL receptor-related protein/alpha 2-macroglobulin receptor, and in proteins which are functionally unrelated, such as the C9 component of complement; the binding of calcium is required for in vitro formation of the native disulfide isomer and is necessary in establishing and maintaining the modular structure : Pssm-ID: 238060 Cd Length: 35 Bit Score: 62.22 E-value: 7.44e-12
|
||||||||||||||
| LDLa | cd00112 | Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central ... |
3403-3436 | 9.97e-12 | ||||||||||
Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central role in mammalian cholesterol metabolism; the receptor protein binds LDL and transports it into cells by endocytosis; 7 successive cysteine-rich repeats of about 40 amino acids are present in the N-terminal of this multidomain membrane protein; other homologous domains occur in related receptors, including the very low-density lipoprotein receptor and the LDL receptor-related protein/alpha 2-macroglobulin receptor, and in proteins which are functionally unrelated, such as the C9 component of complement; the binding of calcium is required for in vitro formation of the native disulfide isomer and is necessary in establishing and maintaining the modular structure : Pssm-ID: 238060 Cd Length: 35 Bit Score: 61.84 E-value: 9.97e-12
|
||||||||||||||
| Spectrin | pfam00435 | Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ... |
298-408 | 2.60e-11 | ||||||||||
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in cytoskeletal structure. These include spectrin, alpha-actinin and dystrophin. The sequence repeat used in this family is taken from the structural repeat in reference. The spectrin domain- repeat forms a three helix bundle. The second helix is interrupted by proline in some sequences. The repeats are defined by a characteriztic tryptophan (W) residue at position 17 in helix A and a leucine (L) at 2 residues from the carboxyl end of helix C. Although the domain occurs in multiple repeats along sequences, the domains are actually stable on their own - ie they act, biophysically, like domains rather than repeats that along function when aggregated. : Pssm-ID: 395348 [Multi-domain] Cd Length: 105 Bit Score: 63.11 E-value: 2.60e-11
|
||||||||||||||
| LDLa | cd00112 | Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central ... |
3675-3710 | 4.36e-11 | ||||||||||
Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central role in mammalian cholesterol metabolism; the receptor protein binds LDL and transports it into cells by endocytosis; 7 successive cysteine-rich repeats of about 40 amino acids are present in the N-terminal of this multidomain membrane protein; other homologous domains occur in related receptors, including the very low-density lipoprotein receptor and the LDL receptor-related protein/alpha 2-macroglobulin receptor, and in proteins which are functionally unrelated, such as the C9 component of complement; the binding of calcium is required for in vitro formation of the native disulfide isomer and is necessary in establishing and maintaining the modular structure : Pssm-ID: 238060 Cd Length: 35 Bit Score: 60.30 E-value: 4.36e-11
|
||||||||||||||
| LDLa | cd00112 | Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central ... |
3579-3613 | 1.06e-10 | ||||||||||
Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central role in mammalian cholesterol metabolism; the receptor protein binds LDL and transports it into cells by endocytosis; 7 successive cysteine-rich repeats of about 40 amino acids are present in the N-terminal of this multidomain membrane protein; other homologous domains occur in related receptors, including the very low-density lipoprotein receptor and the LDL receptor-related protein/alpha 2-macroglobulin receptor, and in proteins which are functionally unrelated, such as the C9 component of complement; the binding of calcium is required for in vitro formation of the native disulfide isomer and is necessary in establishing and maintaining the modular structure : Pssm-ID: 238060 Cd Length: 35 Bit Score: 59.14 E-value: 1.06e-10
|
||||||||||||||
| YncE | COG3391 | DNA-binding beta-propeller fold protein YncE [General function prediction only]; |
3123-3276 | 1.76e-08 | ||||||||||
DNA-binding beta-propeller fold protein YncE [General function prediction only]; : Pssm-ID: 442618 [Multi-domain] Cd Length: 237 Bit Score: 58.55 E-value: 1.76e-08
|
||||||||||||||
| FN3 super family | cl27307 | Fibronectin type 3 domain [General function prediction only]; |
4026-4361 | 1.96e-08 | ||||||||||
Fibronectin type 3 domain [General function prediction only]; The actual alignment was detected with superfamily member COG3401: Pssm-ID: 442628 [Multi-domain] Cd Length: 603 Bit Score: 60.79 E-value: 1.96e-08
|
||||||||||||||
| LDLa | cd00112 | Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central ... |
3724-3758 | 3.97e-06 | ||||||||||
Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central role in mammalian cholesterol metabolism; the receptor protein binds LDL and transports it into cells by endocytosis; 7 successive cysteine-rich repeats of about 40 amino acids are present in the N-terminal of this multidomain membrane protein; other homologous domains occur in related receptors, including the very low-density lipoprotein receptor and the LDL receptor-related protein/alpha 2-macroglobulin receptor, and in proteins which are functionally unrelated, such as the C9 component of complement; the binding of calcium is required for in vitro formation of the native disulfide isomer and is necessary in establishing and maintaining the modular structure : Pssm-ID: 238060 Cd Length: 35 Bit Score: 46.05 E-value: 3.97e-06
|
||||||||||||||
| Spectrin | pfam00435 | Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ... |
1266-1330 | 2.45e-05 | ||||||||||
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in cytoskeletal structure. These include spectrin, alpha-actinin and dystrophin. The sequence repeat used in this family is taken from the structural repeat in reference. The spectrin domain- repeat forms a three helix bundle. The second helix is interrupted by proline in some sequences. The repeats are defined by a characteriztic tryptophan (W) residue at position 17 in helix A and a leucine (L) at 2 residues from the carboxyl end of helix C. Although the domain occurs in multiple repeats along sequences, the domains are actually stable on their own - ie they act, biophysically, like domains rather than repeats that along function when aggregated. : Pssm-ID: 395348 [Multi-domain] Cd Length: 105 Bit Score: 46.16 E-value: 2.45e-05
|
||||||||||||||
| LY | smart00135 | Low-density lipoprotein-receptor YWTD domain; Type "B" repeats in low-density lipoprotein (LDL) ... |
3103-3141 | 3.30e-03 | ||||||||||
Low-density lipoprotein-receptor YWTD domain; Type "B" repeats in low-density lipoprotein (LDL) receptor that plays a central role in mammalian cholesterol metabolism. Also present in a variety of molecules similar to gp300/megalin. : Pssm-ID: 214531 [Multi-domain] Cd Length: 43 Bit Score: 37.97 E-value: 3.30e-03
|
||||||||||||||
| Name | Accession | Description | Interval | E-value | |||||||||||||
| VPS10 | smart00602 | VPS10 domain; |
2428-3031 | 1.58e-128 | |||||||||||||
VPS10 domain; Pssm-ID: 214740 [Multi-domain] Cd Length: 612 Bit Score: 419.89 E-value: 1.58e-128
|
|||||||||||||||||
| Sortilin-Vps10 | pfam15902 | Sortilin, neurotensin receptor 3,; Sortilin, also known in mammals as neurotensin receptor-3, ... |
2433-2867 | 4.47e-108 | |||||||||||||
Sortilin, neurotensin receptor 3,; Sortilin, also known in mammals as neurotensin receptor-3, is the archetypical member of a Vps10-domain (Vps10-D) that binds neurotrophic factors and neuropeptides. This domain constitutes the entire luminal part of Sortilin and is activated in the trans-Golgi network by enzymatic propeptide cleavage. The structure of the domain has been determined as a ten-bladed propeller, with up to 9 BNR or beta-hairpin turns in it. The mature receptor binds various ligands, including its own propeptide (Sort-pro), neurotensin, the pro-forms of nerve growth factor-beta (NGF)6 and brain-derived neurotrophic factor (BDNF)7, lipoprotein lipase (LpL), apo lipoprotein AV14 and the receptor-associated protein (RAP)1. Pssm-ID: 464929 [Multi-domain] Cd Length: 444 Bit Score: 354.20 E-value: 4.47e-108
|
|||||||||||||||||
| CH_SPTB-like_rpt1 | cd21246 | first calponin homology (CH) domain found in the beta-I spectrin-like subfamily; The beta-I ... |
36-152 | 2.06e-82 | |||||||||||||
first calponin homology (CH) domain found in the beta-I spectrin-like subfamily; The beta-I spectrin-like family includes beta-I, -II, -III and -IV spectrins. Spectrin is an actin crosslinking and molecular scaffold protein that links the plasma membrane to the actin cytoskeleton, and functions in the determination of cell shape, arrangement of transmembrane proteins, and organization of organelles. It is composed of two antiparallel dimers of alpha- and beta- subunits. Beta-I spectrin, also called spectrin beta chain, erythrocytic (SPTB), may be involved in anaemia pathogenesis. Beta-II spectrin, also called spectrin beta chain, non-erythrocytic 1 (SPTBN1), or fodrin beta chain, is a component of fodrin, which is the general spectrin-like protein that seems to be involved in secretion. Fodrin interacts with calmodulin in a calcium-dependent manner and is thus a candidate for the calcium-dependent movement of the cytoskeleton at the membrane. Beta-III spectrin, also called spectrin beta chain, non-erythrocytic 2 (SPTBN2), or spinocerebellar ataxia 5 protein (SCA5), may play a crucial role as a longer actin-membrane cross-linker or fulfill the need for greater extensible flexibility than can be provided by the other smaller conventional spectrins. Beta-IV spectrin is also called spectrin, non-erythroid beta chain 3 (SPTBN3) or spectrin beta chain, non-erythrocytic 4 (SPTBN4). Its mutation associates with congenital myopathy, neuropathy, and central deafness. Members of this subfamily contain two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs. Pssm-ID: 409095 Cd Length: 117 Bit Score: 266.54 E-value: 2.06e-82
|
|||||||||||||||||
| CH_SPTB_like_rpt2 | cd21248 | second calponin homology (CH) domain found in the beta-I spectrin-like subfamily; The beta-I ... |
169-273 | 2.12e-78 | |||||||||||||
second calponin homology (CH) domain found in the beta-I spectrin-like subfamily; The beta-I spectrin-like family includes beta-I, -II, -III and -IV spectrins. Spectrin is an actin crosslinking and molecular scaffold protein that links the plasma membrane to the actin cytoskeleton, and functions in the determination of cell shape, arrangement of transmembrane proteins, and organization of organelles. It is composed of two antiparallel dimers of alpha- and beta- subunits. Beta-I spectrin, also called spectrin beta chain, erythrocytic (SPTB), may be involved in anaemia pathogenesis. Beta-II spectrin, also called spectrin beta chain, non-erythrocytic 1 (SPTBN1), or fodrin beta chain, is a component of fodrin, which is the general spectrin-like protein that seems to be involved in secretion. Fodrin interacts with calmodulin in a calcium-dependent manner and is thus a candidate for the calcium-dependent movement of the cytoskeleton at the membrane. Beta-III spectrin, also called spectrin beta chain, non-erythrocytic 2 (SPTBN2), or spinocerebellar ataxia 5 protein (SCA5), may play a crucial role as a longer actin-membrane cross-linker or fulfill the need for greater extensible flexibility than can be provided by the other smaller conventional spectrins. Beta-IV spectrin is also called spectrin, non-erythroid beta chain 3 (SPTBN3) or spectrin beta chain, non-erythrocytic 4 (SPTBN4). Its mutation associates with congenital myopathy, neuropathy, and central deafness. Members of this subfamily contain two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs. Pssm-ID: 409097 Cd Length: 105 Bit Score: 254.63 E-value: 2.12e-78
|
|||||||||||||||||
| SAC6 | COG5069 | Ca2+-binding actin-bundling protein fimbrin/plastin (EF-Hand superfamily) [Cytoskeleton]; |
44-450 | 6.75e-64 | |||||||||||||
Ca2+-binding actin-bundling protein fimbrin/plastin (EF-Hand superfamily) [Cytoskeleton]; Pssm-ID: 227401 [Multi-domain] Cd Length: 612 Bit Score: 231.75 E-value: 6.75e-64
|
|||||||||||||||||
| SPEC | cd00176 | Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
638-845 | 9.08e-50 | |||||||||||||
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here Pssm-ID: 238103 [Multi-domain] Cd Length: 213 Bit Score: 177.25 E-value: 9.08e-50
|
|||||||||||||||||
| SPEC | cd00176 | Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
525-740 | 2.07e-48 | |||||||||||||
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here Pssm-ID: 238103 [Multi-domain] Cd Length: 213 Bit Score: 173.40 E-value: 2.07e-48
|
|||||||||||||||||
| SPEC | cd00176 | Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
1546-1758 | 2.83e-48 | |||||||||||||
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here Pssm-ID: 238103 [Multi-domain] Cd Length: 213 Bit Score: 173.02 E-value: 2.83e-48
|
|||||||||||||||||
| SPEC | cd00176 | Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
1440-1651 | 9.87e-47 | |||||||||||||
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here Pssm-ID: 238103 [Multi-domain] Cd Length: 213 Bit Score: 168.39 E-value: 9.87e-47
|
|||||||||||||||||
| SPEC | cd00176 | Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
1759-1967 | 4.30e-45 | |||||||||||||
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here Pssm-ID: 238103 [Multi-domain] Cd Length: 213 Bit Score: 163.77 E-value: 4.30e-45
|
|||||||||||||||||
| PH_beta_spectrin | cd10571 | Beta-spectrin pleckstrin homology (PH) domain; Beta spectrin binds actin and functions as a ... |
2195-2290 | 6.86e-45 | |||||||||||||
Beta-spectrin pleckstrin homology (PH) domain; Beta spectrin binds actin and functions as a major component of the cytoskeleton underlying cellular membranes. Beta spectrin consists of multiple spectrin repeats followed by a PH domain, which binds to inositol-1,4,5-trisphosphate. The PH domain of beta-spectrin is thought to play a role in the association of spectrin with the plasma membrane of cells. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes. Pssm-ID: 269975 Cd Length: 106 Bit Score: 158.93 E-value: 6.86e-45
|
|||||||||||||||||
| SPEC | cd00176 | Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
954-1167 | 1.15e-44 | |||||||||||||
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here Pssm-ID: 238103 [Multi-domain] Cd Length: 213 Bit Score: 162.62 E-value: 1.15e-44
|
|||||||||||||||||
| SPEC | cd00176 | Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
1338-1543 | 4.28e-44 | |||||||||||||
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here Pssm-ID: 238103 [Multi-domain] Cd Length: 213 Bit Score: 161.07 E-value: 4.28e-44
|
|||||||||||||||||
| SPEC | cd00176 | Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
847-1057 | 8.32e-42 | |||||||||||||
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here Pssm-ID: 238103 [Multi-domain] Cd Length: 213 Bit Score: 154.53 E-value: 8.32e-42
|
|||||||||||||||||
| SPEC | cd00176 | Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
1169-1436 | 4.11e-33 | |||||||||||||
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here Pssm-ID: 238103 [Multi-domain] Cd Length: 213 Bit Score: 129.49 E-value: 4.11e-33
|
|||||||||||||||||
| CH | pfam00307 | Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal ... |
169-275 | 6.58e-31 | |||||||||||||
Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal transduction proteins. The CH domain is involved in actin binding in some members of the family. However in calponins there is evidence that the CH domain is not involved in its actin binding activity. Most member proteins have from two to four copies of the CH domain, however some proteins such as calponin have only a single copy. Pssm-ID: 425596 [Multi-domain] Cd Length: 109 Bit Score: 119.31 E-value: 6.58e-31
|
|||||||||||||||||
| Spectrin | pfam00435 | Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ... |
634-738 | 6.89e-30 | |||||||||||||
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in cytoskeletal structure. These include spectrin, alpha-actinin and dystrophin. The sequence repeat used in this family is taken from the structural repeat in reference. The spectrin domain- repeat forms a three helix bundle. The second helix is interrupted by proline in some sequences. The repeats are defined by a characteriztic tryptophan (W) residue at position 17 in helix A and a leucine (L) at 2 residues from the carboxyl end of helix C. Although the domain occurs in multiple repeats along sequences, the domains are actually stable on their own - ie they act, biophysically, like domains rather than repeats that along function when aggregated. Pssm-ID: 395348 [Multi-domain] Cd Length: 105 Bit Score: 116.26 E-value: 6.89e-30
|
|||||||||||||||||
| SPEC | smart00150 | Spectrin repeats; |
637-737 | 6.59e-29 | |||||||||||||
Spectrin repeats; Pssm-ID: 197544 [Multi-domain] Cd Length: 101 Bit Score: 113.19 E-value: 6.59e-29
|
|||||||||||||||||
| SPEC | smart00150 | Spectrin repeats; |
1548-1648 | 3.12e-25 | |||||||||||||
Spectrin repeats; Pssm-ID: 197544 [Multi-domain] Cd Length: 101 Bit Score: 102.79 E-value: 3.12e-25
|
|||||||||||||||||
| SPEC | smart00150 | Spectrin repeats; |
1443-1541 | 5.59e-24 | |||||||||||||
Spectrin repeats; Pssm-ID: 197544 [Multi-domain] Cd Length: 101 Bit Score: 98.94 E-value: 5.59e-24
|
|||||||||||||||||
| Spectrin | pfam00435 | Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ... |
1545-1649 | 1.32e-23 | |||||||||||||
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in cytoskeletal structure. These include spectrin, alpha-actinin and dystrophin. The sequence repeat used in this family is taken from the structural repeat in reference. The spectrin domain- repeat forms a three helix bundle. The second helix is interrupted by proline in some sequences. The repeats are defined by a characteriztic tryptophan (W) residue at position 17 in helix A and a leucine (L) at 2 residues from the carboxyl end of helix C. Although the domain occurs in multiple repeats along sequences, the domains are actually stable on their own - ie they act, biophysically, like domains rather than repeats that along function when aggregated. Pssm-ID: 395348 [Multi-domain] Cd Length: 105 Bit Score: 98.16 E-value: 1.32e-23
|
|||||||||||||||||
| Spectrin | pfam00435 | Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ... |
1439-1543 | 5.71e-23 | |||||||||||||
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in cytoskeletal structure. These include spectrin, alpha-actinin and dystrophin. The sequence repeat used in this family is taken from the structural repeat in reference. The spectrin domain- repeat forms a three helix bundle. The second helix is interrupted by proline in some sequences. The repeats are defined by a characteriztic tryptophan (W) residue at position 17 in helix A and a leucine (L) at 2 residues from the carboxyl end of helix C. Although the domain occurs in multiple repeats along sequences, the domains are actually stable on their own - ie they act, biophysically, like domains rather than repeats that along function when aggregated. Pssm-ID: 395348 [Multi-domain] Cd Length: 105 Bit Score: 96.23 E-value: 5.71e-23
|
|||||||||||||||||
| CH | smart00033 | Calponin homology domain; Actin binding domains present in duplicate at the N-termini of ... |
173-267 | 3.06e-22 | |||||||||||||
Calponin homology domain; Actin binding domains present in duplicate at the N-termini of spectrin-like proteins (including dystrophin, alpha-actinin). These domains cross-link actin filaments into bundles and networks. A calponin homology domain is predicted in yeasst Cdc24p. Pssm-ID: 214479 [Multi-domain] Cd Length: 101 Bit Score: 93.92 E-value: 3.06e-22
|
|||||||||||||||||
| SPEC | smart00150 | Spectrin repeats; |
848-948 | 1.30e-21 | |||||||||||||
Spectrin repeats; Pssm-ID: 197544 [Multi-domain] Cd Length: 101 Bit Score: 92.39 E-value: 1.30e-21
|
|||||||||||||||||
| CH | pfam00307 | Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal ... |
50-155 | 7.69e-21 | |||||||||||||
Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal transduction proteins. The CH domain is involved in actin binding in some members of the family. However in calponins there is evidence that the CH domain is not involved in its actin binding activity. Most member proteins have from two to four copies of the CH domain, however some proteins such as calponin have only a single copy. Pssm-ID: 425596 [Multi-domain] Cd Length: 109 Bit Score: 90.42 E-value: 7.69e-21
|
|||||||||||||||||
| SPEC | smart00150 | Spectrin repeats; |
1868-1967 | 1.13e-20 | |||||||||||||
Spectrin repeats; Pssm-ID: 197544 [Multi-domain] Cd Length: 101 Bit Score: 89.70 E-value: 1.13e-20
|
|||||||||||||||||
| Spectrin | pfam00435 | Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ... |
1865-1967 | 2.81e-20 | |||||||||||||
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in cytoskeletal structure. These include spectrin, alpha-actinin and dystrophin. The sequence repeat used in this family is taken from the structural repeat in reference. The spectrin domain- repeat forms a three helix bundle. The second helix is interrupted by proline in some sequences. The repeats are defined by a characteriztic tryptophan (W) residue at position 17 in helix A and a leucine (L) at 2 residues from the carboxyl end of helix C. Although the domain occurs in multiple repeats along sequences, the domains are actually stable on their own - ie they act, biophysically, like domains rather than repeats that along function when aggregated. Pssm-ID: 395348 [Multi-domain] Cd Length: 105 Bit Score: 88.53 E-value: 2.81e-20
|
|||||||||||||||||
| SPEC | smart00150 | Spectrin repeats; |
422-521 | 3.99e-20 | |||||||||||||
Spectrin repeats; Pssm-ID: 197544 [Multi-domain] Cd Length: 101 Bit Score: 88.16 E-value: 3.99e-20
|
|||||||||||||||||
| Spectrin | pfam00435 | Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ... |
422-521 | 8.78e-20 | |||||||||||||
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in cytoskeletal structure. These include spectrin, alpha-actinin and dystrophin. The sequence repeat used in this family is taken from the structural repeat in reference. The spectrin domain- repeat forms a three helix bundle. The second helix is interrupted by proline in some sequences. The repeats are defined by a characteriztic tryptophan (W) residue at position 17 in helix A and a leucine (L) at 2 residues from the carboxyl end of helix C. Although the domain occurs in multiple repeats along sequences, the domains are actually stable on their own - ie they act, biophysically, like domains rather than repeats that along function when aggregated. Pssm-ID: 395348 [Multi-domain] Cd Length: 105 Bit Score: 87.37 E-value: 8.78e-20
|
|||||||||||||||||
| Spectrin | pfam00435 | Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ... |
847-947 | 1.67e-19 | |||||||||||||
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in cytoskeletal structure. These include spectrin, alpha-actinin and dystrophin. The sequence repeat used in this family is taken from the structural repeat in reference. The spectrin domain- repeat forms a three helix bundle. The second helix is interrupted by proline in some sequences. The repeats are defined by a characteriztic tryptophan (W) residue at position 17 in helix A and a leucine (L) at 2 residues from the carboxyl end of helix C. Although the domain occurs in multiple repeats along sequences, the domains are actually stable on their own - ie they act, biophysically, like domains rather than repeats that along function when aggregated. Pssm-ID: 395348 [Multi-domain] Cd Length: 105 Bit Score: 86.60 E-value: 1.67e-19
|
|||||||||||||||||
| SPEC | smart00150 | Spectrin repeats; |
954-1055 | 3.05e-19 | |||||||||||||
Spectrin repeats; Pssm-ID: 197544 [Multi-domain] Cd Length: 101 Bit Score: 85.46 E-value: 3.05e-19
|
|||||||||||||||||
| CH | smart00033 | Calponin homology domain; Actin binding domains present in duplicate at the N-termini of ... |
54-152 | 7.10e-19 | |||||||||||||
Calponin homology domain; Actin binding domains present in duplicate at the N-termini of spectrin-like proteins (including dystrophin, alpha-actinin). These domains cross-link actin filaments into bundles and networks. A calponin homology domain is predicted in yeasst Cdc24p. Pssm-ID: 214479 [Multi-domain] Cd Length: 101 Bit Score: 84.67 E-value: 7.10e-19
|
|||||||||||||||||
| SPEC | smart00150 | Spectrin repeats; |
527-631 | 2.97e-18 | |||||||||||||
Spectrin repeats; Pssm-ID: 197544 [Multi-domain] Cd Length: 101 Bit Score: 82.76 E-value: 2.97e-18
|
|||||||||||||||||
| SPEC | smart00150 | Spectrin repeats; |
1172-1270 | 4.87e-18 | |||||||||||||
Spectrin repeats; Pssm-ID: 197544 [Multi-domain] Cd Length: 101 Bit Score: 81.99 E-value: 4.87e-18
|
|||||||||||||||||
| SPEC | cd00176 | Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
301-524 | 6.61e-18 | |||||||||||||
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here Pssm-ID: 238103 [Multi-domain] Cd Length: 213 Bit Score: 85.58 E-value: 6.61e-18
|
|||||||||||||||||
| Spectrin | pfam00435 | Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ... |
954-1056 | 1.52e-17 | |||||||||||||
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in cytoskeletal structure. These include spectrin, alpha-actinin and dystrophin. The sequence repeat used in this family is taken from the structural repeat in reference. The spectrin domain- repeat forms a three helix bundle. The second helix is interrupted by proline in some sequences. The repeats are defined by a characteriztic tryptophan (W) residue at position 17 in helix A and a leucine (L) at 2 residues from the carboxyl end of helix C. Although the domain occurs in multiple repeats along sequences, the domains are actually stable on their own - ie they act, biophysically, like domains rather than repeats that along function when aggregated. Pssm-ID: 395348 [Multi-domain] Cd Length: 105 Bit Score: 80.83 E-value: 1.52e-17
|
|||||||||||||||||
| Spectrin | pfam00435 | Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ... |
524-632 | 7.19e-17 | |||||||||||||
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in cytoskeletal structure. These include spectrin, alpha-actinin and dystrophin. The sequence repeat used in this family is taken from the structural repeat in reference. The spectrin domain- repeat forms a three helix bundle. The second helix is interrupted by proline in some sequences. The repeats are defined by a characteriztic tryptophan (W) residue at position 17 in helix A and a leucine (L) at 2 residues from the carboxyl end of helix C. Although the domain occurs in multiple repeats along sequences, the domains are actually stable on their own - ie they act, biophysically, like domains rather than repeats that along function when aggregated. Pssm-ID: 395348 [Multi-domain] Cd Length: 105 Bit Score: 78.90 E-value: 7.19e-17
|
|||||||||||||||||
| SMC_prok_B | TIGR02168 | chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
709-1614 | 2.32e-16 | |||||||||||||
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins] Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 87.03 E-value: 2.32e-16
|
|||||||||||||||||
| LDLa | cd00112 | Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central ... |
3441-3475 | 2.75e-16 | |||||||||||||
Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central role in mammalian cholesterol metabolism; the receptor protein binds LDL and transports it into cells by endocytosis; 7 successive cysteine-rich repeats of about 40 amino acids are present in the N-terminal of this multidomain membrane protein; other homologous domains occur in related receptors, including the very low-density lipoprotein receptor and the LDL receptor-related protein/alpha 2-macroglobulin receptor, and in proteins which are functionally unrelated, such as the C9 component of complement; the binding of calcium is required for in vitro formation of the native disulfide isomer and is necessary in establishing and maintaining the modular structure Pssm-ID: 238060 Cd Length: 35 Bit Score: 74.94 E-value: 2.75e-16
|
|||||||||||||||||
| LDLa | cd00112 | Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central ... |
3363-3397 | 6.06e-16 | |||||||||||||
Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central role in mammalian cholesterol metabolism; the receptor protein binds LDL and transports it into cells by endocytosis; 7 successive cysteine-rich repeats of about 40 amino acids are present in the N-terminal of this multidomain membrane protein; other homologous domains occur in related receptors, including the very low-density lipoprotein receptor and the LDL receptor-related protein/alpha 2-macroglobulin receptor, and in proteins which are functionally unrelated, such as the C9 component of complement; the binding of calcium is required for in vitro formation of the native disulfide isomer and is necessary in establishing and maintaining the modular structure Pssm-ID: 238060 Cd Length: 35 Bit Score: 73.78 E-value: 6.06e-16
|
|||||||||||||||||
| LDLa | smart00192 | Low-density lipoprotein receptor domain class A; Cysteine-rich repeat in the low-density ... |
3440-3472 | 1.27e-14 | |||||||||||||
Low-density lipoprotein receptor domain class A; Cysteine-rich repeat in the low-density lipoprotein (LDL) receptor that plays a central role in mammalian cholesterol metabolism. The N-terminal type A repeats in LDL receptor bind the lipoproteins. Other homologous domains occur in related receptors, including the very low-density lipoprotein receptor and the LDL receptor-related protein/alpha 2-macroglobulin receptor, and in proteins which are functionally unrelated, such as the C9 component of complement. Mutations in the LDL receptor gene cause familial hypercholesterolemia. Pssm-ID: 197566 Cd Length: 33 Bit Score: 69.97 E-value: 1.27e-14
|
|||||||||||||||||
| LDLa | smart00192 | Low-density lipoprotein receptor domain class A; Cysteine-rich repeat in the low-density ... |
3362-3394 | 1.79e-14 | |||||||||||||
Low-density lipoprotein receptor domain class A; Cysteine-rich repeat in the low-density lipoprotein (LDL) receptor that plays a central role in mammalian cholesterol metabolism. The N-terminal type A repeats in LDL receptor bind the lipoproteins. Other homologous domains occur in related receptors, including the very low-density lipoprotein receptor and the LDL receptor-related protein/alpha 2-macroglobulin receptor, and in proteins which are functionally unrelated, such as the C9 component of complement. Mutations in the LDL receptor gene cause familial hypercholesterolemia. Pssm-ID: 197566 Cd Length: 33 Bit Score: 69.58 E-value: 1.79e-14
|
|||||||||||||||||
| LDLa | cd00112 | Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central ... |
3484-3518 | 3.40e-14 | |||||||||||||
Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central role in mammalian cholesterol metabolism; the receptor protein binds LDL and transports it into cells by endocytosis; 7 successive cysteine-rich repeats of about 40 amino acids are present in the N-terminal of this multidomain membrane protein; other homologous domains occur in related receptors, including the very low-density lipoprotein receptor and the LDL receptor-related protein/alpha 2-macroglobulin receptor, and in proteins which are functionally unrelated, such as the C9 component of complement; the binding of calcium is required for in vitro formation of the native disulfide isomer and is necessary in establishing and maintaining the modular structure Pssm-ID: 238060 Cd Length: 35 Bit Score: 69.16 E-value: 3.40e-14
|
|||||||||||||||||
| Ldl_recept_a | pfam00057 | Low-density lipoprotein receptor domain class A; |
3483-3518 | 4.17e-14 | |||||||||||||
Low-density lipoprotein receptor domain class A; Pssm-ID: 395011 Cd Length: 37 Bit Score: 68.81 E-value: 4.17e-14
|
|||||||||||||||||
| Ldl_recept_a | pfam00057 | Low-density lipoprotein receptor domain class A; |
3361-3397 | 7.95e-14 | |||||||||||||
Low-density lipoprotein receptor domain class A; Pssm-ID: 395011 Cd Length: 37 Bit Score: 68.04 E-value: 7.95e-14
|
|||||||||||||||||
| FN3 | COG3401 | Fibronectin type 3 domain [General function prediction only]; |
3766-4135 | 1.20e-13 | |||||||||||||
Fibronectin type 3 domain [General function prediction only]; Pssm-ID: 442628 [Multi-domain] Cd Length: 603 Bit Score: 77.35 E-value: 1.20e-13
|
|||||||||||||||||
| Ldl_recept_a | pfam00057 | Low-density lipoprotein receptor domain class A; |
3440-3475 | 1.46e-13 | |||||||||||||
Low-density lipoprotein receptor domain class A; Pssm-ID: 395011 Cd Length: 37 Bit Score: 67.27 E-value: 1.46e-13
|
|||||||||||||||||
| Spectrin | pfam00435 | Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ... |
1970-2029 | 3.14e-13 | |||||||||||||
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in cytoskeletal structure. These include spectrin, alpha-actinin and dystrophin. The sequence repeat used in this family is taken from the structural repeat in reference. The spectrin domain- repeat forms a three helix bundle. The second helix is interrupted by proline in some sequences. The repeats are defined by a characteriztic tryptophan (W) residue at position 17 in helix A and a leucine (L) at 2 residues from the carboxyl end of helix C. Although the domain occurs in multiple repeats along sequences, the domains are actually stable on their own - ie they act, biophysically, like domains rather than repeats that along function when aggregated. Pssm-ID: 395348 [Multi-domain] Cd Length: 105 Bit Score: 68.50 E-value: 3.14e-13
|
|||||||||||||||||
| LDLa | smart00192 | Low-density lipoprotein receptor domain class A; Cysteine-rich repeat in the low-density ... |
3483-3515 | 3.25e-13 | |||||||||||||
Low-density lipoprotein receptor domain class A; Cysteine-rich repeat in the low-density lipoprotein (LDL) receptor that plays a central role in mammalian cholesterol metabolism. The N-terminal type A repeats in LDL receptor bind the lipoproteins. Other homologous domains occur in related receptors, including the very low-density lipoprotein receptor and the LDL receptor-related protein/alpha 2-macroglobulin receptor, and in proteins which are functionally unrelated, such as the C9 component of complement. Mutations in the LDL receptor gene cause familial hypercholesterolemia. Pssm-ID: 197566 Cd Length: 33 Bit Score: 66.12 E-value: 3.25e-13
|
|||||||||||||||||
| LDLa | cd00112 | Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central ... |
3633-3667 | 4.26e-13 | |||||||||||||
Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central role in mammalian cholesterol metabolism; the receptor protein binds LDL and transports it into cells by endocytosis; 7 successive cysteine-rich repeats of about 40 amino acids are present in the N-terminal of this multidomain membrane protein; other homologous domains occur in related receptors, including the very low-density lipoprotein receptor and the LDL receptor-related protein/alpha 2-macroglobulin receptor, and in proteins which are functionally unrelated, such as the C9 component of complement; the binding of calcium is required for in vitro formation of the native disulfide isomer and is necessary in establishing and maintaining the modular structure Pssm-ID: 238060 Cd Length: 35 Bit Score: 65.69 E-value: 4.26e-13
|
|||||||||||||||||
| Ldl_recept_a | pfam00057 | Low-density lipoprotein receptor domain class A; |
3633-3667 | 4.74e-13 | |||||||||||||
Low-density lipoprotein receptor domain class A; Pssm-ID: 395011 Cd Length: 37 Bit Score: 65.73 E-value: 4.74e-13
|
|||||||||||||||||
| SPEC | smart00150 | Spectrin repeats; |
1973-2032 | 7.74e-13 | |||||||||||||
Spectrin repeats; Pssm-ID: 197544 [Multi-domain] Cd Length: 101 Bit Score: 67.35 E-value: 7.74e-13
|
|||||||||||||||||
| PH_9 | pfam15410 | Pleckstrin homology domain; This Pleckstrin homology domain is found in some fungal species. |
2196-2291 | 2.54e-12 | |||||||||||||
Pleckstrin homology domain; This Pleckstrin homology domain is found in some fungal species. Pssm-ID: 434701 Cd Length: 118 Bit Score: 66.30 E-value: 2.54e-12
|
|||||||||||||||||
| LDLa | cd00112 | Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central ... |
3523-3561 | 7.44e-12 | |||||||||||||
Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central role in mammalian cholesterol metabolism; the receptor protein binds LDL and transports it into cells by endocytosis; 7 successive cysteine-rich repeats of about 40 amino acids are present in the N-terminal of this multidomain membrane protein; other homologous domains occur in related receptors, including the very low-density lipoprotein receptor and the LDL receptor-related protein/alpha 2-macroglobulin receptor, and in proteins which are functionally unrelated, such as the C9 component of complement; the binding of calcium is required for in vitro formation of the native disulfide isomer and is necessary in establishing and maintaining the modular structure Pssm-ID: 238060 Cd Length: 35 Bit Score: 62.22 E-value: 7.44e-12
|
|||||||||||||||||
| LDLa | smart00192 | Low-density lipoprotein receptor domain class A; Cysteine-rich repeat in the low-density ... |
3633-3664 | 7.46e-12 | |||||||||||||
Low-density lipoprotein receptor domain class A; Cysteine-rich repeat in the low-density lipoprotein (LDL) receptor that plays a central role in mammalian cholesterol metabolism. The N-terminal type A repeats in LDL receptor bind the lipoproteins. Other homologous domains occur in related receptors, including the very low-density lipoprotein receptor and the LDL receptor-related protein/alpha 2-macroglobulin receptor, and in proteins which are functionally unrelated, such as the C9 component of complement. Mutations in the LDL receptor gene cause familial hypercholesterolemia. Pssm-ID: 197566 Cd Length: 33 Bit Score: 62.27 E-value: 7.46e-12
|
|||||||||||||||||
| Spectrin | pfam00435 | Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ... |
1167-1271 | 7.49e-12 | |||||||||||||
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in cytoskeletal structure. These include spectrin, alpha-actinin and dystrophin. The sequence repeat used in this family is taken from the structural repeat in reference. The spectrin domain- repeat forms a three helix bundle. The second helix is interrupted by proline in some sequences. The repeats are defined by a characteriztic tryptophan (W) residue at position 17 in helix A and a leucine (L) at 2 residues from the carboxyl end of helix C. Although the domain occurs in multiple repeats along sequences, the domains are actually stable on their own - ie they act, biophysically, like domains rather than repeats that along function when aggregated. Pssm-ID: 395348 [Multi-domain] Cd Length: 105 Bit Score: 64.65 E-value: 7.49e-12
|
|||||||||||||||||
| LDLa | cd00112 | Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central ... |
3403-3436 | 9.97e-12 | |||||||||||||
Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central role in mammalian cholesterol metabolism; the receptor protein binds LDL and transports it into cells by endocytosis; 7 successive cysteine-rich repeats of about 40 amino acids are present in the N-terminal of this multidomain membrane protein; other homologous domains occur in related receptors, including the very low-density lipoprotein receptor and the LDL receptor-related protein/alpha 2-macroglobulin receptor, and in proteins which are functionally unrelated, such as the C9 component of complement; the binding of calcium is required for in vitro formation of the native disulfide isomer and is necessary in establishing and maintaining the modular structure Pssm-ID: 238060 Cd Length: 35 Bit Score: 61.84 E-value: 9.97e-12
|
|||||||||||||||||
| fn3 | pfam00041 | Fibronectin type III domain; |
3866-3946 | 1.18e-11 | |||||||||||||
Fibronectin type III domain; Pssm-ID: 394996 [Multi-domain] Cd Length: 85 Bit Score: 63.59 E-value: 1.18e-11
|
|||||||||||||||||
| Spectrin | pfam00435 | Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ... |
298-408 | 2.60e-11 | |||||||||||||
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in cytoskeletal structure. These include spectrin, alpha-actinin and dystrophin. The sequence repeat used in this family is taken from the structural repeat in reference. The spectrin domain- repeat forms a three helix bundle. The second helix is interrupted by proline in some sequences. The repeats are defined by a characteriztic tryptophan (W) residue at position 17 in helix A and a leucine (L) at 2 residues from the carboxyl end of helix C. Although the domain occurs in multiple repeats along sequences, the domains are actually stable on their own - ie they act, biophysically, like domains rather than repeats that along function when aggregated. Pssm-ID: 395348 [Multi-domain] Cd Length: 105 Bit Score: 63.11 E-value: 2.60e-11
|
|||||||||||||||||
| LDLa | cd00112 | Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central ... |
3675-3710 | 4.36e-11 | |||||||||||||
Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central role in mammalian cholesterol metabolism; the receptor protein binds LDL and transports it into cells by endocytosis; 7 successive cysteine-rich repeats of about 40 amino acids are present in the N-terminal of this multidomain membrane protein; other homologous domains occur in related receptors, including the very low-density lipoprotein receptor and the LDL receptor-related protein/alpha 2-macroglobulin receptor, and in proteins which are functionally unrelated, such as the C9 component of complement; the binding of calcium is required for in vitro formation of the native disulfide isomer and is necessary in establishing and maintaining the modular structure Pssm-ID: 238060 Cd Length: 35 Bit Score: 60.30 E-value: 4.36e-11
|
|||||||||||||||||
| Ldl_recept_a | pfam00057 | Low-density lipoprotein receptor domain class A; |
3401-3436 | 5.57e-11 | |||||||||||||
Low-density lipoprotein receptor domain class A; Pssm-ID: 395011 Cd Length: 37 Bit Score: 59.95 E-value: 5.57e-11
|
|||||||||||||||||
| LDLa | cd00112 | Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central ... |
3579-3613 | 1.06e-10 | |||||||||||||
Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central role in mammalian cholesterol metabolism; the receptor protein binds LDL and transports it into cells by endocytosis; 7 successive cysteine-rich repeats of about 40 amino acids are present in the N-terminal of this multidomain membrane protein; other homologous domains occur in related receptors, including the very low-density lipoprotein receptor and the LDL receptor-related protein/alpha 2-macroglobulin receptor, and in proteins which are functionally unrelated, such as the C9 component of complement; the binding of calcium is required for in vitro formation of the native disulfide isomer and is necessary in establishing and maintaining the modular structure Pssm-ID: 238060 Cd Length: 35 Bit Score: 59.14 E-value: 1.06e-10
|
|||||||||||||||||
| LDLa | smart00192 | Low-density lipoprotein receptor domain class A; Cysteine-rich repeat in the low-density ... |
3523-3558 | 2.82e-10 | |||||||||||||
Low-density lipoprotein receptor domain class A; Cysteine-rich repeat in the low-density lipoprotein (LDL) receptor that plays a central role in mammalian cholesterol metabolism. The N-terminal type A repeats in LDL receptor bind the lipoproteins. Other homologous domains occur in related receptors, including the very low-density lipoprotein receptor and the LDL receptor-related protein/alpha 2-macroglobulin receptor, and in proteins which are functionally unrelated, such as the C9 component of complement. Mutations in the LDL receptor gene cause familial hypercholesterolemia. Pssm-ID: 197566 Cd Length: 33 Bit Score: 57.64 E-value: 2.82e-10
|
|||||||||||||||||
| FN3 | cd00063 | Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ... |
3865-3952 | 3.04e-10 | |||||||||||||
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases. Pssm-ID: 238020 [Multi-domain] Cd Length: 93 Bit Score: 59.82 E-value: 3.04e-10
|
|||||||||||||||||
| LDLa | smart00192 | Low-density lipoprotein receptor domain class A; Cysteine-rich repeat in the low-density ... |
3402-3433 | 4.21e-10 | |||||||||||||
Low-density lipoprotein receptor domain class A; Cysteine-rich repeat in the low-density lipoprotein (LDL) receptor that plays a central role in mammalian cholesterol metabolism. The N-terminal type A repeats in LDL receptor bind the lipoproteins. Other homologous domains occur in related receptors, including the very low-density lipoprotein receptor and the LDL receptor-related protein/alpha 2-macroglobulin receptor, and in proteins which are functionally unrelated, such as the C9 component of complement. Mutations in the LDL receptor gene cause familial hypercholesterolemia. Pssm-ID: 197566 Cd Length: 33 Bit Score: 57.26 E-value: 4.21e-10
|
|||||||||||||||||
| Ldl_recept_a | pfam00057 | Low-density lipoprotein receptor domain class A; |
3523-3561 | 5.12e-10 | |||||||||||||
Low-density lipoprotein receptor domain class A; Pssm-ID: 395011 Cd Length: 37 Bit Score: 57.26 E-value: 5.12e-10
|
|||||||||||||||||
| LDLa | smart00192 | Low-density lipoprotein receptor domain class A; Cysteine-rich repeat in the low-density ... |
3579-3610 | 8.95e-10 | |||||||||||||
Low-density lipoprotein receptor domain class A; Cysteine-rich repeat in the low-density lipoprotein (LDL) receptor that plays a central role in mammalian cholesterol metabolism. The N-terminal type A repeats in LDL receptor bind the lipoproteins. Other homologous domains occur in related receptors, including the very low-density lipoprotein receptor and the LDL receptor-related protein/alpha 2-macroglobulin receptor, and in proteins which are functionally unrelated, such as the C9 component of complement. Mutations in the LDL receptor gene cause familial hypercholesterolemia. Pssm-ID: 197566 Cd Length: 33 Bit Score: 56.49 E-value: 8.95e-10
|
|||||||||||||||||
| PH | smart00233 | Pleckstrin homology domain; Domain commonly found in eukaryotic signalling proteins. The ... |
2196-2292 | 1.34e-09 | |||||||||||||
Pleckstrin homology domain; Domain commonly found in eukaryotic signalling proteins. The domain family possesses multiple functions including the abilities to bind inositol phosphates, and various proteins. PH domains have been found to possess inserted domains (such as in PLC gamma, syntrophins) and to be inserted within other domains. Mutations in Brutons tyrosine kinase (Btk) within its PH domain cause X-linked agammaglobulinaemia (XLA) in patients. Point mutations cluster into the positively charged end of the molecule around the predicted binding site for phosphatidylinositol lipids. Pssm-ID: 214574 [Multi-domain] Cd Length: 102 Bit Score: 58.33 E-value: 1.34e-09
|
|||||||||||||||||
| LDLa | smart00192 | Low-density lipoprotein receptor domain class A; Cysteine-rich repeat in the low-density ... |
3675-3707 | 1.81e-09 | |||||||||||||
Low-density lipoprotein receptor domain class A; Cysteine-rich repeat in the low-density lipoprotein (LDL) receptor that plays a central role in mammalian cholesterol metabolism. The N-terminal type A repeats in LDL receptor bind the lipoproteins. Other homologous domains occur in related receptors, including the very low-density lipoprotein receptor and the LDL receptor-related protein/alpha 2-macroglobulin receptor, and in proteins which are functionally unrelated, such as the C9 component of complement. Mutations in the LDL receptor gene cause familial hypercholesterolemia. Pssm-ID: 197566 Cd Length: 33 Bit Score: 55.72 E-value: 1.81e-09
|
|||||||||||||||||
| Ldl_recept_a | pfam00057 | Low-density lipoprotein receptor domain class A; |
3673-3710 | 2.95e-09 | |||||||||||||
Low-density lipoprotein receptor domain class A; Pssm-ID: 395011 Cd Length: 37 Bit Score: 54.95 E-value: 2.95e-09
|
|||||||||||||||||
| YncE | COG3391 | DNA-binding beta-propeller fold protein YncE [General function prediction only]; |
3123-3276 | 1.76e-08 | |||||||||||||
DNA-binding beta-propeller fold protein YncE [General function prediction only]; Pssm-ID: 442618 [Multi-domain] Cd Length: 237 Bit Score: 58.55 E-value: 1.76e-08
|
|||||||||||||||||
| FN3 | COG3401 | Fibronectin type 3 domain [General function prediction only]; |
4026-4361 | 1.96e-08 | |||||||||||||
Fibronectin type 3 domain [General function prediction only]; Pssm-ID: 442628 [Multi-domain] Cd Length: 603 Bit Score: 60.79 E-value: 1.96e-08
|
|||||||||||||||||
| FN3 | smart00060 | Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ... |
3865-3943 | 3.72e-08 | |||||||||||||
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, fibronectin. The tenth fibronectin type III repeat contains a RGD cell recognition sequence in a flexible loop between 2 strands. Type III modules are present in both extracellular and intracellular proteins. Pssm-ID: 214495 [Multi-domain] Cd Length: 83 Bit Score: 53.39 E-value: 3.72e-08
|
|||||||||||||||||
| Ldl_recept_b | pfam00058 | Low-density lipoprotein receptor repeat class B; This domain is also known as the YWTD motif ... |
3171-3214 | 5.11e-08 | |||||||||||||
Low-density lipoprotein receptor repeat class B; This domain is also known as the YWTD motif after the most conserved region of the repeat. The YWTD repeat is found in multiple tandem repeats and has been predicted to form a beta-propeller structure. Pssm-ID: 459654 Cd Length: 42 Bit Score: 51.78 E-value: 5.11e-08
|
|||||||||||||||||
| LY | smart00135 | Low-density lipoprotein-receptor YWTD domain; Type "B" repeats in low-density lipoprotein (LDL) ... |
3197-3237 | 9.23e-08 | |||||||||||||
Low-density lipoprotein-receptor YWTD domain; Type "B" repeats in low-density lipoprotein (LDL) receptor that plays a central role in mammalian cholesterol metabolism. Also present in a variety of molecules similar to gp300/megalin. Pssm-ID: 214531 [Multi-domain] Cd Length: 43 Bit Score: 51.06 E-value: 9.23e-08
|
|||||||||||||||||
| SMC_prok_A | TIGR02169 | chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1020-1406 | 3.07e-07 | |||||||||||||
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins] Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 57.00 E-value: 3.07e-07
|
|||||||||||||||||
| PTZ00121 | PTZ00121 | MAEBL; Provisional |
1175-1669 | 3.97e-07 | |||||||||||||
MAEBL; Provisional Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 57.07 E-value: 3.97e-07
|
|||||||||||||||||
| PRK02224 | PRK02224 | DNA double-strand break repair Rad50 ATPase; |
990-1451 | 4.06e-07 | |||||||||||||
DNA double-strand break repair Rad50 ATPase; Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 56.59 E-value: 4.06e-07
|
|||||||||||||||||
| GumC | COG3206 | Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
817-1147 | 6.20e-07 | |||||||||||||
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 55.79 E-value: 6.20e-07
|
|||||||||||||||||
| Ldl_recept_a | pfam00057 | Low-density lipoprotein receptor domain class A; |
3584-3613 | 1.52e-06 | |||||||||||||
Low-density lipoprotein receptor domain class A; Pssm-ID: 395011 Cd Length: 37 Bit Score: 47.24 E-value: 1.52e-06
|
|||||||||||||||||
| CwlO1 | COG3883 | Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1239-1464 | 1.73e-06 | |||||||||||||
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown]; Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 53.68 E-value: 1.73e-06
|
|||||||||||||||||
| LDLa | cd00112 | Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central ... |
3724-3758 | 3.97e-06 | |||||||||||||
Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central role in mammalian cholesterol metabolism; the receptor protein binds LDL and transports it into cells by endocytosis; 7 successive cysteine-rich repeats of about 40 amino acids are present in the N-terminal of this multidomain membrane protein; other homologous domains occur in related receptors, including the very low-density lipoprotein receptor and the LDL receptor-related protein/alpha 2-macroglobulin receptor, and in proteins which are functionally unrelated, such as the C9 component of complement; the binding of calcium is required for in vitro formation of the native disulfide isomer and is necessary in establishing and maintaining the modular structure Pssm-ID: 238060 Cd Length: 35 Bit Score: 46.05 E-value: 3.97e-06
|
|||||||||||||||||
| NHL | cd05819 | NHL repeat unit of beta-propeller proteins; The NHL(NCL-1, HT2A and LIN-41)-repeat is found in ... |
3115-3276 | 4.65e-06 | |||||||||||||
NHL repeat unit of beta-propeller proteins; The NHL(NCL-1, HT2A and LIN-41)-repeat is found in multiple tandem copies, typically as 6 instances. It is about 40 residues long and resembles the WD repeat and other beta-propeller structures. The repeats have a catalytic activity in Peptidyl-glycine alpha-amidating monooxygenase; proteolysis has shown that the Peptidyl-alpha-hydroxyglycine alpha-amidating lyase (PAL) activity is localized to the repeats. Tripartite motif-containing protein 32 interacts with the activation domain of Tat. This interaction is mediated by the NHL repeats. Pssm-ID: 271320 [Multi-domain] Cd Length: 269 Bit Score: 51.55 E-value: 4.65e-06
|
|||||||||||||||||
| Spectrin | pfam00435 | Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ... |
1266-1330 | 2.45e-05 | |||||||||||||
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in cytoskeletal structure. These include spectrin, alpha-actinin and dystrophin. The sequence repeat used in this family is taken from the structural repeat in reference. The spectrin domain- repeat forms a three helix bundle. The second helix is interrupted by proline in some sequences. The repeats are defined by a characteriztic tryptophan (W) residue at position 17 in helix A and a leucine (L) at 2 residues from the carboxyl end of helix C. Although the domain occurs in multiple repeats along sequences, the domains are actually stable on their own - ie they act, biophysically, like domains rather than repeats that along function when aggregated. Pssm-ID: 395348 [Multi-domain] Cd Length: 105 Bit Score: 46.16 E-value: 2.45e-05
|
|||||||||||||||||
| LDLa | smart00192 | Low-density lipoprotein receptor domain class A; Cysteine-rich repeat in the low-density ... |
3724-3755 | 5.60e-05 | |||||||||||||
Low-density lipoprotein receptor domain class A; Cysteine-rich repeat in the low-density lipoprotein (LDL) receptor that plays a central role in mammalian cholesterol metabolism. The N-terminal type A repeats in LDL receptor bind the lipoproteins. Other homologous domains occur in related receptors, including the very low-density lipoprotein receptor and the LDL receptor-related protein/alpha 2-macroglobulin receptor, and in proteins which are functionally unrelated, such as the C9 component of complement. Mutations in the LDL receptor gene cause familial hypercholesterolemia. Pssm-ID: 197566 Cd Length: 33 Bit Score: 43.01 E-value: 5.60e-05
|
|||||||||||||||||
| Ldl_recept_a | pfam00057 | Low-density lipoprotein receptor domain class A; |
3729-3758 | 7.45e-04 | |||||||||||||
Low-density lipoprotein receptor domain class A; Pssm-ID: 395011 Cd Length: 37 Bit Score: 39.92 E-value: 7.45e-04
|
|||||||||||||||||
| EnvC | COG4942 | Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
772-1021 | 1.78e-03 | |||||||||||||
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning]; Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 43.98 E-value: 1.78e-03
|
|||||||||||||||||
| GimC | COG1382 | Prefoldin, chaperonin cofactor [Posttranslational modification, protein turnover, chaperones]; |
1266-1399 | 2.75e-03 | |||||||||||||
Prefoldin, chaperonin cofactor [Posttranslational modification, protein turnover, chaperones]; Pssm-ID: 440992 [Multi-domain] Cd Length: 121 Bit Score: 40.64 E-value: 2.75e-03
|
|||||||||||||||||
| LY | smart00135 | Low-density lipoprotein-receptor YWTD domain; Type "B" repeats in low-density lipoprotein (LDL) ... |
3103-3141 | 3.30e-03 | |||||||||||||
Low-density lipoprotein-receptor YWTD domain; Type "B" repeats in low-density lipoprotein (LDL) receptor that plays a central role in mammalian cholesterol metabolism. Also present in a variety of molecules similar to gp300/megalin. Pssm-ID: 214531 [Multi-domain] Cd Length: 43 Bit Score: 37.97 E-value: 3.30e-03
|
|||||||||||||||||
| PTZ00440 | PTZ00440 | reticulocyte binding protein 2-like protein; Provisional |
1205-1541 | 3.39e-03 | |||||||||||||
reticulocyte binding protein 2-like protein; Provisional Pssm-ID: 240419 [Multi-domain] Cd Length: 2722 Bit Score: 44.05 E-value: 3.39e-03
|
|||||||||||||||||
| SAC6 | COG5069 | Ca2+-binding actin-bundling protein fimbrin/plastin (EF-Hand superfamily) [Cytoskeleton]; |
46-194 | 3.46e-03 | |||||||||||||
Ca2+-binding actin-bundling protein fimbrin/plastin (EF-Hand superfamily) [Cytoskeleton]; Pssm-ID: 227401 [Multi-domain] Cd Length: 612 Bit Score: 43.39 E-value: 3.46e-03
|
|||||||||||||||||
| FN3 | smart00060 | Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ... |
4152-4228 | 6.07e-03 | |||||||||||||
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, fibronectin. The tenth fibronectin type III repeat contains a RGD cell recognition sequence in a flexible loop between 2 strands. Type III modules are present in both extracellular and intracellular proteins. Pssm-ID: 214495 [Multi-domain] Cd Length: 83 Bit Score: 38.75 E-value: 6.07e-03
|
|||||||||||||||||
| Name | Accession | Description | Interval | E-value | ||||||||||||||
| VPS10 | smart00602 | VPS10 domain; |
2428-3031 | 1.58e-128 | ||||||||||||||
VPS10 domain; Pssm-ID: 214740 [Multi-domain] Cd Length: 612 Bit Score: 419.89 E-value: 1.58e-128
|
||||||||||||||||||
| Sortilin-Vps10 | pfam15902 | Sortilin, neurotensin receptor 3,; Sortilin, also known in mammals as neurotensin receptor-3, ... |
2433-2867 | 4.47e-108 | ||||||||||||||
Sortilin, neurotensin receptor 3,; Sortilin, also known in mammals as neurotensin receptor-3, is the archetypical member of a Vps10-domain (Vps10-D) that binds neurotrophic factors and neuropeptides. This domain constitutes the entire luminal part of Sortilin and is activated in the trans-Golgi network by enzymatic propeptide cleavage. The structure of the domain has been determined as a ten-bladed propeller, with up to 9 BNR or beta-hairpin turns in it. The mature receptor binds various ligands, including its own propeptide (Sort-pro), neurotensin, the pro-forms of nerve growth factor-beta (NGF)6 and brain-derived neurotrophic factor (BDNF)7, lipoprotein lipase (LpL), apo lipoprotein AV14 and the receptor-associated protein (RAP)1. Pssm-ID: 464929 [Multi-domain] Cd Length: 444 Bit Score: 354.20 E-value: 4.47e-108
|
||||||||||||||||||
| CH_SPTB-like_rpt1 | cd21246 | first calponin homology (CH) domain found in the beta-I spectrin-like subfamily; The beta-I ... |
36-152 | 2.06e-82 | ||||||||||||||
first calponin homology (CH) domain found in the beta-I spectrin-like subfamily; The beta-I spectrin-like family includes beta-I, -II, -III and -IV spectrins. Spectrin is an actin crosslinking and molecular scaffold protein that links the plasma membrane to the actin cytoskeleton, and functions in the determination of cell shape, arrangement of transmembrane proteins, and organization of organelles. It is composed of two antiparallel dimers of alpha- and beta- subunits. Beta-I spectrin, also called spectrin beta chain, erythrocytic (SPTB), may be involved in anaemia pathogenesis. Beta-II spectrin, also called spectrin beta chain, non-erythrocytic 1 (SPTBN1), or fodrin beta chain, is a component of fodrin, which is the general spectrin-like protein that seems to be involved in secretion. Fodrin interacts with calmodulin in a calcium-dependent manner and is thus a candidate for the calcium-dependent movement of the cytoskeleton at the membrane. Beta-III spectrin, also called spectrin beta chain, non-erythrocytic 2 (SPTBN2), or spinocerebellar ataxia 5 protein (SCA5), may play a crucial role as a longer actin-membrane cross-linker or fulfill the need for greater extensible flexibility than can be provided by the other smaller conventional spectrins. Beta-IV spectrin is also called spectrin, non-erythroid beta chain 3 (SPTBN3) or spectrin beta chain, non-erythrocytic 4 (SPTBN4). Its mutation associates with congenital myopathy, neuropathy, and central deafness. Members of this subfamily contain two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs. Pssm-ID: 409095 Cd Length: 117 Bit Score: 266.54 E-value: 2.06e-82
|
||||||||||||||||||
| CH_SPTB_like_rpt2 | cd21248 | second calponin homology (CH) domain found in the beta-I spectrin-like subfamily; The beta-I ... |
169-273 | 2.12e-78 | ||||||||||||||
second calponin homology (CH) domain found in the beta-I spectrin-like subfamily; The beta-I spectrin-like family includes beta-I, -II, -III and -IV spectrins. Spectrin is an actin crosslinking and molecular scaffold protein that links the plasma membrane to the actin cytoskeleton, and functions in the determination of cell shape, arrangement of transmembrane proteins, and organization of organelles. It is composed of two antiparallel dimers of alpha- and beta- subunits. Beta-I spectrin, also called spectrin beta chain, erythrocytic (SPTB), may be involved in anaemia pathogenesis. Beta-II spectrin, also called spectrin beta chain, non-erythrocytic 1 (SPTBN1), or fodrin beta chain, is a component of fodrin, which is the general spectrin-like protein that seems to be involved in secretion. Fodrin interacts with calmodulin in a calcium-dependent manner and is thus a candidate for the calcium-dependent movement of the cytoskeleton at the membrane. Beta-III spectrin, also called spectrin beta chain, non-erythrocytic 2 (SPTBN2), or spinocerebellar ataxia 5 protein (SCA5), may play a crucial role as a longer actin-membrane cross-linker or fulfill the need for greater extensible flexibility than can be provided by the other smaller conventional spectrins. Beta-IV spectrin is also called spectrin, non-erythroid beta chain 3 (SPTBN3) or spectrin beta chain, non-erythrocytic 4 (SPTBN4). Its mutation associates with congenital myopathy, neuropathy, and central deafness. Members of this subfamily contain two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs. Pssm-ID: 409097 Cd Length: 105 Bit Score: 254.63 E-value: 2.12e-78
|
||||||||||||||||||
| CH_SPTBN2_rpt1 | cd21317 | first calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 2 (SPTBN2) ... |
22-152 | 7.46e-78 | ||||||||||||||
first calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 2 (SPTBN2) and similar proteins; Spectrin is an actin crosslinking and molecular scaffold protein that links the plasma membrane to the actin cytoskeleton, and functions in the determination of cell shape, arrangement of transmembrane proteins, and organization of organelles. It is composed of two antiparallel dimers of alpha- and beta- subunits. SPTBN2, also called beta-III spectrin, or spinocerebellar ataxia 5 protein (SCA5), probably plays an important role in the neuronal membrane skeleton. Mutations in SPTBN2 is associated with spinocerebellar ataxia type 5. SPTBN2 contains two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs. Pssm-ID: 409166 Cd Length: 132 Bit Score: 254.21 E-value: 7.46e-78
|
||||||||||||||||||
| CH_SPTBN4_rpt1 | cd21318 | first calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 4 (SPTBN4) ... |
26-152 | 5.63e-70 | ||||||||||||||
first calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 4 (SPTBN4) and similar proteins; Spectrin is an actin crosslinking and molecular scaffold protein that links the plasma membrane to the actin cytoskeleton, and functions in the determination of cell shape, arrangement of transmembrane proteins, and organization of organelles. It is composed of two antiparallel dimers of alpha- and beta- subunits. SPTBN4, also called beta-IV spectrin, or spectrin, non-erythroid beta chain 3 (SPTBN3), is a novel spectrin isolated as an interactor of the receptor tyrosine phosphatase-like protein ICA512. Its mutation associates with congenital myopathy, neuropathy, and central deafness. SPTBN4 contains two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs. Pssm-ID: 409167 Cd Length: 139 Bit Score: 232.22 E-value: 5.63e-70
|
||||||||||||||||||
| CH_SPTBN1_rpt1 | cd21316 | first calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 1 (SPTBN1) ... |
22-152 | 6.44e-68 | ||||||||||||||
first calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 1 (SPTBN1) and similar proteins; Spectrin is an actin crosslinking and molecular scaffold protein that links the plasma membrane to the actin cytoskeleton, and functions in the determination of cell shape, arrangement of transmembrane proteins, and organization of organelles. It is composed of two antiparallel dimers of alpha- and beta- subunits. SPTBN1, also called beta-II spectrin, fodrin beta chain, or spectrin, non-erythroid beta chain 1, is also a component of fodrin, which is the general spectrin-like protein that seems to be involved in secretion. Fodrin interacts with calmodulin in a calcium-dependent manner and is thus a candidate for the calcium-dependent movement of the cytoskeleton at the membrane. SPTBN1 contains two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs. Pssm-ID: 409165 Cd Length: 154 Bit Score: 226.85 E-value: 6.44e-68
|
||||||||||||||||||
| CH_SPTB_rpt2 | cd21319 | second calponin homology (CH) domain found in spectrin beta chain, erythrocytic (SPTB) and ... |
166-277 | 2.03e-67 | ||||||||||||||
second calponin homology (CH) domain found in spectrin beta chain, erythrocytic (SPTB) and similar proteins; Spectrin is an actin crosslinking and molecular scaffold protein that links the plasma membrane to the actin cytoskeleton, and functions in the determination of cell shape, arrangement of transmembrane proteins, and organization of organelles. It is composed of two antiparallel dimers of alpha- and beta- subunits. SPTB, also called beta-I spectrin, may be involved in anaemia pathogenesis. SPTB contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs. Pssm-ID: 409168 Cd Length: 112 Bit Score: 223.73 E-value: 2.03e-67
|
||||||||||||||||||
| CH_beta_spectrin_rpt2 | cd21194 | second calponin homology (CH) domain found in the beta spectrin family; The beta spectrin ... |
169-273 | 5.70e-67 | ||||||||||||||
second calponin homology (CH) domain found in the beta spectrin family; The beta spectrin family includes beta-I, -II, -III, -IV and -V spectrins. Spectrin is an actin crosslinking and molecular scaffold protein that links the plasma membrane to the actin cytoskeleton, and functions in the determination of cell shape, arrangement of transmembrane proteins, and organization of organelles. It is composed of two antiparallel dimers of alpha- and beta- subunits. Beta-I spectrin, also called spectrin beta chain, erythrocytic (SPTB), may be involved in anaemia pathogenesis. Beta-II spectrin, also called spectrin beta chain, non-erythrocytic 1 (SPTBN1), or fodrin beta chain, is a component of fodrin, which is the general spectrin-like protein that seems to be involved in secretion. Fodrin interacts with calmodulin in a calcium-dependent manner and is thus a candidate for the calcium-dependent movement of the cytoskeleton at the membrane. Beta-IV spectrin is also called spectrin, non-erythroid beta chain 3 (SPTBN3) or spectrin beta chain, non-erythrocytic 4 (SPTBN4). Its mutation associates with congenital myopathy, neuropathy, and central deafness. Beta-III spectrin is also called spectrin beta chain, non-erythrocytic 2 (SPTBN2), or spinocerebellar ataxia 5 protein (SCA5). Beta-V spectrin, also called spectrin beta chain, non-erythrocytic 5 (SPTBN5), is a mammalian ortholog of Drosophila beta H spectrin. Beta-III and Beta-V spectrins may play crucial roles as longer actin-membrane cross-linkers or fulfill the need for greater extensible flexibility than can be provided by the other smaller conventional spectrins. Members of this family contain two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs. Pssm-ID: 409043 Cd Length: 105 Bit Score: 221.90 E-value: 5.70e-67
|
||||||||||||||||||
| CH_SPTBN2_rpt2 | cd21321 | second calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 2 (SPTBN2) ... |
166-284 | 4.19e-66 | ||||||||||||||
second calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 2 (SPTBN2) and similar proteins; Spectrin is an actin crosslinking and molecular scaffold protein that links the plasma membrane to the actin cytoskeleton, and functions in the determination of cell shape, arrangement of transmembrane proteins, and organization of organelles. It is composed of two antiparallel dimers of alpha- and beta- subunits. SPTBN2, also called beta-III spectrin, or spinocerebellar ataxia 5 protein (SCA5), probably plays an important role in the neuronal membrane skeleton. Mutations in SPTBN2 is associated with spinocerebellar ataxia type 5. SPTBN2 contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs. Pssm-ID: 409170 Cd Length: 119 Bit Score: 220.31 E-value: 4.19e-66
|
||||||||||||||||||
| CH_SPTBN4_rpt2 | cd21322 | second calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 4 (SPTBN4) ... |
154-283 | 8.86e-66 | ||||||||||||||
second calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 4 (SPTBN4) and similar proteins; Spectrin is an actin crosslinking and molecular scaffold protein that links the plasma membrane to the actin cytoskeleton, and functions in the determination of cell shape, arrangement of transmembrane proteins, and organization of organelles. It is composed of two antiparallel dimers of alpha- and beta- subunits. SPTBN4, also called beta-IV spectrin, or spectrin, non-erythroid beta chain 3 (SPTBN3), is a novel spectrin isolated as an interactor of the receptor tyrosine phosphatase-like protein ICA512. Its mutation associates with congenital myopathy, neuropathy, and central deafness. SPTBN4 contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs. Pssm-ID: 409171 Cd Length: 130 Bit Score: 219.54 E-value: 8.86e-66
|
||||||||||||||||||
| CH_beta_spectrin_rpt1 | cd21193 | first calponin homology (CH) domain found in the beta spectrin family; The beta spectrin ... |
36-152 | 6.03e-65 | ||||||||||||||
first calponin homology (CH) domain found in the beta spectrin family; The beta spectrin family includes beta-I, -II, -III, -IV and -V spectrins. Spectrin is an actin crosslinking and molecular scaffold protein that links the plasma membrane to the actin cytoskeleton, and functions in the determination of cell shape, arrangement of transmembrane proteins, and organization of organelles. It is composed of two antiparallel dimers of alpha- and beta- subunits. Beta-I spectrin, also called spectrin beta chain, erythrocytic (SPTB), may be involved in anaemia pathogenesis. Beta-II spectrin, also called spectrin beta chain, non-erythrocytic 1 (SPTBN1), or fodrin beta chain, is a component of fodrin, which is the general spectrin-like protein that seems to be involved in secretion. Fodrin interacts with calmodulin in a calcium-dependent manner and is thus a candidate for the calcium-dependent movement of the cytoskeleton at the membrane. Beta-IV spectrin is also called spectrin, non-erythroid beta chain 3 (SPTBN3) or spectrin beta chain, non-erythrocytic 4 (SPTBN4). Its mutation associates with congenital myopathy, neuropathy, and central deafness. Beta-III spectrin is also called spectrin beta chain, non-erythrocytic 2 (SPTBN2), or spinocerebellar ataxia 5 protein (SCA5). Beta-V spectrin, also called spectrin beta chain, non-erythrocytic 5 (SPTBN5), is a mammalian ortholog of Drosophila beta H spectrin. Beta-III and Beta-V spectrins may play crucial roles as longer actin-membrane cross-linkers or fulfill the need for greater extensible flexibility than can be provided by the other smaller conventional spectrins. Members of this family contain two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs. Pssm-ID: 409042 Cd Length: 116 Bit Score: 216.78 E-value: 6.03e-65
|
||||||||||||||||||
| SAC6 | COG5069 | Ca2+-binding actin-bundling protein fimbrin/plastin (EF-Hand superfamily) [Cytoskeleton]; |
44-450 | 6.75e-64 | ||||||||||||||
Ca2+-binding actin-bundling protein fimbrin/plastin (EF-Hand superfamily) [Cytoskeleton]; Pssm-ID: 227401 [Multi-domain] Cd Length: 612 Bit Score: 231.75 E-value: 6.75e-64
|
||||||||||||||||||
| CH_SPTBN1_rpt2 | cd21320 | second calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 1 (SPTBN1) ... |
169-276 | 4.07e-58 | ||||||||||||||
second calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 1 (SPTBN1) and similar proteins; Spectrin is an actin crosslinking and molecular scaffold protein that links the plasma membrane to the actin cytoskeleton, and functions in the determination of cell shape, arrangement of transmembrane proteins, and organization of organelles. It is composed of two antiparallel dimers of alpha- and beta- subunits. SPTBN1, also called beta-II spectrin, fodrin beta chain, or spectrin, non-erythroid beta chain 1, is also a component of fodrin, which is the general spectrin-like protein that seems to be involved in secretion. Fodrin interacts with calmodulin in a calcium-dependent manner and is thus a candidate for the calcium-dependent movement of the cytoskeleton at the membrane. SPTBN1 contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs. Pssm-ID: 409169 Cd Length: 108 Bit Score: 196.86 E-value: 4.07e-58
|
||||||||||||||||||
| CH_ACTN_rpt2 | cd21216 | second calponin homology (CH) domain found in the alpha-actinin family; The alpha-actinin ... |
155-274 | 1.23e-55 | ||||||||||||||
second calponin homology (CH) domain found in the alpha-actinin family; The alpha-actinin (ACTN) family includes alpha-actinin-1, -2, -3, and -4. They are F-actin cross-linking proteins which are thought to anchor actin to a variety of intracellular structures. ACTN1 mutations cause congenital macrothrombocytopenia. ACTN2 mutations are associated with cardiomyopathies, as well as skeletal muscle disorder. ACTN3 is critical in anchoring the myofibrillar actin filaments and plays a key role in muscle contraction. ACTN4 is associated with cell motility and cancer invasion. It is probably involved in vesicular trafficking via its association with the CART complex, which is necessary for efficient transferrin receptor recycling but not for epidermal growth factor receptor (EGFR) degradation. Members of this family contain two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs. Pssm-ID: 409065 Cd Length: 115 Bit Score: 189.88 E-value: 1.23e-55
|
||||||||||||||||||
| CH_SPTBN5_rpt2 | cd21249 | second calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 5 (SPTBN5) ... |
169-275 | 1.75e-55 | ||||||||||||||
second calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 5 (SPTBN5) and similar proteins; Spectrin is an actin crosslinking and molecular scaffold protein that links the plasma membrane to the actin cytoskeleton, and functions in the determination of cell shape, arrangement of transmembrane proteins, and organization of organelles. It is composed of two antiparallel dimers of alpha- and beta- subunits. SPTBN5, also called beta-V spectrin, is a mammalian ortholog of Drosophila beta H spectrin that may play a crucial role as a longer actin-membrane cross-linker or to fulfill the need for greater extensible flexibility than can be provided by the other smaller conventional spectrins. SPTBN5 contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs. Pssm-ID: 409098 Cd Length: 109 Bit Score: 189.30 E-value: 1.75e-55
|
||||||||||||||||||
| CH_PLEC-like_rpt1 | cd21188 | first calponin homology (CH) domain found in the plectin/dystonin/MACF1 family; This family ... |
51-154 | 1.30e-50 | ||||||||||||||
first calponin homology (CH) domain found in the plectin/dystonin/MACF1 family; This family includes plectin, dystonin and microtubule-actin cross-linking factor 1, isoforms 1/2/3/5 (MACF1). Plectin, also called PCN, PLTN, hemidesmosomal protein 1 (HD1), or plectin-1, is a structural component of muscle. It interlinks intermediate filaments with microtubules and microfilaments, and anchors intermediate filaments to desmosomes or hemidesmosomes. It could also bind muscle proteins such as actin to membrane complexes in muscle. Dystonin, also called 230 kDa bullous pemphigoid antigen, 230/240 kDa bullous pemphigoid antigen, bullous pemphigoid antigen 1 (BPA or BPAG1), dystonia musculorum protein, or hemidesmosomal plaque protein, is a cytoskeletal linker protein that acts as an integrator of intermediate filaments, actin, and microtubule cytoskeleton networks. It is required for anchoring either intermediate filaments to the actin cytoskeleton in neural and muscle cells, or keratin-containing intermediate filaments to hemidesmosomes in epithelial cells. MACF1, also called 620 kDa actin-binding protein (ABP620), actin cross-linking family protein 7 (ACF7), macrophin-1, or trabeculin-alpha, is a large protein containing numerous spectrin and leucine-rich repeat (LRR) domains. It facilitates actin-microtubule interactions at the cell periphery and couples the microtubule network to cellular junctions. Members of this family contain two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs. Pssm-ID: 409037 Cd Length: 105 Bit Score: 175.28 E-value: 1.30e-50
|
||||||||||||||||||
| Sortilin_C | pfam15901 | Sortilin, neurotensin receptor 3, C-terminal; Sortilin_C is the C-terminal cytoplasmic tail of ... |
2869-3030 | 1.32e-50 | ||||||||||||||
Sortilin, neurotensin receptor 3, C-terminal; Sortilin_C is the C-terminal cytoplasmic tail of sortilin, a Vps10p domain-containing family of proteins. Most sortilin is expressed within intracellular compartments, where it chaperones diverse ligands, including proBDNF and acid hydrolases. The sortilin cytoplasmic tail is homologous to mannose 6-phosphate receptor and is required for the intracellular trafficking of cargo proteins via interactions with distinct adaptor molecules. In addition to mediating lysosomal targeting of specific acid hydrolases, the sortilin cytoplasmic tail also directs trafficking of BDNF to the secretory pathway in neurons, where it can be released in response to depolarization to modulate cell survival and synaptic plasticity. Pssm-ID: 464928 [Multi-domain] Cd Length: 164 Bit Score: 177.51 E-value: 1.32e-50
|
||||||||||||||||||
| SPEC | cd00176 | Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
638-845 | 9.08e-50 | ||||||||||||||
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here Pssm-ID: 238103 [Multi-domain] Cd Length: 213 Bit Score: 177.25 E-value: 9.08e-50
|
||||||||||||||||||
| SPEC | cd00176 | Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
525-740 | 2.07e-48 | ||||||||||||||
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here Pssm-ID: 238103 [Multi-domain] Cd Length: 213 Bit Score: 173.40 E-value: 2.07e-48
|
||||||||||||||||||
| SPEC | cd00176 | Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
1546-1758 | 2.83e-48 | ||||||||||||||
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here Pssm-ID: 238103 [Multi-domain] Cd Length: 213 Bit Score: 173.02 E-value: 2.83e-48
|
||||||||||||||||||
| CH_PLEC-like_rpt2 | cd21189 | second calponin homology (CH) domain found in the plectin/dystonin/MACF1 family; This family ... |
170-273 | 1.02e-47 | ||||||||||||||
second calponin homology (CH) domain found in the plectin/dystonin/MACF1 family; This family includes plectin, dystonin and microtubule-actin cross-linking factor 1, isoforms 1/2/3/5 (MACF1). Plectin, also called PCN, PLTN, hemidesmosomal protein 1 (HD1), or plectin-1, is a structural component of muscle. It interlinks intermediate filaments with microtubules and microfilaments, and anchors intermediate filaments to desmosomes or hemidesmosomes. It could also bind muscle proteins such as actin to membrane complexes in muscle. Dystonin, also called 230 kDa bullous pemphigoid antigen, 230/240 kDa bullous pemphigoid antigen, bullous pemphigoid antigen 1 (BPA or BPAG1), dystonia musculorum protein, or hemidesmosomal plaque protein, is a cytoskeletal linker protein that acts as an integrator of intermediate filaments, actin, and microtubule cytoskeleton networks. It is required for anchoring either intermediate filaments to the actin cytoskeleton in neural and muscle cells, or keratin-containing intermediate filaments to hemidesmosomes in epithelial cells. MACF1, also called 620 kDa actin-binding protein (ABP620), actin cross-linking family protein 7 (ACF7), macrophin-1, or trabeculin-alpha, is a large protein containing numerous spectrin and leucine-rich repeat (LRR) domains. It facilitates actin-microtubule interactions at the cell periphery and couples the microtubule network to cellular junctions. Members of this family contain two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs. Pssm-ID: 409038 Cd Length: 105 Bit Score: 167.18 E-value: 1.02e-47
|
||||||||||||||||||
| SPEC | cd00176 | Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
1440-1651 | 9.87e-47 | ||||||||||||||
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here Pssm-ID: 238103 [Multi-domain] Cd Length: 213 Bit Score: 168.39 E-value: 9.87e-47
|
||||||||||||||||||
| SPEC | cd00176 | Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
1759-1967 | 4.30e-45 | ||||||||||||||
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here Pssm-ID: 238103 [Multi-domain] Cd Length: 213 Bit Score: 163.77 E-value: 4.30e-45
|
||||||||||||||||||
| PH_beta_spectrin | cd10571 | Beta-spectrin pleckstrin homology (PH) domain; Beta spectrin binds actin and functions as a ... |
2195-2290 | 6.86e-45 | ||||||||||||||
Beta-spectrin pleckstrin homology (PH) domain; Beta spectrin binds actin and functions as a major component of the cytoskeleton underlying cellular membranes. Beta spectrin consists of multiple spectrin repeats followed by a PH domain, which binds to inositol-1,4,5-trisphosphate. The PH domain of beta-spectrin is thought to play a role in the association of spectrin with the plasma membrane of cells. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes. Pssm-ID: 269975 Cd Length: 106 Bit Score: 158.93 E-value: 6.86e-45
|
||||||||||||||||||
| SPEC | cd00176 | Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
954-1167 | 1.15e-44 | ||||||||||||||
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here Pssm-ID: 238103 [Multi-domain] Cd Length: 213 Bit Score: 162.62 E-value: 1.15e-44
|
||||||||||||||||||
| SPEC | cd00176 | Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
1338-1543 | 4.28e-44 | ||||||||||||||
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here Pssm-ID: 238103 [Multi-domain] Cd Length: 213 Bit Score: 161.07 E-value: 4.28e-44
|
||||||||||||||||||
| CH_ACTN4_rpt2 | cd21290 | second calponin homology (CH) domain found in alpha-actinin-4; Alpha-actinin-4 (ACTN4), also ... |
152-279 | 2.27e-43 | ||||||||||||||
second calponin homology (CH) domain found in alpha-actinin-4; Alpha-actinin-4 (ACTN4), also called non-muscle alpha-actinin 4, is an F-actin cross-linking protein which is thought to anchor actin to a variety of intracellular structures. It is associated with cell motility and cancer invasion. ACTN4 is probably involved in vesicular trafficking via its association with the CART complex, which is necessary for efficient transferrin receptor recycling but not for epidermal growth factor receptor (EGFR) degradation. It contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs. Pssm-ID: 409139 Cd Length: 125 Bit Score: 155.63 E-value: 2.27e-43
|
||||||||||||||||||
| SPEC | cd00176 | Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
741-951 | 4.97e-43 | ||||||||||||||
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here Pssm-ID: 238103 [Multi-domain] Cd Length: 213 Bit Score: 157.99 E-value: 4.97e-43
|
||||||||||||||||||
| CH_SpAIN1-like_rpt2 | cd21291 | second calponin homology (CH) domain found in Schizosaccharomyces pombe alpha-actinin-like ... |
155-274 | 7.61e-43 | ||||||||||||||
second calponin homology (CH) domain found in Schizosaccharomyces pombe alpha-actinin-like protein 1 and similar proteins; Schizosaccharomyces pombe alpha-actinin-like protein 1 (SpAIN1) binds to actin and is involved in actin-ring formation and organization. It plays a role in cytokinesis and is involved in septation. Members of this family contain two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs. Pssm-ID: 409140 Cd Length: 115 Bit Score: 153.45 E-value: 7.61e-43
|
||||||||||||||||||
| CH_DMD-like_rpt1 | cd21186 | first calponin homology (CH) domain found in the dystrophin family; The dystrophin family ... |
51-156 | 2.05e-42 | ||||||||||||||
first calponin homology (CH) domain found in the dystrophin family; The dystrophin family includes dystrophin and its paralog, utrophin. Dystrophin, encoded by the DMD gene, is a large, submembrane cytoskeletal protein that is the main component of the dystrophin-glycoprotein complex (DGC) in skeletal muscles. It links the transmembrane DGC to the actin cytoskeleton through binding strongly to the cytoplasmic tail of beta-dystroglycan, the transmembrane subunit of a highly O-glycosylated cell-surface protein. Dystrophin is also involved in maintaining the structural integrity of cells, as well as in the formation of the blood-brain barrier (BBB). Utrophin, also called dystrophin-related protein 1 (DRP-1), is an autosomal dystrophin homolog that increases dystrophic muscle function and reduces pathology. It is broadly expressed in both the mRNA and protein levels, and occurs in the cerebrovascular endothelium. Utrophin forms the utrophin-glycoprotein complex (UGC) by interacting with dystroglycans (DGs) and sarcoglycan-dystroglycans, as well as sarcoglycan and sarcospan (SG-SSPN) subcomplexes. It may act as a scaffolding protein that stabilizes lipid microdomains and clusters mechanosensitive channel subunits, and links the F-actin cytoskeleton to the cell membrane via the associated glycoprotein complex. Members of this family contain two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs. Pssm-ID: 409035 Cd Length: 107 Bit Score: 151.77 E-value: 2.05e-42
|
||||||||||||||||||
| SPEC | cd00176 | Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
847-1057 | 8.32e-42 | ||||||||||||||
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here Pssm-ID: 238103 [Multi-domain] Cd Length: 213 Bit Score: 154.53 E-value: 8.32e-42
|
||||||||||||||||||
| CH_SYNE1_rpt1 | cd21241 | first calponin homology (CH) domain found in synaptic nuclear envelope protein 1 and similar ... |
47-156 | 1.79e-41 | ||||||||||||||
first calponin homology (CH) domain found in synaptic nuclear envelope protein 1 and similar proteins; Synaptic nuclear envelope protein 1 (SYNE-1), also called nesprin-1, enaptin, KASH domain-containing protein 1 (KASH1), myocyte nuclear envelope protein 1 (MYNE-1), or nuclear envelope spectrin repeat protein 1, is a multi-isomeric modular protein which forms a linking network between organelles and the actin cytoskeleton to maintain subcellular spatial organization. SYNE-1 also acts as a component of the LINC (LInker of Nucleoskeleton and Cytoskeleton) complex, which is involved in the connection between the nuclear lamina and the cytoskeleton. SYNE-1 contains two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs. Pssm-ID: 409090 Cd Length: 113 Bit Score: 149.45 E-value: 1.79e-41
|
||||||||||||||||||
| CH_DMD-like_rpt2 | cd21187 | second calponin homology (CH) domain found in the dystrophin family; The dystrophin family ... |
175-270 | 2.47e-41 | ||||||||||||||
second calponin homology (CH) domain found in the dystrophin family; The dystrophin family includes dystrophin and its paralog, utrophin. Dystrophin, encoded by the DMD gene, is a large, submembrane cytoskeletal protein that is the main component of the dystrophin-glycoprotein complex (DGC) in skeletal muscles. It links the transmembrane DGC to the actin cytoskeleton through binding strongly to the cytoplasmic tail of beta-dystroglycan, the transmembrane subunit of a highly O-glycosylated cell-surface protein. Dystrophin is also involved in maintaining the structural integrity of cells, as well as in the formation of the blood-brain barrier (BBB). Utrophin, also called dystrophin-related protein 1 (DRP-1), is an autosomal dystrophin homolog that increases dystrophic muscle function and reduces pathology. It is broadly expressed in both the mRNA and protein levels, and occurs in the cerebrovascular endothelium. Utrophin forms the utrophin-glycoprotein complex (UGC) by interacting with dystroglycans (DGs) and sarcoglycan-dystroglycans, as well as sarcoglycan and sarcospan (SG-SSPN) subcomplexes. It may act as a scaffolding protein that stabilizes lipid microdomains and clusters mechanosensitive channel subunits, and link the F-actin cytoskeleton to the cell membrane via the associated glycoprotein complex. Members of this family contain two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs. Pssm-ID: 409036 Cd Length: 104 Bit Score: 148.73 E-value: 2.47e-41
|
||||||||||||||||||
| SPEC | cd00176 | Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
422-634 | 3.37e-41 | ||||||||||||||
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here Pssm-ID: 238103 [Multi-domain] Cd Length: 213 Bit Score: 152.60 E-value: 3.37e-41
|
||||||||||||||||||
| CH_DYST_rpt1 | cd21236 | first calponin homology (CH) domain found in dystonin and similar proteins; Dystonin, also ... |
47-158 | 7.09e-41 | ||||||||||||||
first calponin homology (CH) domain found in dystonin and similar proteins; Dystonin, also called 230 kDa bullous pemphigoid antigen, 230/240 kDa bullous pemphigoid antigen, bullous pemphigoid antigen 1 (BPA or BPAG1), dystonia musculorum protein, or hemidesmosomal plaque protein, is a cytoskeletal linker protein that acts as an integrator of intermediate filaments, actin, and microtubule cytoskeleton networks. It is required for anchoring either intermediate filaments to the actin cytoskeleton in neural and muscle cells, or keratin-containing intermediate filaments to hemidesmosomes in epithelial cells. Dystonin contains two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs. Pssm-ID: 409085 Cd Length: 128 Bit Score: 148.59 E-value: 7.09e-41
|
||||||||||||||||||
| SPEC | cd00176 | Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
1652-1862 | 1.14e-40 | ||||||||||||||
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here Pssm-ID: 238103 [Multi-domain] Cd Length: 213 Bit Score: 151.06 E-value: 1.14e-40
|
||||||||||||||||||
| CH_MICALL2 | cd21253 | calponin homology (CH) domain found in MICAL-like protein 2 and similar proteins; MICAL-like ... |
174-273 | 6.78e-40 | ||||||||||||||
calponin homology (CH) domain found in MICAL-like protein 2 and similar proteins; MICAL-like protein 2 (MICAL-L2), also called junctional Rab13-binding protein (JRAB), or molecule interacting with CasL-like 2, acts as an effector of small Rab GTPases which is involved in junctional complexes assembly through the regulation of cell adhesion molecule transport to the plasma membrane, and actin cytoskeleton reorganization. It regulates the endocytic recycling of occludins, claudins, and E-cadherin to the plasma membrane and may thereby regulate the establishment of tight junctions and adherens junctions. Members of this subfamily contain a single copy of CH domain. CH domains are actin filament (F-actin) binding motifs. Pssm-ID: 409102 Cd Length: 106 Bit Score: 144.80 E-value: 6.78e-40
|
||||||||||||||||||
| CH_ACTN1_rpt2 | cd21287 | second calponin homology (CH) domain found in alpha-actinin-1; Alpha-actinin-1 (ACTN1), also ... |
155-278 | 1.37e-39 | ||||||||||||||
second calponin homology (CH) domain found in alpha-actinin-1; Alpha-actinin-1 (ACTN1), also called alpha-actinin cytoskeletal isoform, or non-muscle alpha-actinin-1, is an F-actin cross-linking protein which is thought to anchor actin to a variety of intracellular structures. ACTN1 is a bundling protein. Its mutations cause congenital macrothrombocytopenia. It contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs. Pssm-ID: 409136 Cd Length: 124 Bit Score: 144.46 E-value: 1.37e-39
|
||||||||||||||||||
| CH_ACTN_rpt1 | cd21214 | first calponin homology (CH) domain found in the alpha-actinin family; The alpha-actinin (ACTN) ... |
49-151 | 1.57e-39 | ||||||||||||||
first calponin homology (CH) domain found in the alpha-actinin family; The alpha-actinin (ACTN) family includes alpha-actinin-1, -2, -3, and -4. They are F-actin cross-linking proteins which are thought to anchor actin to a variety of intracellular structures. ACTN1 mutations cause congenital macrothrombocytopenia. ACTN2 mutations are associated with cardiomyopathies, as well as skeletal muscle disorder. ACTN3 is critical in anchoring the myofibrillar actin filaments and plays a key role in muscle contraction. ACTN4 is associated with cell motility and cancer invasion. It is probably involved in vesicular trafficking via its association with the CART complex, which is necessary for efficient transferrin receptor recycling but not for epidermal growth factor receptor (EGFR) degradation. Members of this family contain two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs. Pssm-ID: 409063 Cd Length: 105 Bit Score: 143.68 E-value: 1.57e-39
|
||||||||||||||||||
| CH_PLEC_rpt1 | cd21235 | first calponin homology (CH) domain found in plectin and similar proteins; Plectin, also ... |
47-160 | 2.24e-39 | ||||||||||||||
first calponin homology (CH) domain found in plectin and similar proteins; Plectin, also called PCN, PLTN, hemidesmosomal protein 1 (HD1), or plectin-1, is a structural component of muscle. It interlinks intermediate filaments with microtubules and microfilaments, and anchors intermediate filaments to desmosomes or hemidesmosomes. It can also bind muscle proteins such as actin to membrane complexes in muscle. Plectin contains two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs. Pssm-ID: 409084 Cd Length: 119 Bit Score: 143.63 E-value: 2.24e-39
|
||||||||||||||||||
| CH_ACTN3_rpt2 | cd21289 | second calponin homology (CH) domain found in alpha-actinin-3; Alpha-actinin-3 (ACTN3), also ... |
155-278 | 2.84e-39 | ||||||||||||||
second calponin homology (CH) domain found in alpha-actinin-3; Alpha-actinin-3 (ACTN3), also called alpha-actinin skeletal muscle isoform 3, is an F-actin cross-linking protein which is thought to anchor actin to a variety of intracellular structures. ACTN3 is a bundling protein. It is critical in anchoring the myofibrillar actin filaments and plays a key role in muscle contraction. It contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs. Pssm-ID: 409138 Cd Length: 124 Bit Score: 143.71 E-value: 2.84e-39
|
||||||||||||||||||
| CH_SPTBN5_rpt1 | cd21247 | first calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 5 (SPTBN5) ... |
36-155 | 1.30e-38 | ||||||||||||||
first calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 5 (SPTBN5) and similar proteins; Spectrin is an actin crosslinking and molecular scaffold protein that links the plasma membrane to the actin cytoskeleton, and functions in the determination of cell shape, arrangement of transmembrane proteins, and organization of organelles. It is composed of two antiparallel dimers of alpha- and beta- subunits. SPTBN5, also called beta-V spectrin, is a mammalian ortholog of Drosophila beta H spectrin that may play a crucial role as a longer actin-membrane cross-linker or to fulfill the need for greater extensible flexibility than can be provided by the other smaller conventional spectrins. SPTBN5 contains two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs. Pssm-ID: 409096 Cd Length: 125 Bit Score: 141.82 E-value: 1.30e-38
|
||||||||||||||||||
| CH_SYNE1_rpt2 | cd21243 | second calponin homology (CH) domain found in synaptic nuclear envelope protein 1 (SYNE-1) and ... |
170-273 | 1.93e-38 | ||||||||||||||
second calponin homology (CH) domain found in synaptic nuclear envelope protein 1 (SYNE-1) and similar proteins; SYNE-1, also called nesprin-1, enaptin, KASH domain-containing protein 1 (KASH1), myocyte nuclear envelope protein 1 (MYNE-1), or nuclear envelope spectrin repeat protein 1, is a multi-isomeric modular protein which forms a linking network between organelles and the actin cytoskeleton to maintain subcellular spatial organization. SYNE-1 also acts as a component of the LINC (LInker of Nucleoskeleton and Cytoskeleton) complex, which is involved in the connection between the nuclear lamina and the cytoskeleton. SYNE-1 contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs. Pssm-ID: 409092 Cd Length: 109 Bit Score: 140.53 E-value: 1.93e-38
|
||||||||||||||||||
| CH_DYST_rpt2 | cd21239 | second calponin homology (CH) domain found in dystonin and similar proteins; Dystonin, also ... |
170-273 | 1.83e-37 | ||||||||||||||
second calponin homology (CH) domain found in dystonin and similar proteins; Dystonin, also called 230 kDa bullous pemphigoid antigen, 230/240 kDa bullous pemphigoid antigen, bullous pemphigoid antigen 1 (BPA or BPAG1), dystonia musculorum protein, or hemidesmosomal plaque protein, is a cytoskeletal linker protein that acts as an integrator of intermediate filaments, actin, and microtubule cytoskeleton networks. It is required for anchoring either intermediate filaments to the actin cytoskeleton in neural and muscle cells, or keratin-containing intermediate filaments to hemidesmosomes in epithelial cells. Dystonin contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs. Pssm-ID: 409088 Cd Length: 104 Bit Score: 137.81 E-value: 1.83e-37
|
||||||||||||||||||
| CH_ACTN2_rpt2 | cd21288 | second calponin homology (CH) domain found in alpha-actinin-2; Alpha-actinin-2 (ACTN2), also ... |
155-278 | 3.10e-37 | ||||||||||||||
second calponin homology (CH) domain found in alpha-actinin-2; Alpha-actinin-2 (ACTN2), also called alpha-actinin skeletal muscle isoform 2, is an F-actin cross-linking protein which is thought to anchor actin to a variety of intracellular structures. ACTN2 is a bundling protein. Its mutations are associated with cardiomyopathies, as well as skeletal muscle disorder. It contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs. Pssm-ID: 409137 Cd Length: 124 Bit Score: 137.90 E-value: 3.10e-37
|
||||||||||||||||||
| CH_SpAIN1-like_rpt1 | cd21215 | first calponin homology (CH) domain found in Schizosaccharomyces pombe alpha-actinin-like ... |
49-153 | 3.26e-37 | ||||||||||||||
first calponin homology (CH) domain found in Schizosaccharomyces pombe alpha-actinin-like protein 1 and similar proteins; Schizosaccharomyces pombe alpha-actinin-like protein 1 (SpAIN1) binds to actin and is involved in actin-ring formation and organization. It plays a role in cytokinesis and is involved in septation. Members of this family contain two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs. Pssm-ID: 409064 Cd Length: 107 Bit Score: 137.15 E-value: 3.26e-37
|
||||||||||||||||||
| CH_MACF1_rpt1 | cd21237 | first calponin homology (CH) domain found in microtubule-actin cross-linking factor 1, ... |
47-160 | 3.77e-37 | ||||||||||||||
first calponin homology (CH) domain found in microtubule-actin cross-linking factor 1, isoforms 1/2/3/5 (MACF1) and similar proteins; MACF1, also called 620 kDa actin-binding protein (ABP620), actin cross-linking family protein 7 (ACF7), macrophin-1, or trabeculin-alpha, is a large protein containing numerous spectrin and leucine-rich repeat (LRR) domains. It facilitates actin-microtubule interactions at the cell periphery and couples the microtubule network to cellular junctions. MACF1 contains two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs. Pssm-ID: 409086 Cd Length: 118 Bit Score: 137.47 E-value: 3.77e-37
|
||||||||||||||||||
| CH_SYNE-like_rpt1 | cd21190 | first calponin homology (CH) domain found in the synaptic nuclear envelope protein family; The ... |
47-156 | 2.41e-35 | ||||||||||||||
first calponin homology (CH) domain found in the synaptic nuclear envelope protein family; The synaptic nuclear envelope (SYNE) family includes SYNE-1, -2 and calmin. SYNE-1 (also called nesprin-1, enaptin, KASH domain-containing protein 1, KASH1, myocyte nuclear envelope protein 1, MYNE-1, or nuclear envelope spectrin repeat protein 1) and SYNE-2 (also called nesprin-2, KASH domain-containing protein 2, KASH2, nuclear envelope spectrin repeat protein 2, nucleus and actin connecting element protein, or protein NUANCE) may act redundantly. They are multi-isomeric modular proteins which form a linking network between organelles and the actin cytoskeleton to maintain subcellular spatial organization. They also act as components of the LINC (LInker of Nucleoskeleton and Cytoskeleton) complex, which is involved in the connection between the nuclear lamina and the cytoskeleton. Calmin, also called calponin-like transmembrane domain protein, is a protein with calponin homology (CH) and transmembrane domains expressed in maturing spermatogenic cells. It may be involved in the development and/or maintenance of neuronal functions. Members of this family contain two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs. Pssm-ID: 409039 Cd Length: 113 Bit Score: 131.92 E-value: 2.41e-35
|
||||||||||||||||||
| CH_MICALL | cd21197 | calponin homology (CH) domain found in the MICAL-like protein family; The MICAL-L family ... |
174-273 | 6.03e-35 | ||||||||||||||
calponin homology (CH) domain found in the MICAL-like protein family; The MICAL-L family includes MICAL-L1 and MICAL-L2. MICAL-L1, also called molecule interacting with Rab13 (MIRab13), is a probable lipid-binding protein with higher affinity for phosphatidic acid, a lipid enriched in recycling endosome membranes. It is a tubular endosomal membrane hub that connects Rab35 and Arf6 with Rab8a. It may be involved in a late step of receptor-mediated endocytosis regulating endocytosed-EGF receptor trafficking. Alternatively, it may regulate slow endocytic recycling of endocytosed proteins back to the plasma membrane. MICAL-L1 may indirectly play a role in neurite outgrowth. MICAL-L2, also called junctional Rab13-binding protein (JRAB), or molecule interacting with CasL-like 2, acts as an effector of small Rab GTPases which is involved in junctional complexes assembly through the regulation of cell adhesion molecule transport to the plasma membrane, and actin cytoskeleton reorganization. It regulates the endocytic recycling of occludins, claudins, and E-cadherin to the plasma membrane and may thereby regulate the establishment of tight junctions and adherens junctions. Members of this family contain a single copy of CH domain. CH domains are actin filament (F-actin) binding motifs. Pssm-ID: 409046 Cd Length: 105 Bit Score: 130.73 E-value: 6.03e-35
|
||||||||||||||||||
| SPEC | cd00176 | Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
1865-2032 | 6.58e-35 | ||||||||||||||
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here Pssm-ID: 238103 [Multi-domain] Cd Length: 213 Bit Score: 134.50 E-value: 6.58e-35
|
||||||||||||||||||
| CH_PLEC_rpt2 | cd21238 | second calponin homology (CH) domain found in plectin and similar proteins; Plectin, also ... |
170-270 | 1.93e-34 | ||||||||||||||
second calponin homology (CH) domain found in plectin and similar proteins; Plectin, also called PCN, PLTN, hemidesmosomal protein 1 (HD1), or plectin-1, is a structural component of muscle. It interlinks intermediate filaments with microtubules and microfilaments and anchors intermediate filaments to desmosomes or hemidesmosomes. It can also bind muscle proteins such as actin to membrane complexes in muscle. Plectin contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs. Pssm-ID: 409087 Cd Length: 106 Bit Score: 128.99 E-value: 1.93e-34
|
||||||||||||||||||
| CH_DMD_rpt1 | cd21231 | first calponin homology (CH) domain found in dystrophin and similar proteins; Dystrophin, ... |
47-156 | 2.66e-34 | ||||||||||||||
first calponin homology (CH) domain found in dystrophin and similar proteins; Dystrophin, encoded by the DMD gene, is a large, submembrane cytoskeletal protein that is the main component of the dystrophin-glycoprotein complex (DGC) in skeletal muscles. It links the transmembrane DGC to the actin cytoskeleton through binding strongly to the cytoplasmic tail of beta-dystroglycan, the transmembrane subunit of a highly O-glycosylated cell-surface protein. It is involved in maintaining the structural integrity of cells, as well as in the formation of the blood-brain barrier (BBB). Mutations in dystrophin lead to Duchenne muscular dystrophy (DMD). Moreover, dystrophin deficiency is associated with abnormal cerebral diffusion and perfusion, as well as in acute Trypanosoma cruzi infection. The dystrophin subfamily has been characterized by a compact cluster of domains comprising four EF-hand-like motifs and a ZZ-domain, followed by a looser region with two coiled-coils. These domains are believed to be involved in protein-protein interactions. In addition, dystrophin contains two syntrophin binding sites (SBSs) and a long N-terminal extension that comprises two actin-binding calponin homology (CH) domains, approximately 24 spectrin repeats (SRs) and a WW domain. This model corresponds to the first CH domain. Pssm-ID: 409080 Cd Length: 111 Bit Score: 128.89 E-value: 2.66e-34
|
||||||||||||||||||
| CH_MICAL_EHBP-like | cd22198 | calponin homology (CH) domain found in the MICAL and EHBP families; This group is composed of ... |
173-274 | 3.53e-34 | ||||||||||||||
calponin homology (CH) domain found in the MICAL and EHBP families; This group is composed of the molecule interacting with CasL protein (MICAL) and EH domain-binding protein (EHBP) families. MICAL is a large, multidomain, cytosolic protein with a single LIM domain, a calponin homology (CH) domain and a flavoprotein monooxygenase (MO) domain. In Drosophila, MICAL is expressed in axons, interacts with the neuronal A (PlexA) receptor and is required for Semaphorin 1a (Sema-1a)-PlexA-mediated repulsive axon guidance. The LIM and CH domains mediate interactions with the cytoskeleton, cytoskeletal adaptor proteins, and other signaling proteins. The flavoprotein MO is required for semaphorin-plexin repulsive axon guidance during axonal pathfinding in the Drosophila neuromuscular system. The EHBP family includes EHBP1 and EHBP1-like protein (EHBP1L1). EHBP1 is a regulator of endocytic recycling and may play a role in actin reorganization by linking clathrin-mediated endocytosis to the actin cytoskeleton. It may act as an effector of small GTPases, including RAB-10 (Rab10), and play a role in vesicle trafficking. EHBP proteins contain a single CH domain. CH domains are actin filament (F-actin) binding motifs. Pssm-ID: 409188 Cd Length: 105 Bit Score: 128.17 E-value: 3.53e-34
|
||||||||||||||||||
| SPEC | cd00176 | Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
1059-1273 | 9.14e-34 | ||||||||||||||
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here Pssm-ID: 238103 [Multi-domain] Cd Length: 213 Bit Score: 131.41 E-value: 9.14e-34
|
||||||||||||||||||
| SPEC | cd00176 | Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
1169-1436 | 4.11e-33 | ||||||||||||||
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here Pssm-ID: 238103 [Multi-domain] Cd Length: 213 Bit Score: 129.49 E-value: 4.11e-33
|
||||||||||||||||||
| CH_MICALL1 | cd21252 | calponin homology (CH) domain found in MICAL-like protein 1; MICAL-like protein 1 (MICAL-L1), ... |
171-275 | 2.62e-32 | ||||||||||||||
calponin homology (CH) domain found in MICAL-like protein 1; MICAL-like protein 1 (MICAL-L1), also called molecule interacting with Rab13 (MIRab13), is a probable lipid-binding protein with higher affinity for phosphatidic acid, a lipid enriched in recycling endosome membranes. It is a tubular endosomal membrane hub that connects Rab35 and Arf6 with Rab8a. It may be involved in a late step of receptor-mediated endocytosis regulating endocytosed-EGF receptor trafficking. Alternatively, it may regulate slow endocytic recycling of endocytosed proteins back to the plasma membrane. MICAL-L1 may indirectly play a role in neurite outgrowth. It contains a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs. Pssm-ID: 409101 Cd Length: 107 Bit Score: 123.06 E-value: 2.62e-32
|
||||||||||||||||||
| CH_SYNE-like_rpt2 | cd21192 | second calponin homology (CH) domain found in the synaptic nuclear envelope protein (SYNE) ... |
170-273 | 3.50e-32 | ||||||||||||||
second calponin homology (CH) domain found in the synaptic nuclear envelope protein (SYNE) family; The SYNE family includes SYNE-1, -2 and calmin. SYNE-1 (also called nesprin-1, enaptin, KASH domain-containing protein 1, KASH1, myocyte nuclear envelope protein 1, MYNE-1, or nuclear envelope spectrin repeat protein 1) and SYNE-2 (also called nesprin-2, KASH domain-containing protein 2, KASH2, nuclear envelope spectrin repeat protein 2, nucleus and actin connecting element protein, or protein NUANCE) may act redundantly. They are multi-isomeric modular proteins which form a linking network between organelles and the actin cytoskeleton to maintain subcellular spatial organization. They also act as components of the LINC (LInker of Nucleoskeleton and Cytoskeleton) complex, which is involved in the connection between the nuclear lamina and the cytoskeleton. Calmin, also called calponin-like transmembrane domain protein, is a protein with calponin homology (CH) and transmembrane domains expressed in maturing spermatogenic cells. It may be involved in the development and/or maintenance of neuronal functions. Members of this family contain two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs. Pssm-ID: 409041 Cd Length: 107 Bit Score: 122.53 E-value: 3.50e-32
|
||||||||||||||||||
| CH_MACF1_rpt2 | cd21240 | second calponin homology (CH) domain found in microtubule-actin cross-linking factor 1, ... |
170-273 | 4.37e-32 | ||||||||||||||
second calponin homology (CH) domain found in microtubule-actin cross-linking factor 1, isoforms 1/2/3/5 (MACF1) and similar proteins; MACF1, also called 620 kDa actin-binding protein (ABP620), actin cross-linking family protein 7 (ACF7), macrophin-1, or trabeculin-alpha, is a large protein containing numerous spectrin and leucine-rich repeat (LRR) domains. It facilitates actin-microtubule interactions at the cell periphery and couples the microtubule network to cellular junctions. MACF1 contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs. Pssm-ID: 409089 Cd Length: 107 Bit Score: 122.46 E-value: 4.37e-32
|
||||||||||||||||||
| CH_SYNE2_rpt1 | cd21242 | first calponin homology (CH) domain found in synaptic nuclear envelope protein 2; Synaptic ... |
47-156 | 4.91e-32 | ||||||||||||||
first calponin homology (CH) domain found in synaptic nuclear envelope protein 2; Synaptic nuclear envelope protein 2 (SYNE-2), also called nesprin-2, KASH domain-containing protein 2 (KASH2), nuclear envelope spectrin repeat protein 2, nucleus and actin connecting element protein, or protein NUANCE, is a multi-isomeric modular protein which forms a linking network between organelles and the actin cytoskeleton to maintain subcellular spatial organization. SYNE-2 also acts as a component of the LINC (LInker of Nucleoskeleton and Cytoskeleton) complex, which is involved in the connection between the nuclear lamina and the cytoskeleton. SYNE-2 contains two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs. Pssm-ID: 409091 Cd Length: 111 Bit Score: 122.63 E-value: 4.91e-32
|
||||||||||||||||||
| CH_UTRN_rpt2 | cd21234 | second calponin homology (CH) domain found in utrophin and similar proteins; Utrophin, also ... |
175-270 | 3.15e-31 | ||||||||||||||
second calponin homology (CH) domain found in utrophin and similar proteins; Utrophin, also called dystrophin-related protein 1 (DRP-1), is an autosomal dystrophin homolog that increases dystrophic muscle function and reduces pathology. It is broadly expressed in both the mRNA and protein levels, and occurs in the cerebrovascular endothelium. Utrophin forms the utrophin-glycoprotein complex (UGC) by interacting with dystroglycans (DGs) and sarcoglycan-dystroglycans, as well as sarcoglycan and sarcospan (SG-SSPN) subcomplexes. It may act as a scaffolding protein that stabilizes lipid microdomains and clusters mechanosensitive channel subunits, and link the F-actin cytoskeleton to the cell membrane via the associated glycoprotein complex. Like dystrophin, utrophin has a compact cluster of domains comprising four EF-hand-like motifs and a ZZ-domain, followed by a looser region with two coiled-coils. These domains are believed to be involved in protein-protein interactions. In addition, it contains two syntrophin binding sites (SBSs) and a long N-terminal extension that comprises two actin-binding calponin homology (CH) domains, up to 24 spectrin repeats (SRs), and a WW domain. However, utrophin lacks the intrinsic microtubule binding activity of dystrophin SRs. This model corresponds to the second CH domain. Pssm-ID: 409083 [Multi-domain] Cd Length: 104 Bit Score: 120.06 E-value: 3.15e-31
|
||||||||||||||||||
| CH | pfam00307 | Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal ... |
169-275 | 6.58e-31 | ||||||||||||||
Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal transduction proteins. The CH domain is involved in actin binding in some members of the family. However in calponins there is evidence that the CH domain is not involved in its actin binding activity. Most member proteins have from two to four copies of the CH domain, however some proteins such as calponin have only a single copy. Pssm-ID: 425596 [Multi-domain] Cd Length: 109 Bit Score: 119.31 E-value: 6.58e-31
|
||||||||||||||||||
| CH_SYNE2_rpt2 | cd21244 | second calponin homology (CH) domain found in synaptic nuclear envelope protein 2 (SYNE-2) and ... |
170-273 | 7.45e-31 | ||||||||||||||
second calponin homology (CH) domain found in synaptic nuclear envelope protein 2 (SYNE-2) and similar proteins; SYNE-2, also called nesprin-2, KASH domain-containing protein 2 (KASH2), nuclear envelope spectrin repeat protein 2, nucleus and actin connecting element protein, or protein NUANCE, is a multi-isomeric modular protein which forms a linking network between organelles and the actin cytoskeleton to maintain subcellular spatial organization. SYNE-2 also acts as a component of the LINC (LInker of Nucleoskeleton and Cytoskeleton) complex, which is involved in the connection between the nuclear lamina and the cytoskeleton. SYNE-2 contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs. Pssm-ID: 409093 Cd Length: 109 Bit Score: 119.17 E-value: 7.45e-31
|
||||||||||||||||||
| Spectrin | pfam00435 | Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ... |
634-738 | 6.89e-30 | ||||||||||||||
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in cytoskeletal structure. These include spectrin, alpha-actinin and dystrophin. The sequence repeat used in this family is taken from the structural repeat in reference. The spectrin domain- repeat forms a three helix bundle. The second helix is interrupted by proline in some sequences. The repeats are defined by a characteriztic tryptophan (W) residue at position 17 in helix A and a leucine (L) at 2 residues from the carboxyl end of helix C. Although the domain occurs in multiple repeats along sequences, the domains are actually stable on their own - ie they act, biophysically, like domains rather than repeats that along function when aggregated. Pssm-ID: 395348 [Multi-domain] Cd Length: 105 Bit Score: 116.26 E-value: 6.89e-30
|
||||||||||||||||||
| CH_CLMN_rpt1 | cd21191 | first calponin homology (CH) domain found in calmin and similar proteins; Calmin, also called ... |
47-157 | 9.24e-30 | ||||||||||||||
first calponin homology (CH) domain found in calmin and similar proteins; Calmin, also called calponin-like transmembrane domain protein, is a protein with calponin homology (CH) and transmembrane domains expressed in maturing spermatogenic cells. It may be involved in the development and/or maintenance of neuronal functions. Calmin contains two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs. Pssm-ID: 409040 Cd Length: 114 Bit Score: 116.14 E-value: 9.24e-30
|
||||||||||||||||||
| CH_jitterbug-like_rpt1 | cd21227 | first calponin homology (CH) domain found in Drosophila melanogaster protein jitterbug and ... |
51-155 | 1.47e-29 | ||||||||||||||
first calponin homology (CH) domain found in Drosophila melanogaster protein jitterbug and similar proteins; Protein jitterbug (Jbug) is an actin-meshwork organizing protein. It is required to maintain the shape and cell orientation of the Drosophila notum epithelium during flight muscle attachment to tendon cells. Jbug contains three copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs. Pssm-ID: 409076 Cd Length: 109 Bit Score: 115.46 E-value: 1.47e-29
|
||||||||||||||||||
| CH_DMD_rpt2 | cd21233 | second calponin homology (CH) domain found in dystrophin and similar proteins; Dystrophin, ... |
175-270 | 1.85e-29 | ||||||||||||||
second calponin homology (CH) domain found in dystrophin and similar proteins; Dystrophin, encoded by the DMD gene, is a large, submembrane cytoskeletal protein that is the main component of the dystrophin-glycoprotein complex (DGC) in skeletal muscles. It links the transmembrane DGC to the actin cytoskeleton through binding strongly to the cytoplasmic tail of beta-dystroglycan, the transmembrane subunit of a highly O-glycosylated cell-surface protein. It is involved in maintaining the structural integrity of cells, as well as in the formation of the blood-brain barrier (BBB). Mutations in dystrophin lead to Duchenne muscular dystrophy (DMD). Moreover, dystrophin deficiency is associated with abnormal cerebral diffusion and perfusion, as well as in acute Trypanosoma cruzi infection. The dystrophin subfamily has been characterized by a compact cluster of domains comprising four EF-hand-like motifs and a ZZ-domain, followed by a looser region with two coiled-coils. These domains are believed to be involved in protein-protein interactions. In addition, dystrophin contains two syntrophin binding sites (SBSs) and a long N-terminal extension that comprises two actin-binding calponin homology (CH) domains, approximately 24 spectrin repeats (SRs) and a WW domain. The model corresponds to the second CH domain. Pssm-ID: 409082 Cd Length: 111 Bit Score: 115.03 E-value: 1.85e-29
|
||||||||||||||||||
| CH_CTX_rpt2 | cd21226 | second calponin homology (CH) domain found in cortexillin; Cortexillins are actin-bundling ... |
173-273 | 5.90e-29 | ||||||||||||||
second calponin homology (CH) domain found in cortexillin; Cortexillins are actin-bundling proteins that play a critical role in regulating cell morphology and actin cytoskeleton reorganization. They play a major role in cytokinesis and contain two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs. Pssm-ID: 409075 Cd Length: 103 Bit Score: 113.33 E-value: 5.90e-29
|
||||||||||||||||||
| SPEC | smart00150 | Spectrin repeats; |
637-737 | 6.59e-29 | ||||||||||||||
Spectrin repeats; Pssm-ID: 197544 [Multi-domain] Cd Length: 101 Bit Score: 113.19 E-value: 6.59e-29
|
||||||||||||||||||
| CH_SMTN-like | cd21200 | calponin homology (CH) domain found in the smoothelin family; The smoothelin family includes ... |
170-274 | 1.06e-28 | ||||||||||||||
calponin homology (CH) domain found in the smoothelin family; The smoothelin family includes smoothelin and smoothelin-like proteins. Smoothelins are actin-binding cytoskeletal proteins that are abundantly expressed in healthy visceral (smoothelin-A) and vascular (smoothelin-B) smooth muscle. SMTNL1, also called calponin homology-associated smooth muscle protein (CHASM), plays a role in the regulation of contractile properties of both striated and smooth muscles. It can bind to calmodulin and tropomyosin. When it is unphosphorylated, SMTNL1 may inhibit myosin dephosphorylation. SMTNL2 is highly expressed in skeletal muscle and could be associated with differentiating myocytes. Members of this family contain a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs. Pssm-ID: 409049 Cd Length: 107 Bit Score: 112.82 E-value: 1.06e-28
|
||||||||||||||||||
| CH_UTRN_rpt1 | cd21232 | first calponin homology (CH) domain found in utrophin and similar proteins; Utrophin, also ... |
51-156 | 1.37e-28 | ||||||||||||||
first calponin homology (CH) domain found in utrophin and similar proteins; Utrophin, also called dystrophin-related protein 1 (DRP-1), is an autosomal dystrophin homolog that increases dystrophic muscle function and reduces pathology. It is broadly expressed in both the mRNA and protein levels, and occurs in the cerebrovascular endothelium. Utrophin forms the utrophin-glycoprotein complex (UGC) by interacting with dystroglycans (DGs) and sarcoglycan-dystroglycans, as well as sarcoglycan and sarcospan (SG-SSPN) subcomplexes. It may act as a scaffolding protein that stabilizes lipid microdomains and clusters mechanosensitive channel subunits, and link the F-actin cytoskeleton to the cell membrane via the associated glycoprotein complex. Like dystrophin, utrophin has a compact cluster of domains comprising four EF-hand-like motifs and a ZZ-domain, followed by a looser region with two coiled-coils. These domains are believed to be involved in protein-protein interactions. In addition, it contains two syntrophin binding sites (SBSs) and a long N-terminal extension that comprises two actin-binding calponin homology (CH) domains, up to 24 spectrin repeats (SRs), and a WW domain. However, utrophin lacks the intrinsic microtubule binding activity of dystrophin SRs. This model corresponds to the first CH domain. Pssm-ID: 409081 Cd Length: 107 Bit Score: 112.41 E-value: 1.37e-28
|
||||||||||||||||||
| CH_EHBP | cd21198 | calponin homology (CH) domain found in the EH domain-binding protein (EHBP) family; The EHBP ... |
169-274 | 1.83e-28 | ||||||||||||||
calponin homology (CH) domain found in the EH domain-binding protein (EHBP) family; The EHBP family includes EHBP1 and EHBP1-like protein (EHBP1L1). EHBP1 is a regulator of endocytic recycling and may play a role in actin reorganization by linking clathrin-mediated endocytosis to the actin cytoskeleton. It may act as an effector of small GTPases, including RAB-10 (Rab10), and play a role in vesicle trafficking. EHBP1 is associated with aggressive prostate cancer and insulin-stimulated trafficking and cell migration. EHBP1L1 may also act as Rab effector protein and play a role in vesicle trafficking. It coordinates Rab8 and Bin1 to regulate apical-directed transport in polarized epithelial cells. Members of this family contain a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs. Pssm-ID: 409047 Cd Length: 105 Bit Score: 112.13 E-value: 1.83e-28
|
||||||||||||||||||
| CH_MICAL2_3-like | cd21195 | calponin homology (CH) domain found in molecule interacting with CasL protein 2 (MICAL-2), ... |
175-273 | 5.61e-26 | ||||||||||||||
calponin homology (CH) domain found in molecule interacting with CasL protein 2 (MICAL-2), MICAL-3, and similar proteins; Molecule interacting with CasL protein (MICAL) is a large, multidomain, cytosolic protein with a single LIM domain, a calponin homology (CH) domain and a flavoprotein monooxygenase (MO) domain. In Drosophila, MICAL is expressed in axons, interacts with the neuronal A (PlexA) receptor and is required for Semaphorin 1a (Sema-1a)-PlexA-mediated repulsive axon guidance. The LIM and CH domains mediate interactions with the cytoskeleton, cytoskeletal adaptor proteins, and other signaling proteins. The flavoprotein MO is required for semaphorin-plexin repulsive axon guidance during axonal pathfinding in the Drosophila neuromuscular system. In addition, MICAL functions to interact with Rab13 and Rab8 to coordinate the assembly of tight junctions and adherens junctions in epithelial cells. Thus, MICAL is also called junctional Rab13-binding protein (JRAB). Members of this family, which includes MICAL-2, MICAL-3, and similar proteins, contain one CH domain. CH domains are actin filament (F-actin) binding motifs. Pssm-ID: 409044 [Multi-domain] Cd Length: 110 Bit Score: 105.12 E-value: 5.61e-26
|
||||||||||||||||||
| CH_CYTS | cd21199 | calponin homology (CH) domain found in the cytospin family; The cytospin family includes ... |
170-273 | 7.43e-26 | ||||||||||||||
calponin homology (CH) domain found in the cytospin family; The cytospin family includes cytospin-A and cytospin-B. Cytospin-A, also called renal carcinoma antigen NY-REN-22, sperm antigen with calponin homology and coiled-coil domains 1-like, or SPECC1-like (SPECC1L) protein, is involved in cytokinesis and spindle organization. It may play a role in actin cytoskeleton organization and microtubule stabilization and hence, is required for proper cell adhesion and migration. Cytospin-B, also called nuclear structure protein 5 (NSP5), sperm antigen HCMOGT-1, or sperm antigen with calponin homology and coiled-coil domains 1 (SPECC1), is a novel fusion partner to PDGFRB in juvenile myelomonocytic leukemia with translocation t(5;17)(q33;p11.2). Members of this family contain a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs. Pssm-ID: 409048 Cd Length: 112 Bit Score: 104.75 E-value: 7.43e-26
|
||||||||||||||||||
| CH_dFLNA-like_rpt1 | cd21311 | first calponin homology (CH) domain found in Drosophila melanogaster filamin-A (dFLNA) and ... |
49-155 | 1.23e-25 | ||||||||||||||
first calponin homology (CH) domain found in Drosophila melanogaster filamin-A (dFLNA) and similar proteins; Drosophila melanogaster filamin-A (dFLNA or dFLN-A), also called actin-binding protein 280 (ABP-280) or filamin-1, is involved in germline ring canal formation. It may tether actin microfilaments within the ovarian ring canal to the cell membrane and contributes to actin microfilament organization. dFLNA contains two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs. Pssm-ID: 409160 Cd Length: 124 Bit Score: 104.84 E-value: 1.23e-25
|
||||||||||||||||||
| SPEC | smart00150 | Spectrin repeats; |
1548-1648 | 3.12e-25 | ||||||||||||||
Spectrin repeats; Pssm-ID: 197544 [Multi-domain] Cd Length: 101 Bit Score: 102.79 E-value: 3.12e-25
|
||||||||||||||||||
| CH_FLN-like_rpt1 | cd21183 | first calponin homology (CH) domain found in the filamin family; The filamin family includes ... |
51-153 | 4.52e-25 | ||||||||||||||
first calponin homology (CH) domain found in the filamin family; The filamin family includes filamin-A (FLN-A), filamin-B (FLN-B) and filamin-C (FLN-C). Filamins function to anchor various transmembrane proteins to the actin cytoskeleton. FLN-A is also called actin-binding protein 280 (ABP-280), alpha-filamin, endothelial actin-binding protein, filamin-1, or non-muscle filamin. It promotes orthogonal branching of actin filaments and links actin filaments to membrane glycoproteins. It also serves as a scaffold for a wide range of cytoplasmic signaling proteins. FLN-B is also called ABP-278, ABP-280 homolog, actin-binding-like protein, beta-filamin, filamin homolog 1 (Fh1), filamin-3, thyroid autoantigen, truncated actin-binding protein, or truncated ABP. It connects cell membrane constituents to the actin cytoskeleton and may also promote orthogonal branching of actin filaments as well as link actin filaments to membrane glycoproteins. FLN-C, also called FLNc, ABP-280-like protein, ABP-L, actin-binding-like protein, filamin-2, or gamma-filamin, is a muscle-specific filamin that plays a central role in muscle cells, probably by functioning as a large actin-cross-linking protein. It may be involved in reorganizing the actin cytoskeleton in response to signaling events, and may also display structural functions at the Z lines in muscle cells. FLN-C is critical for normal myogenesis and for maintaining the structural integrity of the muscle fibers. This family also includes Drosophila melanogaster protein jitterbug (Jbug), which is an actin-meshwork organizing protein containing three copies of the CH domain. Other members of this family contain two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs. Pssm-ID: 409032 Cd Length: 108 Bit Score: 102.56 E-value: 4.52e-25
|
||||||||||||||||||
| CH_CLMN_rpt2 | cd21245 | second calponin homology (CH) domain found in calmin and similar proteins; Calmin, also called ... |
169-274 | 6.44e-25 | ||||||||||||||
second calponin homology (CH) domain found in calmin and similar proteins; Calmin, also called calponin-like transmembrane domain protein, is a protein with calponin homology (CH) and transmembrane domains expressed in maturing spermatogenic cells. It may be involved in the development and/or maintenance of neuronal functions. Calmin contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs. Pssm-ID: 409094 Cd Length: 106 Bit Score: 101.79 E-value: 6.44e-25
|
||||||||||||||||||
| CH_EHBP1 | cd21254 | calponin homology (CH) domain found in EH domain-binding protein 1 and similar proteins; EHBP1 ... |
170-274 | 1.48e-24 | ||||||||||||||
calponin homology (CH) domain found in EH domain-binding protein 1 and similar proteins; EHBP1 is a regulator of endocytic recycling and may play a role in actin reorganization by linking clathrin-mediated endocytosis to the actin cytoskeleton. It may act as an effector of small GTPases, including RAB-10 (Rab10), and play a role in vesicle trafficking. EHBP1 is associated with aggressive prostate cancer and insulin-stimulated trafficking and cell migration. Members of this subfamily contain a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs. Pssm-ID: 409103 Cd Length: 107 Bit Score: 101.08 E-value: 1.48e-24
|
||||||||||||||||||
| CH_MICAL3 | cd21251 | calponin homology (CH) domain found in molecule interacting with CasL protein 3; MICAL-3 is a ... |
175-273 | 2.75e-24 | ||||||||||||||
calponin homology (CH) domain found in molecule interacting with CasL protein 3; MICAL-3 is a [F-actin]-monooxygenase that promotes depolymerization of F-actin by mediating oxidation of specific methionine residues on actin to form methionine-sulfoxide, resulting in actin filament disassembly and preventing repolymerization. In the absence of actin, it also functions as a NADPH oxidase producing H(2)O(2). MICAL-3 seems to act as a Rab effector protein and plays a role in vesicle trafficking. It is involved in exocytic vesicle tethering and fusion. MICAL3 contains a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs. Pssm-ID: 409100 [Multi-domain] Cd Length: 111 Bit Score: 100.41 E-value: 2.75e-24
|
||||||||||||||||||
| CH_CYTSB | cd21257 | calponin homology (CH) domain found in cytospin-B; Cytospin-B, also called nuclear structure ... |
170-273 | 5.55e-24 | ||||||||||||||
calponin homology (CH) domain found in cytospin-B; Cytospin-B, also called nuclear structure protein 5 (NSP5), or sperm antigen HCMOGT-1, or sperm antigen with calponin homology and coiled-coil domains 1 (SPECC1), is a novel fusion Cytospin-B that contains a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs. Pssm-ID: 409106 Cd Length: 112 Bit Score: 99.72 E-value: 5.55e-24
|
||||||||||||||||||
| SPEC | smart00150 | Spectrin repeats; |
1443-1541 | 5.59e-24 | ||||||||||||||
Spectrin repeats; Pssm-ID: 197544 [Multi-domain] Cd Length: 101 Bit Score: 98.94 E-value: 5.59e-24
|
||||||||||||||||||
| CH_MICAL2 | cd21250 | calponin homology (CH) domain found in molecule interacting with CasL protein 2; MICAL-2 is a ... |
175-275 | 6.32e-24 | ||||||||||||||
calponin homology (CH) domain found in molecule interacting with CasL protein 2; MICAL-2 is a nuclear [F-actin]-monooxygenase that promotes depolymerization of F-actin by mediating oxidation of specific methionine residues on actin to form methionine-sulfoxide, resulting in actin filament disassembly and preventing repolymerization. In the absence of actin, it also functions as a NADPH oxidase producing H(2)O(2). MICAL-2 acts as a key regulator of the serum response factor (SRF) signaling pathway elicited by nerve growth factor and serum. It mediates oxidation and subsequent depolymerization of nuclear actin, leading to the increased MKL1/MRTF-A presence in the nucleus, promoting SRF:MKL1/MRTF-A-dependent gene transcription. MICAL-2 contains a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs. Pssm-ID: 409099 [Multi-domain] Cd Length: 110 Bit Score: 99.18 E-value: 6.32e-24
|
||||||||||||||||||
| CH_EHBP1L1 | cd21255 | calponin homology (CH) domain found in EH domain-binding protein 1-like protein 1 and similar ... |
170-266 | 7.75e-24 | ||||||||||||||
calponin homology (CH) domain found in EH domain-binding protein 1-like protein 1 and similar proteins; EHBP1L1 may act as Rab effector protein and play a role in vesicle trafficking. It coordinates Rab8 and Bin1 to regulate apical-directed transport in polarized epithelial cells. Members of this subfamily contain a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs. Pssm-ID: 409104 Cd Length: 105 Bit Score: 98.71 E-value: 7.75e-24
|
||||||||||||||||||
| CH_FLN_rpt1 | cd21228 | first calponin homology (CH) domain found in filamins; The filamin family includes filamin-A ... |
51-153 | 1.07e-23 | ||||||||||||||
first calponin homology (CH) domain found in filamins; The filamin family includes filamin-A (FLN-A), filamin-B (FLN-B) and filamin-C (FLN-C). Filamins function to anchor various transmembrane proteins to the actin cytoskeleton. FLN-A is also called actin-binding protein 280 (ABP-280), alpha-filamin, endothelial actin-binding protein, filamin-1, or non-muscle filamin. It promotes orthogonal branching of actin filaments and links actin filaments to membrane glycoproteins. It also serves as a scaffold for a wide range of cytoplasmic signaling proteins. FLN-B is also called ABP-278, ABP-280 homolog, actin-binding-like protein, beta-filamin, filamin homolog 1 (Fh1), filamin-3, thyroid autoantigen, truncated actin-binding protein, or truncated ABP. It connects cell membrane constituents to the actin cytoskeleton and may also promote orthogonal branching of actin filaments as well as link actin filaments to membrane glycoproteins. FLN-C, also called FLNc, ABP-280-like protein, ABP-L, actin-binding-like protein, filamin-2, or gamma-filamin, is a muscle-specific filamin that plays a central role in muscle cells, probably by functioning as a large actin-cross-linking protein. It may be involved in reorganizing the actin cytoskeleton in response to signaling events, and may also display structural functions at the Z lines in muscle cells. FLN-C is critical for normal myogenesis and for maintaining the structural integrity of the muscle fibers. Members of this family contain two copies of the CH domain. The model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs. Pssm-ID: 409077 Cd Length: 108 Bit Score: 98.71 E-value: 1.07e-23
|
||||||||||||||||||
| Spectrin | pfam00435 | Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ... |
1545-1649 | 1.32e-23 | ||||||||||||||
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in cytoskeletal structure. These include spectrin, alpha-actinin and dystrophin. The sequence repeat used in this family is taken from the structural repeat in reference. The spectrin domain- repeat forms a three helix bundle. The second helix is interrupted by proline in some sequences. The repeats are defined by a characteriztic tryptophan (W) residue at position 17 in helix A and a leucine (L) at 2 residues from the carboxyl end of helix C. Although the domain occurs in multiple repeats along sequences, the domains are actually stable on their own - ie they act, biophysically, like domains rather than repeats that along function when aggregated. Pssm-ID: 395348 [Multi-domain] Cd Length: 105 Bit Score: 98.16 E-value: 1.32e-23
|
||||||||||||||||||
| Spectrin | pfam00435 | Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ... |
1439-1543 | 5.71e-23 | ||||||||||||||
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in cytoskeletal structure. These include spectrin, alpha-actinin and dystrophin. The sequence repeat used in this family is taken from the structural repeat in reference. The spectrin domain- repeat forms a three helix bundle. The second helix is interrupted by proline in some sequences. The repeats are defined by a characteriztic tryptophan (W) residue at position 17 in helix A and a leucine (L) at 2 residues from the carboxyl end of helix C. Although the domain occurs in multiple repeats along sequences, the domains are actually stable on their own - ie they act, biophysically, like domains rather than repeats that along function when aggregated. Pssm-ID: 395348 [Multi-domain] Cd Length: 105 Bit Score: 96.23 E-value: 5.71e-23
|
||||||||||||||||||
| CH_SMTNB | cd21259 | calponin homology (CH) domain found in smoothelin-B and similar proteins; Smoothelins are ... |
170-270 | 1.43e-22 | ||||||||||||||
calponin homology (CH) domain found in smoothelin-B and similar proteins; Smoothelins are actin-binding cytoskeletal proteins that are abundantly expressed in healthy visceral (smoothelin-A) and vascular (smoothelin-B) smooth muscle. The human SMTN gene encodes smoothelin-A and smoothelin-B. This model corresponds to the single CH domain of smoothelin-B. CH domains are actin filament (F-actin) binding motifs. Pssm-ID: 409108 Cd Length: 112 Bit Score: 95.44 E-value: 1.43e-22
|
||||||||||||||||||
| CH_SMTNA | cd21258 | calponin homology (CH) domain found in smoothelin-A and similar proteins; Smoothelins are ... |
170-275 | 2.56e-22 | ||||||||||||||
calponin homology (CH) domain found in smoothelin-A and similar proteins; Smoothelins are actin-binding cytoskeletal proteins that are abundantly expressed in healthy visceral (smoothelin-A) and vascular (smoothelin-B) smooth muscle. This model corresponds to the single CH domain of smoothelin-A. CH domains are actin filament (F-actin) binding motifs. Pssm-ID: 409107 Cd Length: 111 Bit Score: 94.73 E-value: 2.56e-22
|
||||||||||||||||||
| CH | smart00033 | Calponin homology domain; Actin binding domains present in duplicate at the N-termini of ... |
173-267 | 3.06e-22 | ||||||||||||||
Calponin homology domain; Actin binding domains present in duplicate at the N-termini of spectrin-like proteins (including dystrophin, alpha-actinin). These domains cross-link actin filaments into bundles and networks. A calponin homology domain is predicted in yeasst Cdc24p. Pssm-ID: 214479 [Multi-domain] Cd Length: 101 Bit Score: 93.92 E-value: 3.06e-22
|
||||||||||||||||||
| CH_FLN-like_rpt2 | cd21184 | second calponin homology (CH) domain found in the filamin family; The filamin family includes ... |
170-272 | 5.70e-22 | ||||||||||||||
second calponin homology (CH) domain found in the filamin family; The filamin family includes filamin-A (FLN-A), filamin-B (FLN-B) and filamin-C (FLN-C). Filamins function to anchor various transmembrane proteins to the actin cytoskeleton. FLN-A is also called actin-binding protein 280 (ABP-280), alpha-filamin, endothelial actin-binding protein, filamin-1, or non-muscle filamin. It promotes orthogonal branching of actin filaments and links actin filaments to membrane glycoproteins. It also serves as a scaffold for a wide range of cytoplasmic signaling proteins. FLN-B is also called ABP-278, ABP-280 homolog, actin-binding-like protein, beta-filamin, filamin homolog 1 (Fh1), filamin-3, thyroid autoantigen, truncated actin-binding protein, or truncated ABP. It connects cell membrane constituents to the actin cytoskeleton and may also promote orthogonal branching of actin filaments as well as link actin filaments to membrane glycoproteins. FLN-C, also called FLNc, ABP-280-like protein, ABP-L, actin-binding-like protein, filamin-2, or gamma-filamin, is a muscle-specific filamin that plays a central role in muscle cells, probably by functioning as a large actin-cross-linking protein. It may be involved in reorganizing the actin cytoskeleton in response to signaling events, and may also display structural functions at the Z lines in muscle cells. FLN-C is critical for normal myogenesis and for maintaining the structural integrity of the muscle fibers. This family also includes Drosophila melanogaster protein jitterbug (Jbug), which is an actin-meshwork organizing protein containing three copies of the CH domain. Other members of this family contain two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs. Pssm-ID: 409033 Cd Length: 103 Bit Score: 93.46 E-value: 5.70e-22
|
||||||||||||||||||
| Spectrin | pfam00435 | Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ... |
741-843 | 1.10e-21 | ||||||||||||||
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in cytoskeletal structure. These include spectrin, alpha-actinin and dystrophin. The sequence repeat used in this family is taken from the structural repeat in reference. The spectrin domain- repeat forms a three helix bundle. The second helix is interrupted by proline in some sequences. The repeats are defined by a characteriztic tryptophan (W) residue at position 17 in helix A and a leucine (L) at 2 residues from the carboxyl end of helix C. Although the domain occurs in multiple repeats along sequences, the domains are actually stable on their own - ie they act, biophysically, like domains rather than repeats that along function when aggregated. Pssm-ID: 395348 [Multi-domain] Cd Length: 105 Bit Score: 92.77 E-value: 1.10e-21
|
||||||||||||||||||
| CH_FLNC_rpt1 | cd21310 | first calponin homology (CH) domain found in filamin-C (FLN-C) and similar proteins; Filamin-C ... |
51-155 | 1.23e-21 | ||||||||||||||
first calponin homology (CH) domain found in filamin-C (FLN-C) and similar proteins; Filamin-C (FLN-C), also called FLNc, ABP-280-like protein, ABP-L, actin-binding-like protein, filamin-2, or gamma-filamin, is a muscle-specific filamin that plays a central role in muscle cells, probably by functioning as a large actin-cross-linking protein. It may be involved in reorganizing the actin cytoskeleton in response to signaling events, and may also display structural functions at the Z lines in muscle cells. FLN-C is critical for normal myogenesis and for maintaining the structural integrity of the muscle fibers. FLN-C contains two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs. Pssm-ID: 409159 Cd Length: 125 Bit Score: 93.17 E-value: 1.23e-21
|
||||||||||||||||||
| SPEC | smart00150 | Spectrin repeats; |
848-948 | 1.30e-21 | ||||||||||||||
Spectrin repeats; Pssm-ID: 197544 [Multi-domain] Cd Length: 101 Bit Score: 92.39 E-value: 1.30e-21
|
||||||||||||||||||
| CH_CYTSA | cd21256 | calponin homology (CH) domain found in cytospin-A; Cytospin-A, also called renal carcinoma ... |
170-273 | 2.19e-21 | ||||||||||||||
calponin homology (CH) domain found in cytospin-A; Cytospin-A, also called renal carcinoma antigen NY-REN-22, or sperm antigen with calponin homology and coiled-coil domains 1-like, or SPECC1-like protein (SPECC1L), is involved in cytokinesis and spindle organization. It may play a role in actin cytoskeleton organization and microtubule stabilization and hence, is required for proper cell adhesion and migration. Cytospin-A contains a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs. Pssm-ID: 409105 Cd Length: 119 Bit Score: 92.44 E-value: 2.19e-21
|
||||||||||||||||||
| CH_SMTNL2 | cd21261 | calponin homology (CH) domain found in smoothelin-like protein 2; Smoothelin-like protein 2 ... |
170-273 | 4.31e-21 | ||||||||||||||
calponin homology (CH) domain found in smoothelin-like protein 2; Smoothelin-like protein 2 (SMTNL2) is highly expressed in skeletal muscle and could be associated with differentiating myocytes. It contains a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs. Pssm-ID: 409110 Cd Length: 107 Bit Score: 91.18 E-value: 4.31e-21
|
||||||||||||||||||
| CH_SMTNL1 | cd21260 | calponin homology (CH) domain found in smoothelin-like protein 1; Smoothelin-like protein 1 ... |
172-270 | 4.44e-21 | ||||||||||||||
calponin homology (CH) domain found in smoothelin-like protein 1; Smoothelin-like protein 1 (SMTNL1), also called calponin homology-associated smooth muscle protein (CHASM), plays a role in the regulation of contractile properties of both striated and smooth muscles. It can bind to calmodulin and tropomyosin. When it is unphosphorylated, SMTNL1 may inhibit myosin dephosphorylation. SMTNL1 contains a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs. Pssm-ID: 409109 Cd Length: 116 Bit Score: 91.30 E-value: 4.44e-21
|
||||||||||||||||||
| CH_NAV2-like | cd21212 | calponin homology (CH) domain found in neuron navigator (NAV) 2, NAV3, and similar proteins; ... |
52-153 | 5.17e-21 | ||||||||||||||
calponin homology (CH) domain found in neuron navigator (NAV) 2, NAV3, and similar proteins; This family includes neuron navigator 2 (NAV2) and NAV3, both of which contain a single copy of the CH domain at the N-terminus. CH domains are actin filament (F-actin) binding motifs. NAV2, also called helicase APC down-regulated 1 (HELAD1), pore membrane and/or filament-interacting-like protein 2 (POMFIL2), retinoic acid inducible in neuroblastoma 1 (RAINB1), Steerin-2 (STEERIN2), or Unc-53 homolog 2 (unc53H2), possesses 3' to 5' helicase activity and exonuclease activity. It is involved in neuronal development, specifically in the development of different sensory organs. NAV3, also called pore membrane and/or filament-interacting-like protein 1 (POMFIL1), Steerin-3 (STEERIN3), or Unc-53 homolog 3 (unc53H3), may regulate IL2 production by T-cells. It may be involved in neuron regeneration. Pssm-ID: 409061 Cd Length: 105 Bit Score: 90.72 E-value: 5.17e-21
|
||||||||||||||||||
| SPEC | smart00150 | Spectrin repeats; |
743-841 | 5.77e-21 | ||||||||||||||
Spectrin repeats; Pssm-ID: 197544 [Multi-domain] Cd Length: 101 Bit Score: 90.47 E-value: 5.77e-21
|
||||||||||||||||||
| CH | pfam00307 | Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal ... |
50-155 | 7.69e-21 | ||||||||||||||
Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal transduction proteins. The CH domain is involved in actin binding in some members of the family. However in calponins there is evidence that the CH domain is not involved in its actin binding activity. Most member proteins have from two to four copies of the CH domain, however some proteins such as calponin have only a single copy. Pssm-ID: 425596 [Multi-domain] Cd Length: 109 Bit Score: 90.42 E-value: 7.69e-21
|
||||||||||||||||||
| SPEC | smart00150 | Spectrin repeats; |
1868-1967 | 1.13e-20 | ||||||||||||||
Spectrin repeats; Pssm-ID: 197544 [Multi-domain] Cd Length: 101 Bit Score: 89.70 E-value: 1.13e-20
|
||||||||||||||||||
| SPEC | smart00150 | Spectrin repeats; |
1656-1755 | 1.94e-20 | ||||||||||||||
Spectrin repeats; Pssm-ID: 197544 [Multi-domain] Cd Length: 101 Bit Score: 88.93 E-value: 1.94e-20
|
||||||||||||||||||
| CH_FLNB_rpt1 | cd21309 | first calponin homology (CH) domain found in filamin-B (FLN-B) and similar proteins; Filamin-B ... |
51-155 | 2.11e-20 | ||||||||||||||
first calponin homology (CH) domain found in filamin-B (FLN-B) and similar proteins; Filamin-B (FLN-B) is also called ABP-278, ABP-280 homolog, actin-binding-like protein, beta-filamin, filamin homolog 1 (Fh1), filamin-3, thyroid autoantigen, truncated actin-binding protein, or truncated ABP. It connects cell membrane constituents to the actin cytoskeleton. It may promote orthogonal branching of actin filaments and links actin filaments to membrane glycoproteins. It anchors various transmembrane proteins to the actin cytoskeleton. FLN-B contains two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs. Pssm-ID: 409158 Cd Length: 131 Bit Score: 90.14 E-value: 2.11e-20
|
||||||||||||||||||
| Spectrin | pfam00435 | Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ... |
1651-1756 | 2.76e-20 | ||||||||||||||
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in cytoskeletal structure. These include spectrin, alpha-actinin and dystrophin. The sequence repeat used in this family is taken from the structural repeat in reference. The spectrin domain- repeat forms a three helix bundle. The second helix is interrupted by proline in some sequences. The repeats are defined by a characteriztic tryptophan (W) residue at position 17 in helix A and a leucine (L) at 2 residues from the carboxyl end of helix C. Although the domain occurs in multiple repeats along sequences, the domains are actually stable on their own - ie they act, biophysically, like domains rather than repeats that along function when aggregated. Pssm-ID: 395348 [Multi-domain] Cd Length: 105 Bit Score: 88.53 E-value: 2.76e-20
|
||||||||||||||||||
| Spectrin | pfam00435 | Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ... |
1865-1967 | 2.81e-20 | ||||||||||||||
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in cytoskeletal structure. These include spectrin, alpha-actinin and dystrophin. The sequence repeat used in this family is taken from the structural repeat in reference. The spectrin domain- repeat forms a three helix bundle. The second helix is interrupted by proline in some sequences. The repeats are defined by a characteriztic tryptophan (W) residue at position 17 in helix A and a leucine (L) at 2 residues from the carboxyl end of helix C. Although the domain occurs in multiple repeats along sequences, the domains are actually stable on their own - ie they act, biophysically, like domains rather than repeats that along function when aggregated. Pssm-ID: 395348 [Multi-domain] Cd Length: 105 Bit Score: 88.53 E-value: 2.81e-20
|
||||||||||||||||||
| SPEC | smart00150 | Spectrin repeats; |
422-521 | 3.99e-20 | ||||||||||||||
Spectrin repeats; Pssm-ID: 197544 [Multi-domain] Cd Length: 101 Bit Score: 88.16 E-value: 3.99e-20
|
||||||||||||||||||
| Spectrin | pfam00435 | Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ... |
422-521 | 8.78e-20 | ||||||||||||||
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in cytoskeletal structure. These include spectrin, alpha-actinin and dystrophin. The sequence repeat used in this family is taken from the structural repeat in reference. The spectrin domain- repeat forms a three helix bundle. The second helix is interrupted by proline in some sequences. The repeats are defined by a characteriztic tryptophan (W) residue at position 17 in helix A and a leucine (L) at 2 residues from the carboxyl end of helix C. Although the domain occurs in multiple repeats along sequences, the domains are actually stable on their own - ie they act, biophysically, like domains rather than repeats that along function when aggregated. Pssm-ID: 395348 [Multi-domain] Cd Length: 105 Bit Score: 87.37 E-value: 8.78e-20
|
||||||||||||||||||
| Spectrin | pfam00435 | Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ... |
847-947 | 1.67e-19 | ||||||||||||||
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in cytoskeletal structure. These include spectrin, alpha-actinin and dystrophin. The sequence repeat used in this family is taken from the structural repeat in reference. The spectrin domain- repeat forms a three helix bundle. The second helix is interrupted by proline in some sequences. The repeats are defined by a characteriztic tryptophan (W) residue at position 17 in helix A and a leucine (L) at 2 residues from the carboxyl end of helix C. Although the domain occurs in multiple repeats along sequences, the domains are actually stable on their own - ie they act, biophysically, like domains rather than repeats that along function when aggregated. Pssm-ID: 395348 [Multi-domain] Cd Length: 105 Bit Score: 86.60 E-value: 1.67e-19
|
||||||||||||||||||
| SPEC | smart00150 | Spectrin repeats; |
954-1055 | 3.05e-19 | ||||||||||||||
Spectrin repeats; Pssm-ID: 197544 [Multi-domain] Cd Length: 101 Bit Score: 85.46 E-value: 3.05e-19
|
||||||||||||||||||
| SPEC | smart00150 | Spectrin repeats; |
1761-1861 | 4.95e-19 | ||||||||||||||
Spectrin repeats; Pssm-ID: 197544 [Multi-domain] Cd Length: 101 Bit Score: 85.07 E-value: 4.95e-19
|
||||||||||||||||||
| CH_FLNA_rpt1 | cd21308 | first calponin homology (CH) domain found in filamin-A (FLN-A) and similar proteins; Filamin-A ... |
51-155 | 5.31e-19 | ||||||||||||||
first calponin homology (CH) domain found in filamin-A (FLN-A) and similar proteins; Filamin-A (FLN-A) is also called actin-binding protein 280 (ABP-280), alpha-filamin, endothelial actin-binding protein, filamin-1, or non-muscle filamin. It promotes orthogonal branching of actin filaments and links actin filaments to membrane glycoproteins. It also anchors various transmembrane proteins to the actin cytoskeleton and serves as a scaffold for a wide range of cytoplasmic signaling proteins. FLN-A contains two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs. Pssm-ID: 409157 Cd Length: 129 Bit Score: 85.91 E-value: 5.31e-19
|
||||||||||||||||||
| CH | smart00033 | Calponin homology domain; Actin binding domains present in duplicate at the N-termini of ... |
54-152 | 7.10e-19 | ||||||||||||||
Calponin homology domain; Actin binding domains present in duplicate at the N-termini of spectrin-like proteins (including dystrophin, alpha-actinin). These domains cross-link actin filaments into bundles and networks. A calponin homology domain is predicted in yeasst Cdc24p. Pssm-ID: 214479 [Multi-domain] Cd Length: 101 Bit Score: 84.67 E-value: 7.10e-19
|
||||||||||||||||||
| SPEC | smart00150 | Spectrin repeats; |
1338-1436 | 7.67e-19 | ||||||||||||||
Spectrin repeats; Pssm-ID: 197544 [Multi-domain] Cd Length: 101 Bit Score: 84.30 E-value: 7.67e-19
|
||||||||||||||||||
| SPEC | smart00150 | Spectrin repeats; |
527-631 | 2.97e-18 | ||||||||||||||
Spectrin repeats; Pssm-ID: 197544 [Multi-domain] Cd Length: 101 Bit Score: 82.76 E-value: 2.97e-18
|
||||||||||||||||||
| SPEC | smart00150 | Spectrin repeats; |
1061-1163 | 3.40e-18 | ||||||||||||||
Spectrin repeats; Pssm-ID: 197544 [Multi-domain] Cd Length: 101 Bit Score: 82.76 E-value: 3.40e-18
|
||||||||||||||||||
| SPEC | smart00150 | Spectrin repeats; |
1172-1270 | 4.87e-18 | ||||||||||||||
Spectrin repeats; Pssm-ID: 197544 [Multi-domain] Cd Length: 101 Bit Score: 81.99 E-value: 4.87e-18
|
||||||||||||||||||
| SPEC | cd00176 | Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
301-524 | 6.61e-18 | ||||||||||||||
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here Pssm-ID: 238103 [Multi-domain] Cd Length: 213 Bit Score: 85.58 E-value: 6.61e-18
|
||||||||||||||||||
| Spectrin | pfam00435 | Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ... |
954-1056 | 1.52e-17 | ||||||||||||||
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in cytoskeletal structure. These include spectrin, alpha-actinin and dystrophin. The sequence repeat used in this family is taken from the structural repeat in reference. The spectrin domain- repeat forms a three helix bundle. The second helix is interrupted by proline in some sequences. The repeats are defined by a characteriztic tryptophan (W) residue at position 17 in helix A and a leucine (L) at 2 residues from the carboxyl end of helix C. Although the domain occurs in multiple repeats along sequences, the domains are actually stable on their own - ie they act, biophysically, like domains rather than repeats that along function when aggregated. Pssm-ID: 395348 [Multi-domain] Cd Length: 105 Bit Score: 80.83 E-value: 1.52e-17
|
||||||||||||||||||
| CH_CTX_rpt1 | cd21225 | first calponin homology (CH) domain found in cortexillin; Cortexillins are actin-bundling ... |
49-149 | 2.19e-17 | ||||||||||||||
first calponin homology (CH) domain found in cortexillin; Cortexillins are actin-bundling proteins that play a critical role in regulating cell morphology and actin cytoskeleton reorganization. They play a major role in cytokinesis and contain two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs. Pssm-ID: 409074 Cd Length: 111 Bit Score: 80.65 E-value: 2.19e-17
|
||||||||||||||||||
| Spectrin | pfam00435 | Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ... |
1758-1862 | 6.52e-17 | ||||||||||||||
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in cytoskeletal structure. These include spectrin, alpha-actinin and dystrophin. The sequence repeat used in this family is taken from the structural repeat in reference. The spectrin domain- repeat forms a three helix bundle. The second helix is interrupted by proline in some sequences. The repeats are defined by a characteriztic tryptophan (W) residue at position 17 in helix A and a leucine (L) at 2 residues from the carboxyl end of helix C. Although the domain occurs in multiple repeats along sequences, the domains are actually stable on their own - ie they act, biophysically, like domains rather than repeats that along function when aggregated. Pssm-ID: 395348 [Multi-domain] Cd Length: 105 Bit Score: 78.90 E-value: 6.52e-17
|
||||||||||||||||||
| Spectrin | pfam00435 | Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ... |
524-632 | 7.19e-17 | ||||||||||||||
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in cytoskeletal structure. These include spectrin, alpha-actinin and dystrophin. The sequence repeat used in this family is taken from the structural repeat in reference. The spectrin domain- repeat forms a three helix bundle. The second helix is interrupted by proline in some sequences. The repeats are defined by a characteriztic tryptophan (W) residue at position 17 in helix A and a leucine (L) at 2 residues from the carboxyl end of helix C. Although the domain occurs in multiple repeats along sequences, the domains are actually stable on their own - ie they act, biophysically, like domains rather than repeats that along function when aggregated. Pssm-ID: 395348 [Multi-domain] Cd Length: 105 Bit Score: 78.90 E-value: 7.19e-17
|
||||||||||||||||||
| SMC_prok_B | TIGR02168 | chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
709-1614 | 2.32e-16 | ||||||||||||||
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins] Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 87.03 E-value: 2.32e-16
|
||||||||||||||||||
| LDLa | cd00112 | Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central ... |
3441-3475 | 2.75e-16 | ||||||||||||||
Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central role in mammalian cholesterol metabolism; the receptor protein binds LDL and transports it into cells by endocytosis; 7 successive cysteine-rich repeats of about 40 amino acids are present in the N-terminal of this multidomain membrane protein; other homologous domains occur in related receptors, including the very low-density lipoprotein receptor and the LDL receptor-related protein/alpha 2-macroglobulin receptor, and in proteins which are functionally unrelated, such as the C9 component of complement; the binding of calcium is required for in vitro formation of the native disulfide isomer and is necessary in establishing and maintaining the modular structure Pssm-ID: 238060 Cd Length: 35 Bit Score: 74.94 E-value: 2.75e-16
|
||||||||||||||||||
| SMC_prok_B | TIGR02168 | chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1251-2029 | 2.79e-16 | ||||||||||||||
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins] Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 87.03 E-value: 2.79e-16
|
||||||||||||||||||
| CH_SF | cd00014 | calponin homology (CH) domain superfamily; CH domains are actin filament (F-actin) binding ... |
172-271 | 5.91e-16 | ||||||||||||||
calponin homology (CH) domain superfamily; CH domains are actin filament (F-actin) binding motifs, which may be present as a single copy or in tandem repeats (which increase binding affinity). They either function as autonomous actin binding motifs or serve a regulatory function. CH domains are found in cytoskeletal and signal transduction proteins, including actin-binding proteins like spectrin, alpha-actinin, dystrophin, utrophin, and fimbrin, as well as proteins essential for regulation of cell shape (cortexillins), and signaling proteins (Vav). Pssm-ID: 409031 [Multi-domain] Cd Length: 103 Bit Score: 76.22 E-value: 5.91e-16
|
||||||||||||||||||
| LDLa | cd00112 | Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central ... |
3363-3397 | 6.06e-16 | ||||||||||||||
Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central role in mammalian cholesterol metabolism; the receptor protein binds LDL and transports it into cells by endocytosis; 7 successive cysteine-rich repeats of about 40 amino acids are present in the N-terminal of this multidomain membrane protein; other homologous domains occur in related receptors, including the very low-density lipoprotein receptor and the LDL receptor-related protein/alpha 2-macroglobulin receptor, and in proteins which are functionally unrelated, such as the C9 component of complement; the binding of calcium is required for in vitro formation of the native disulfide isomer and is necessary in establishing and maintaining the modular structure Pssm-ID: 238060 Cd Length: 35 Bit Score: 73.78 E-value: 6.06e-16
|
||||||||||||||||||
| CH_SF | cd00014 | calponin homology (CH) domain superfamily; CH domains are actin filament (F-actin) binding ... |
53-151 | 9.42e-16 | ||||||||||||||
calponin homology (CH) domain superfamily; CH domains are actin filament (F-actin) binding motifs, which may be present as a single copy or in tandem repeats (which increase binding affinity). They either function as autonomous actin binding motifs or serve a regulatory function. CH domains are found in cytoskeletal and signal transduction proteins, including actin-binding proteins like spectrin, alpha-actinin, dystrophin, utrophin, and fimbrin, as well as proteins essential for regulation of cell shape (cortexillins), and signaling proteins (Vav). Pssm-ID: 409031 [Multi-domain] Cd Length: 103 Bit Score: 75.84 E-value: 9.42e-16
|
||||||||||||||||||
| Spectrin | pfam00435 | Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ... |
1338-1436 | 1.65e-15 | ||||||||||||||
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in cytoskeletal structure. These include spectrin, alpha-actinin and dystrophin. The sequence repeat used in this family is taken from the structural repeat in reference. The spectrin domain- repeat forms a three helix bundle. The second helix is interrupted by proline in some sequences. The repeats are defined by a characteriztic tryptophan (W) residue at position 17 in helix A and a leucine (L) at 2 residues from the carboxyl end of helix C. Although the domain occurs in multiple repeats along sequences, the domains are actually stable on their own - ie they act, biophysically, like domains rather than repeats that along function when aggregated. Pssm-ID: 395348 [Multi-domain] Cd Length: 105 Bit Score: 75.05 E-value: 1.65e-15
|
||||||||||||||||||
| CH_MICAL1 | cd21196 | calponin homology (CH) domain found in molecule interacting with CasL protein 1; MICAL-1, also ... |
170-273 | 1.83e-15 | ||||||||||||||
calponin homology (CH) domain found in molecule interacting with CasL protein 1; MICAL-1, also called NEDD9-interacting protein with calponin homology and LIM domains, acts as a [F-actin]-monooxygenase that promotes depolymerization of F-actin by mediating oxidation of specific methionine residues on actin to form methionine-sulfoxide, resulting in actin filament disassembly and preventing repolymerization. In the absence of actin, it also functions as a NADPH oxidase producing H(2)O(2). MICAL-1 acts as a cytoskeletal regulator that connects NEDD9 to intermediate filaments. It also acts as a negative regulator of apoptosis via its interaction with STK38 and STK38L. MICAL-1 is a Rab effector protein that plays a role in vesicle trafficking. It contains a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs. Pssm-ID: 409045 Cd Length: 106 Bit Score: 75.08 E-value: 1.83e-15
|
||||||||||||||||||
| Spectrin | pfam00435 | Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ... |
1059-1163 | 2.18e-15 | ||||||||||||||
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in cytoskeletal structure. These include spectrin, alpha-actinin and dystrophin. The sequence repeat used in this family is taken from the structural repeat in reference. The spectrin domain- repeat forms a three helix bundle. The second helix is interrupted by proline in some sequences. The repeats are defined by a characteriztic tryptophan (W) residue at position 17 in helix A and a leucine (L) at 2 residues from the carboxyl end of helix C. Although the domain occurs in multiple repeats along sequences, the domains are actually stable on their own - ie they act, biophysically, like domains rather than repeats that along function when aggregated. Pssm-ID: 395348 [Multi-domain] Cd Length: 105 Bit Score: 74.66 E-value: 2.18e-15
|
||||||||||||||||||
| PH_ARHGAP21-like | cd01253 | ARHGAP21 and related proteins pleckstrin homology (PH) domain; ARHGAP family genes encode Rho ... |
2194-2287 | 6.66e-15 | ||||||||||||||
ARHGAP21 and related proteins pleckstrin homology (PH) domain; ARHGAP family genes encode Rho/Rac/Cdc42-like GTPase activating proteins with a RhoGAP domain. These proteins functions as a GTPase-activating protein (GAP) for RHOA and CDC42. ARHGAP21 controls the Arp2/3 complex and F-actin dynamics at the Golgi complex by regulating the activity of the small GTPase Cdc42. It is recruited to the Golgi by to GTPase, ARF1, through its PH domain and its helical motif. It is also required for CTNNA1 recruitment to adherens junctions. ARHGAP21 and it related proteins all contains a PH domain and a RhoGAP domain. Some of the members have additional N-terminal domains including PDZ, SH3, and SPEC. The ARHGAP21 PH domain interacts with the GTPbound forms of both ARF1 and ARF6 ARF-binding domain/ArfBD. The members here include: ARHGAP15, ARHGAP21, and ARHGAP23. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes. Pssm-ID: 269955 Cd Length: 113 Bit Score: 73.56 E-value: 6.66e-15
|
||||||||||||||||||
| CH_DIXDC1 | cd21213 | calponin homology (CH) domain found in Dixin and similar proteins; Dixin, also called ... |
52-146 | 9.51e-15 | ||||||||||||||
calponin homology (CH) domain found in Dixin and similar proteins; Dixin, also called coiled-coil protein DIX1, coiled-coil-DIX1, or DIX domain-containing protein 1, is a positive effector of the Wnt signaling pathway. It activates WNT3A signaling via DVL2 and regulates JNK activation by AXIN1 and DVL2. Members of this family contain a single copy of the CH domain at the N-terminus. CH domains are actin filament (F-actin) binding motifs. Pssm-ID: 409062 Cd Length: 107 Bit Score: 73.10 E-value: 9.51e-15
|
||||||||||||||||||
| SMC_prok_B | TIGR02168 | chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
385-1335 | 1.20e-14 | ||||||||||||||
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins] Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 81.64 E-value: 1.20e-14
|
||||||||||||||||||
| LDLa | smart00192 | Low-density lipoprotein receptor domain class A; Cysteine-rich repeat in the low-density ... |
3440-3472 | 1.27e-14 | ||||||||||||||
Low-density lipoprotein receptor domain class A; Cysteine-rich repeat in the low-density lipoprotein (LDL) receptor that plays a central role in mammalian cholesterol metabolism. The N-terminal type A repeats in LDL receptor bind the lipoproteins. Other homologous domains occur in related receptors, including the very low-density lipoprotein receptor and the LDL receptor-related protein/alpha 2-macroglobulin receptor, and in proteins which are functionally unrelated, such as the C9 component of complement. Mutations in the LDL receptor gene cause familial hypercholesterolemia. Pssm-ID: 197566 Cd Length: 33 Bit Score: 69.97 E-value: 1.27e-14
|
||||||||||||||||||
| LDLa | smart00192 | Low-density lipoprotein receptor domain class A; Cysteine-rich repeat in the low-density ... |
3362-3394 | 1.79e-14 | ||||||||||||||
Low-density lipoprotein receptor domain class A; Cysteine-rich repeat in the low-density lipoprotein (LDL) receptor that plays a central role in mammalian cholesterol metabolism. The N-terminal type A repeats in LDL receptor bind the lipoproteins. Other homologous domains occur in related receptors, including the very low-density lipoprotein receptor and the LDL receptor-related protein/alpha 2-macroglobulin receptor, and in proteins which are functionally unrelated, such as the C9 component of complement. Mutations in the LDL receptor gene cause familial hypercholesterolemia. Pssm-ID: 197566 Cd Length: 33 Bit Score: 69.58 E-value: 1.79e-14
|
||||||||||||||||||
| LDLa | cd00112 | Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central ... |
3484-3518 | 3.40e-14 | ||||||||||||||
Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central role in mammalian cholesterol metabolism; the receptor protein binds LDL and transports it into cells by endocytosis; 7 successive cysteine-rich repeats of about 40 amino acids are present in the N-terminal of this multidomain membrane protein; other homologous domains occur in related receptors, including the very low-density lipoprotein receptor and the LDL receptor-related protein/alpha 2-macroglobulin receptor, and in proteins which are functionally unrelated, such as the C9 component of complement; the binding of calcium is required for in vitro formation of the native disulfide isomer and is necessary in establishing and maintaining the modular structure Pssm-ID: 238060 Cd Length: 35 Bit Score: 69.16 E-value: 3.40e-14
|
||||||||||||||||||
| Ldl_recept_a | pfam00057 | Low-density lipoprotein receptor domain class A; |
3483-3518 | 4.17e-14 | ||||||||||||||
Low-density lipoprotein receptor domain class A; Pssm-ID: 395011 Cd Length: 37 Bit Score: 68.81 E-value: 4.17e-14
|
||||||||||||||||||
| CH_FLN_rpt2 | cd21230 | second calponin homology (CH) domain found in filamins; The filamin family includes filamin-A ... |
170-277 | 4.52e-14 | ||||||||||||||
second calponin homology (CH) domain found in filamins; The filamin family includes filamin-A (FLN-A), filamin-B (FLN-B) and filamin-C (FLN-C). Filamins function to anchor various transmembrane proteins to the actin cytoskeleton. FLN-A is also called actin-binding protein 280 (ABP-280), alpha-filamin, endothelial actin-binding protein, filamin-1, or non-muscle filamin. It promotes orthogonal branching of actin filaments and links actin filaments to membrane glycoproteins. It also serves as a scaffold for a wide range of cytoplasmic signaling proteins. FLN-B is also called ABP-278, ABP-280 homolog, actin-binding-like protein, beta-filamin, filamin homolog 1 (Fh1), filamin-3, thyroid autoantigen, truncated actin-binding protein, or truncated ABP. It connects cell membrane constituents to the actin cytoskeleton and may also promote orthogonal branching of actin filaments as well as link actin filaments to membrane glycoproteins. FLN-C, also called FLNc, ABP-280-like protein, ABP-L, actin-binding-like protein, filamin-2, or gamma-filamin, is a muscle-specific filamin that plays a central role in muscle cells, probably by functioning as a large actin-cross-linking protein. It may be involved in reorganizing the actin cytoskeleton in response to signaling events, and may also display structural functions at the Z lines in muscle cells. FLN-C is critical for normal myogenesis and for maintaining the structural integrity of the muscle fibers. Members of this family contain two copies of the CH domain. The model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs. Pssm-ID: 409079 Cd Length: 103 Bit Score: 70.87 E-value: 4.52e-14
|
||||||||||||||||||
| Ldl_recept_a | pfam00057 | Low-density lipoprotein receptor domain class A; |
3361-3397 | 7.95e-14 | ||||||||||||||
Low-density lipoprotein receptor domain class A; Pssm-ID: 395011 Cd Length: 37 Bit Score: 68.04 E-value: 7.95e-14
|
||||||||||||||||||
| CH_jitterbug-like_rpt2 | cd21229 | second calponin homology (CH) domain found in Drosophila melanogaster protein jitterbug and ... |
172-279 | 8.63e-14 | ||||||||||||||
second calponin homology (CH) domain found in Drosophila melanogaster protein jitterbug and similar proteins; Protein jitterbug (Jbug) is an actin-meshwork organizing protein. It is required to maintain the shape and cell orientation of the Drosophila notum epithelium during flight muscle attachment to tendon cells. Jbug contains three copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs. Pssm-ID: 409078 Cd Length: 105 Bit Score: 70.11 E-value: 8.63e-14
|
||||||||||||||||||
| FN3 | COG3401 | Fibronectin type 3 domain [General function prediction only]; |
3766-4135 | 1.20e-13 | ||||||||||||||
Fibronectin type 3 domain [General function prediction only]; Pssm-ID: 442628 [Multi-domain] Cd Length: 603 Bit Score: 77.35 E-value: 1.20e-13
|
||||||||||||||||||
| Ldl_recept_a | pfam00057 | Low-density lipoprotein receptor domain class A; |
3440-3475 | 1.46e-13 | ||||||||||||||
Low-density lipoprotein receptor domain class A; Pssm-ID: 395011 Cd Length: 37 Bit Score: 67.27 E-value: 1.46e-13
|
||||||||||||||||||
| Spectrin | pfam00435 | Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ... |
1970-2029 | 3.14e-13 | ||||||||||||||
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in cytoskeletal structure. These include spectrin, alpha-actinin and dystrophin. The sequence repeat used in this family is taken from the structural repeat in reference. The spectrin domain- repeat forms a three helix bundle. The second helix is interrupted by proline in some sequences. The repeats are defined by a characteriztic tryptophan (W) residue at position 17 in helix A and a leucine (L) at 2 residues from the carboxyl end of helix C. Although the domain occurs in multiple repeats along sequences, the domains are actually stable on their own - ie they act, biophysically, like domains rather than repeats that along function when aggregated. Pssm-ID: 395348 [Multi-domain] Cd Length: 105 Bit Score: 68.50 E-value: 3.14e-13
|
||||||||||||||||||
| LDLa | smart00192 | Low-density lipoprotein receptor domain class A; Cysteine-rich repeat in the low-density ... |
3483-3515 | 3.25e-13 | ||||||||||||||
Low-density lipoprotein receptor domain class A; Cysteine-rich repeat in the low-density lipoprotein (LDL) receptor that plays a central role in mammalian cholesterol metabolism. The N-terminal type A repeats in LDL receptor bind the lipoproteins. Other homologous domains occur in related receptors, including the very low-density lipoprotein receptor and the LDL receptor-related protein/alpha 2-macroglobulin receptor, and in proteins which are functionally unrelated, such as the C9 component of complement. Mutations in the LDL receptor gene cause familial hypercholesterolemia. Pssm-ID: 197566 Cd Length: 33 Bit Score: 66.12 E-value: 3.25e-13
|
||||||||||||||||||
| LDLa | cd00112 | Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central ... |
3633-3667 | 4.26e-13 | ||||||||||||||
Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central role in mammalian cholesterol metabolism; the receptor protein binds LDL and transports it into cells by endocytosis; 7 successive cysteine-rich repeats of about 40 amino acids are present in the N-terminal of this multidomain membrane protein; other homologous domains occur in related receptors, including the very low-density lipoprotein receptor and the LDL receptor-related protein/alpha 2-macroglobulin receptor, and in proteins which are functionally unrelated, such as the C9 component of complement; the binding of calcium is required for in vitro formation of the native disulfide isomer and is necessary in establishing and maintaining the modular structure Pssm-ID: 238060 Cd Length: 35 Bit Score: 65.69 E-value: 4.26e-13
|
||||||||||||||||||
| CH_PLS_FIM_rpt3 | cd21219 | third calponin homology (CH) domain found in the plastin/fimbrin family; This family includes ... |
45-155 | 4.31e-13 | ||||||||||||||
third calponin homology (CH) domain found in the plastin/fimbrin family; This family includes plastin and fimbrin. Plastin has three isoforms, plastin-1, -2, and -3. Plastin-1, also called intestine-specific plastin, or I-plastin, is an actin-bundling protein in the absence of calcium. Plastin-2, also called L-plastin, or LC64P, or lymphocyte cytosolic protein 1 (LCP-1), is an actin-binding protein that plays a role in the activation of T-cells in response to costimulation through TCR/CD3 and CD2 or CD28. It modulates the cell surface expression of IL2RA/CD25 and CD69. Plastin-3, also called T-plastin, is an actin-bundling protein found in intestinal microvilli, hair cell stereocilia, and fibroblast filopodia. It may play a role in the regulation of bone development. Fimbrin has been found in plants and fungi. Arabidopsis thaliana fimbrin (AtFIM) includes fimbrin-1, -2, -3, -4, and -5, which cross-link actin filaments (F-actin) in a calcium independent manner. They stabilize and prevent F-actin depolymerization mediated by profilin. They act as key regulators of actin cytoarchitecture, probably involved in cell cycle, cell division, cell elongation and cytoplasmic tractus. AtFIM5 is an actin bundling factor that is required for pollen germination and pollen tube growth. Fungal fimbrin binds to actin, and functionally associates with actin structures involved in the development and maintenance of cell polarity. Members of this family contain four copies of the CH domain. This model corresponds to the third CH domain. CH domains are actin filament (F-actin) binding motifs. Pssm-ID: 409068 Cd Length: 113 Bit Score: 68.46 E-value: 4.31e-13
|
||||||||||||||||||
| Ldl_recept_a | pfam00057 | Low-density lipoprotein receptor domain class A; |
3633-3667 | 4.74e-13 | ||||||||||||||
Low-density lipoprotein receptor domain class A; Pssm-ID: 395011 Cd Length: 37 Bit Score: 65.73 E-value: 4.74e-13
|
||||||||||||||||||
| SPEC | smart00150 | Spectrin repeats; |
1973-2032 | 7.74e-13 | ||||||||||||||
Spectrin repeats; Pssm-ID: 197544 [Multi-domain] Cd Length: 101 Bit Score: 67.35 E-value: 7.74e-13
|
||||||||||||||||||
| PH_9 | pfam15410 | Pleckstrin homology domain; This Pleckstrin homology domain is found in some fungal species. |
2196-2291 | 2.54e-12 | ||||||||||||||
Pleckstrin homology domain; This Pleckstrin homology domain is found in some fungal species. Pssm-ID: 434701 Cd Length: 118 Bit Score: 66.30 E-value: 2.54e-12
|
||||||||||||||||||
| LDLa | cd00112 | Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central ... |
3523-3561 | 7.44e-12 | ||||||||||||||
Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central role in mammalian cholesterol metabolism; the receptor protein binds LDL and transports it into cells by endocytosis; 7 successive cysteine-rich repeats of about 40 amino acids are present in the N-terminal of this multidomain membrane protein; other homologous domains occur in related receptors, including the very low-density lipoprotein receptor and the LDL receptor-related protein/alpha 2-macroglobulin receptor, and in proteins which are functionally unrelated, such as the C9 component of complement; the binding of calcium is required for in vitro formation of the native disulfide isomer and is necessary in establishing and maintaining the modular structure Pssm-ID: 238060 Cd Length: 35 Bit Score: 62.22 E-value: 7.44e-12
|
||||||||||||||||||
| LDLa | smart00192 | Low-density lipoprotein receptor domain class A; Cysteine-rich repeat in the low-density ... |
3633-3664 | 7.46e-12 | ||||||||||||||
Low-density lipoprotein receptor domain class A; Cysteine-rich repeat in the low-density lipoprotein (LDL) receptor that plays a central role in mammalian cholesterol metabolism. The N-terminal type A repeats in LDL receptor bind the lipoproteins. Other homologous domains occur in related receptors, including the very low-density lipoprotein receptor and the LDL receptor-related protein/alpha 2-macroglobulin receptor, and in proteins which are functionally unrelated, such as the C9 component of complement. Mutations in the LDL receptor gene cause familial hypercholesterolemia. Pssm-ID: 197566 Cd Length: 33 Bit Score: 62.27 E-value: 7.46e-12
|
||||||||||||||||||
| Spectrin | pfam00435 | Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ... |
1167-1271 | 7.49e-12 | ||||||||||||||
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in cytoskeletal structure. These include spectrin, alpha-actinin and dystrophin. The sequence repeat used in this family is taken from the structural repeat in reference. The spectrin domain- repeat forms a three helix bundle. The second helix is interrupted by proline in some sequences. The repeats are defined by a characteriztic tryptophan (W) residue at position 17 in helix A and a leucine (L) at 2 residues from the carboxyl end of helix C. Although the domain occurs in multiple repeats along sequences, the domains are actually stable on their own - ie they act, biophysically, like domains rather than repeats that along function when aggregated. Pssm-ID: 395348 [Multi-domain] Cd Length: 105 Bit Score: 64.65 E-value: 7.49e-12
|
||||||||||||||||||
| LDLa | cd00112 | Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central ... |
3403-3436 | 9.97e-12 | ||||||||||||||
Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central role in mammalian cholesterol metabolism; the receptor protein binds LDL and transports it into cells by endocytosis; 7 successive cysteine-rich repeats of about 40 amino acids are present in the N-terminal of this multidomain membrane protein; other homologous domains occur in related receptors, including the very low-density lipoprotein receptor and the LDL receptor-related protein/alpha 2-macroglobulin receptor, and in proteins which are functionally unrelated, such as the C9 component of complement; the binding of calcium is required for in vitro formation of the native disulfide isomer and is necessary in establishing and maintaining the modular structure Pssm-ID: 238060 Cd Length: 35 Bit Score: 61.84 E-value: 9.97e-12
|
||||||||||||||||||
| PH_EFA6 | cd13295 | Exchange Factor for ARF6 Pleckstrin homology (PH) domain; EFA6 (also called PSD/pleckstrin and ... |
2189-2291 | 1.17e-11 | ||||||||||||||
Exchange Factor for ARF6 Pleckstrin homology (PH) domain; EFA6 (also called PSD/pleckstrin and Sec7 domain containing) is an guanine nucleotide exchange factor for ADP ribosylation factor 6 (ARF6), which is involved in membrane recycling. EFA6 has four structurally related polypeptides: EFA6A, EFA6B, EFA6C and EFA6D. It consists of a N-terminal proline rich region (PR), a SEC7 domain, a PH domain, a PR, a coiled-coil region, and a C-terminal PR. The EFA6 PH domain regulates its association with the plasma membrane. EFA6 activates Arf6 through its Sec7 catalytic domain and modulates this activity through its C-terminal domain, which rearranges the actin cytoskeleton in fibroblastic cell lines. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes. Pssm-ID: 270107 Cd Length: 126 Bit Score: 64.66 E-value: 1.17e-11
|
||||||||||||||||||
| fn3 | pfam00041 | Fibronectin type III domain; |
3866-3946 | 1.18e-11 | ||||||||||||||
Fibronectin type III domain; Pssm-ID: 394996 [Multi-domain] Cd Length: 85 Bit Score: 63.59 E-value: 1.18e-11
|
||||||||||||||||||
| YhaN | COG4717 | Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1246-1721 | 2.51e-11 | ||||||||||||||
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 70.18 E-value: 2.51e-11
|
||||||||||||||||||
| Spectrin | pfam00435 | Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ... |
298-408 | 2.60e-11 | ||||||||||||||
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in cytoskeletal structure. These include spectrin, alpha-actinin and dystrophin. The sequence repeat used in this family is taken from the structural repeat in reference. The spectrin domain- repeat forms a three helix bundle. The second helix is interrupted by proline in some sequences. The repeats are defined by a characteriztic tryptophan (W) residue at position 17 in helix A and a leucine (L) at 2 residues from the carboxyl end of helix C. Although the domain occurs in multiple repeats along sequences, the domains are actually stable on their own - ie they act, biophysically, like domains rather than repeats that along function when aggregated. Pssm-ID: 395348 [Multi-domain] Cd Length: 105 Bit Score: 63.11 E-value: 2.60e-11
|
||||||||||||||||||
| DUF3584 | pfam12128 | Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
938-1857 | 3.13e-11 | ||||||||||||||
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication. Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 70.25 E-value: 3.13e-11
|
||||||||||||||||||
| LDLa | cd00112 | Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central ... |
3675-3710 | 4.36e-11 | ||||||||||||||
Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central role in mammalian cholesterol metabolism; the receptor protein binds LDL and transports it into cells by endocytosis; 7 successive cysteine-rich repeats of about 40 amino acids are present in the N-terminal of this multidomain membrane protein; other homologous domains occur in related receptors, including the very low-density lipoprotein receptor and the LDL receptor-related protein/alpha 2-macroglobulin receptor, and in proteins which are functionally unrelated, such as the C9 component of complement; the binding of calcium is required for in vitro formation of the native disulfide isomer and is necessary in establishing and maintaining the modular structure Pssm-ID: 238060 Cd Length: 35 Bit Score: 60.30 E-value: 4.36e-11
|
||||||||||||||||||
| CCDC158 | pfam15921 | Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
1282-1823 | 5.16e-11 | ||||||||||||||
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known. Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 69.38 E-value: 5.16e-11
|
||||||||||||||||||
| Ldl_recept_a | pfam00057 | Low-density lipoprotein receptor domain class A; |
3401-3436 | 5.57e-11 | ||||||||||||||
Low-density lipoprotein receptor domain class A; Pssm-ID: 395011 Cd Length: 37 Bit Score: 59.95 E-value: 5.57e-11
|
||||||||||||||||||
| LDLa | cd00112 | Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central ... |
3579-3613 | 1.06e-10 | ||||||||||||||
Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central role in mammalian cholesterol metabolism; the receptor protein binds LDL and transports it into cells by endocytosis; 7 successive cysteine-rich repeats of about 40 amino acids are present in the N-terminal of this multidomain membrane protein; other homologous domains occur in related receptors, including the very low-density lipoprotein receptor and the LDL receptor-related protein/alpha 2-macroglobulin receptor, and in proteins which are functionally unrelated, such as the C9 component of complement; the binding of calcium is required for in vitro formation of the native disulfide isomer and is necessary in establishing and maintaining the modular structure Pssm-ID: 238060 Cd Length: 35 Bit Score: 59.14 E-value: 1.06e-10
|
||||||||||||||||||
| CH_PLS_rpt3 | cd21298 | third calponin homology (CH) domain found in the plastin family; The plastin family includes ... |
47-156 | 1.21e-10 | ||||||||||||||
third calponin homology (CH) domain found in the plastin family; The plastin family includes plastin-1, -2, and -3. Plastin-1, also called intestine-specific plastin, or I-plastin, is an actin-bundling protein in the absence of calcium. Plastin-2, also called L-plastin, or LC64P, or lymphocyte cytosolic protein 1 (LCP-1), is an actin-binding protein that plays a role in the activation of T-cells in response to costimulation through TCR/CD3 and CD2 or CD28. It modulates the cell surface expression of IL2RA/CD25 and CD69. Plastin-3, also called T-plastin, is an actin-bundling protein found in intestinal microvilli, hair cell stereocilia, and fibroblast filopodia. It may play a role in the regulation of bone development. Members of this family contain four copies of the CH domain. This model corresponds to the third CH domain. CH domains are actin filament (F-actin) binding motifs. Pssm-ID: 409147 Cd Length: 117 Bit Score: 61.48 E-value: 1.21e-10
|
||||||||||||||||||
| LDLa | smart00192 | Low-density lipoprotein receptor domain class A; Cysteine-rich repeat in the low-density ... |
3523-3558 | 2.82e-10 | ||||||||||||||
Low-density lipoprotein receptor domain class A; Cysteine-rich repeat in the low-density lipoprotein (LDL) receptor that plays a central role in mammalian cholesterol metabolism. The N-terminal type A repeats in LDL receptor bind the lipoproteins. Other homologous domains occur in related receptors, including the very low-density lipoprotein receptor and the LDL receptor-related protein/alpha 2-macroglobulin receptor, and in proteins which are functionally unrelated, such as the C9 component of complement. Mutations in the LDL receptor gene cause familial hypercholesterolemia. Pssm-ID: 197566 Cd Length: 33 Bit Score: 57.64 E-value: 2.82e-10
|
||||||||||||||||||
| FN3 | cd00063 | Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ... |
3865-3952 | 3.04e-10 | ||||||||||||||
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases. Pssm-ID: 238020 [Multi-domain] Cd Length: 93 Bit Score: 59.82 E-value: 3.04e-10
|
||||||||||||||||||
| LDLa | smart00192 | Low-density lipoprotein receptor domain class A; Cysteine-rich repeat in the low-density ... |
3402-3433 | 4.21e-10 | ||||||||||||||
Low-density lipoprotein receptor domain class A; Cysteine-rich repeat in the low-density lipoprotein (LDL) receptor that plays a central role in mammalian cholesterol metabolism. The N-terminal type A repeats in LDL receptor bind the lipoproteins. Other homologous domains occur in related receptors, including the very low-density lipoprotein receptor and the LDL receptor-related protein/alpha 2-macroglobulin receptor, and in proteins which are functionally unrelated, such as the C9 component of complement. Mutations in the LDL receptor gene cause familial hypercholesterolemia. Pssm-ID: 197566 Cd Length: 33 Bit Score: 57.26 E-value: 4.21e-10
|
||||||||||||||||||
| Ldl_recept_a | pfam00057 | Low-density lipoprotein receptor domain class A; |
3523-3561 | 5.12e-10 | ||||||||||||||
Low-density lipoprotein receptor domain class A; Pssm-ID: 395011 Cd Length: 37 Bit Score: 57.26 E-value: 5.12e-10
|
||||||||||||||||||
| SMC_prok_A | TIGR02169 | chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
815-1495 | 5.13e-10 | ||||||||||||||
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins] Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 66.24 E-value: 5.13e-10
|
||||||||||||||||||
| CH_FIMB_rpt3 | cd21300 | third calponin homology (CH) domain found in Saccharomyces cerevisiae fimbrin and similar ... |
46-155 | 5.24e-10 | ||||||||||||||
third calponin homology (CH) domain found in Saccharomyces cerevisiae fimbrin and similar proteins; Fimbrin binds to actin, and functionally associates with actin structures involved in the development and maintenance of cell polarity. Members of this family contain four copies of the CH domain. This model corresponds to the third CH domain. CH domains are actin filament (F-actin) binding motifs. Pssm-ID: 409149 Cd Length: 119 Bit Score: 59.74 E-value: 5.24e-10
|
||||||||||||||||||
| CH_ASPM_rpt1 | cd21223 | first calponin homology (CH) domain found in abnormal spindle-like microcephaly-associated ... |
73-150 | 6.51e-10 | ||||||||||||||
first calponin homology (CH) domain found in abnormal spindle-like microcephaly-associated protein (ASPM) and similar proteins; ASPM, also called abnormal spindle protein homolog, or Asp homolog, is involved in mitotic spindle regulation and coordination of mitotic processes. It may also have a preferential role in regulating neurogenesis. Members of this family contain two copies of the CH domain in the middle region. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs. Pssm-ID: 409072 Cd Length: 113 Bit Score: 59.53 E-value: 6.51e-10
|
||||||||||||||||||
| LDLa | smart00192 | Low-density lipoprotein receptor domain class A; Cysteine-rich repeat in the low-density ... |
3579-3610 | 8.95e-10 | ||||||||||||||
Low-density lipoprotein receptor domain class A; Cysteine-rich repeat in the low-density lipoprotein (LDL) receptor that plays a central role in mammalian cholesterol metabolism. The N-terminal type A repeats in LDL receptor bind the lipoproteins. Other homologous domains occur in related receptors, including the very low-density lipoprotein receptor and the LDL receptor-related protein/alpha 2-macroglobulin receptor, and in proteins which are functionally unrelated, such as the C9 component of complement. Mutations in the LDL receptor gene cause familial hypercholesterolemia. Pssm-ID: 197566 Cd Length: 33 Bit Score: 56.49 E-value: 8.95e-10
|
||||||||||||||||||
| PH | smart00233 | Pleckstrin homology domain; Domain commonly found in eukaryotic signalling proteins. The ... |
2196-2292 | 1.34e-09 | ||||||||||||||
Pleckstrin homology domain; Domain commonly found in eukaryotic signalling proteins. The domain family possesses multiple functions including the abilities to bind inositol phosphates, and various proteins. PH domains have been found to possess inserted domains (such as in PLC gamma, syntrophins) and to be inserted within other domains. Mutations in Brutons tyrosine kinase (Btk) within its PH domain cause X-linked agammaglobulinaemia (XLA) in patients. Point mutations cluster into the positively charged end of the molecule around the predicted binding site for phosphatidylinositol lipids. Pssm-ID: 214574 [Multi-domain] Cd Length: 102 Bit Score: 58.33 E-value: 1.34e-09
|
||||||||||||||||||
| LDLa | smart00192 | Low-density lipoprotein receptor domain class A; Cysteine-rich repeat in the low-density ... |
3675-3707 | 1.81e-09 | ||||||||||||||
Low-density lipoprotein receptor domain class A; Cysteine-rich repeat in the low-density lipoprotein (LDL) receptor that plays a central role in mammalian cholesterol metabolism. The N-terminal type A repeats in LDL receptor bind the lipoproteins. Other homologous domains occur in related receptors, including the very low-density lipoprotein receptor and the LDL receptor-related protein/alpha 2-macroglobulin receptor, and in proteins which are functionally unrelated, such as the C9 component of complement. Mutations in the LDL receptor gene cause familial hypercholesterolemia. Pssm-ID: 197566 Cd Length: 33 Bit Score: 55.72 E-value: 1.81e-09
|
||||||||||||||||||
| SMC_prok_A | TIGR02169 | chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
709-1606 | 2.38e-09 | ||||||||||||||
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins] Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 63.93 E-value: 2.38e-09
|
||||||||||||||||||
| Ldl_recept_a | pfam00057 | Low-density lipoprotein receptor domain class A; |
3673-3710 | 2.95e-09 | ||||||||||||||
Low-density lipoprotein receptor domain class A; Pssm-ID: 395011 Cd Length: 37 Bit Score: 54.95 E-value: 2.95e-09
|
||||||||||||||||||
| PH_ARHGAP9-like | cd13233 | Beta-spectrin pleckstrin homology (PH) domain; ARHGAP family genes encode Rho/Rac/Cdc42-like ... |
2196-2292 | 3.22e-09 | ||||||||||||||
Beta-spectrin pleckstrin homology (PH) domain; ARHGAP family genes encode Rho/Rac/Cdc42-like GTPase activating proteins with RhoGAP domain. The ARHGAP members here all have a PH domain upstream of their C-terminal RhoGAP domain. Some have additional N-terminal SH3 and WW domains. The members here include: ARHGAP9, ARHGAP12, ARHGAP15, and ARHGAP27. ARHGAP27 and ARHGAP12 shared the common-domain structure, consisting of SH3, WW, PH, and RhoGAP domains. The PH domain of ArhGAP9 employs a non-canonical phosphoinositide binding mechanism, a variation of the spectrin- Ins(4,5)P2-binding mode, that gives rise to a unique PI binding profile, namely a preference for both PI(4,5)P2 and the PI 3-kinase products PI(3,4,5)P3 and PI(3,4)P2. This lipid binding mechanism is also employed by the PH domain of Tiam1 and Slm1. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes. Pssm-ID: 270053 Cd Length: 110 Bit Score: 57.29 E-value: 3.22e-09
|
||||||||||||||||||
| SMC_prok_B | TIGR02168 | chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1020-1823 | 3.26e-09 | ||||||||||||||
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins] Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 63.54 E-value: 3.26e-09
|
||||||||||||||||||
| COG4913 | COG4913 | Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
604-1146 | 9.72e-09 | ||||||||||||||
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 61.85 E-value: 9.72e-09
|
||||||||||||||||||
| SMC_prok_B | TIGR02168 | chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
393-1108 | 1.41e-08 | ||||||||||||||
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins] Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 61.61 E-value: 1.41e-08
|
||||||||||||||||||
| YncE | COG3391 | DNA-binding beta-propeller fold protein YncE [General function prediction only]; |
3123-3276 | 1.76e-08 | ||||||||||||||
DNA-binding beta-propeller fold protein YncE [General function prediction only]; Pssm-ID: 442618 [Multi-domain] Cd Length: 237 Bit Score: 58.55 E-value: 1.76e-08
|
||||||||||||||||||
| CH_PLS3_rpt3 | cd21331 | third calponin homology (CH) domain found in plastin-3; Plastin-3, also called T-plastin, is ... |
47-155 | 1.85e-08 | ||||||||||||||
third calponin homology (CH) domain found in plastin-3; Plastin-3, also called T-plastin, is an actin-bundling protein found in intestinal microvilli, hair cell stereocilia, and fibroblast filopodia. It may play a role in the regulation of bone development. Plastin-3 contains four copies of the CH domain. This model corresponds to the third CH domain. CH domains are actin filament (F-actin) binding motifs. Pssm-ID: 409180 Cd Length: 134 Bit Score: 55.78 E-value: 1.85e-08
|
||||||||||||||||||
| FN3 | COG3401 | Fibronectin type 3 domain [General function prediction only]; |
4026-4361 | 1.96e-08 | ||||||||||||||
Fibronectin type 3 domain [General function prediction only]; Pssm-ID: 442628 [Multi-domain] Cd Length: 603 Bit Score: 60.79 E-value: 1.96e-08
|
||||||||||||||||||
| 235kDa-fam | TIGR01612 | reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
923-1637 | 2.01e-08 | ||||||||||||||
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii. Pssm-ID: 130673 [Multi-domain] Cd Length: 2757 Bit Score: 61.22 E-value: 2.01e-08
|
||||||||||||||||||
| CH_NAV3 | cd21286 | calponin homology (CH) domain found in neuron navigator 3; Neuron navigator 3 (NAV3), also ... |
54-149 | 2.56e-08 | ||||||||||||||
calponin homology (CH) domain found in neuron navigator 3; Neuron navigator 3 (NAV3), also called pore membrane and/or filament-interacting-like protein 1 (POMFIL1), Steerin-3 (STEERIN3), or Unc-53 homolog 3 (unc53H3), may regulate IL2 production by T-cells. It may be involved in neuron regeneration. NAV3 contains a single copy of the CH domain at the N-terminus. CH domains are actin filament (F-actin) binding motifs. Pssm-ID: 409135 Cd Length: 105 Bit Score: 54.65 E-value: 2.56e-08
|
||||||||||||||||||
| CH_PLS_FIM_rpt1 | cd21217 | first calponin homology (CH) domain found in the plastin/fimbrin family; This family includes ... |
53-150 | 2.61e-08 | ||||||||||||||
first calponin homology (CH) domain found in the plastin/fimbrin family; This family includes plastin and fimbrin. Plastin has three isoforms, plastin-1, -2, and -3, which are all actin-bundling proteins. Plastin-1, also called intestine-specific plastin, or I-plastin, is an actin-bundling protein in the absence of calcium. Plastin-2, also called L-plastin, LC64P, or lymphocyte cytosolic protein 1 (LCP-1), plays a role in the activation of T-cells in response to costimulation through TCR/CD3 and CD2 or CD28. It modulates the cell surface expression of IL2RA/CD25 and CD69. Plastin-3, also called T-plastin, is found in intestinal microvilli, hair cell stereocilia, and fibroblast filopodia. It may play a role in the regulation of bone development. Fimbrin has been found in plants and fungi. Arabidopsis thaliana fimbrin (AtFIM) includes fimbrin-1, -2, -3, -4, and -5; they cross-link actin filaments (F-actin) in a calcium independent manner. They stabilize and prevent F-actin depolymerization mediated by profilin. They act as key regulators of actin cytoarchitecture, probably involved in cell cycle, cell division, cell elongation and cytoplasmic tractus. AtFIM5 is an actin bundling factor that is required for pollen germination and pollen tube growth. Fungal fimbrin binds to actin, and functionally associates with actin structures involved in the development and maintenance of cell polarity. Members of this family contain four copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs. Pssm-ID: 409066 [Multi-domain] Cd Length: 114 Bit Score: 54.89 E-value: 2.61e-08
|
||||||||||||||||||
| sbcc | TIGR00618 | exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
565-1328 | 2.84e-08 | ||||||||||||||
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair] Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 60.37 E-value: 2.84e-08
|
||||||||||||||||||
| CAMSAP_CH | pfam11971 | CAMSAP CH domain; This domain is the N-terminal CH domain from the CAMSAP proteins. |
185-254 | 3.68e-08 | ||||||||||||||
CAMSAP CH domain; This domain is the N-terminal CH domain from the CAMSAP proteins. Pssm-ID: 432229 Cd Length: 85 Bit Score: 53.46 E-value: 3.68e-08
|
||||||||||||||||||
| FN3 | smart00060 | Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ... |
3865-3943 | 3.72e-08 | ||||||||||||||
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, fibronectin. The tenth fibronectin type III repeat contains a RGD cell recognition sequence in a flexible loop between 2 strands. Type III modules are present in both extracellular and intracellular proteins. Pssm-ID: 214495 [Multi-domain] Cd Length: 83 Bit Score: 53.39 E-value: 3.72e-08
|
||||||||||||||||||
| Ldl_recept_b | pfam00058 | Low-density lipoprotein receptor repeat class B; This domain is also known as the YWTD motif ... |
3171-3214 | 5.11e-08 | ||||||||||||||
Low-density lipoprotein receptor repeat class B; This domain is also known as the YWTD motif after the most conserved region of the repeat. The YWTD repeat is found in multiple tandem repeats and has been predicted to form a beta-propeller structure. Pssm-ID: 459654 Cd Length: 42 Bit Score: 51.78 E-value: 5.11e-08
|
||||||||||||||||||
| CH_FLNC_rpt2 | cd21314 | second calponin homology (CH) domain found in filamin-C (FLN-C) and similar proteins; ... |
161-269 | 5.22e-08 | ||||||||||||||
second calponin homology (CH) domain found in filamin-C (FLN-C) and similar proteins; Filamin-C (FLN-C), also called FLNc, ABP-280-like protein, ABP-L, actin-binding-like protein, filamin-2, or gamma-filamin, is a muscle-specific filamin that plays a central role in muscle cells, probably by functioning as a large actin-cross-linking protein. It may be involved in reorganizing the actin cytoskeleton in response to signaling events, and may also display structural functions at the Z lines in muscle cells. FLN-C is critical for normal myogenesis and for maintaining the structural integrity of the muscle fibers. FLN-C contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs. Pssm-ID: 409163 Cd Length: 115 Bit Score: 53.92 E-value: 5.22e-08
|
||||||||||||||||||
| CH_dFLNA-like_rpt2 | cd21315 | second calponin homology (CH) domain found in Drosophila melanogaster filamin-A (dFLNA) and ... |
164-269 | 5.40e-08 | ||||||||||||||
second calponin homology (CH) domain found in Drosophila melanogaster filamin-A (dFLNA) and similar proteins; Drosophila melanogaster filamin-A (dFLNA or dFLN-A), also called actin-binding protein 280 (ABP-280) or filamin-1, is involved in germline ring canal formation. It may tether actin microfilaments within the ovarian ring canal to the cell membrane and contributes to actin microfilament organization. dFLNA contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs. Pssm-ID: 409164 Cd Length: 118 Bit Score: 54.02 E-value: 5.40e-08
|
||||||||||||||||||
| Smc | COG1196 | Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
920-1497 | 5.68e-08 | ||||||||||||||
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 59.57 E-value: 5.68e-08
|
||||||||||||||||||
| sbcc | TIGR00618 | exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1207-1852 | 5.82e-08 | ||||||||||||||
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair] Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 59.60 E-value: 5.82e-08
|
||||||||||||||||||
| SMC_prok_A | TIGR02169 | chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
934-1671 | 6.62e-08 | ||||||||||||||
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins] Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 59.31 E-value: 6.62e-08
|
||||||||||||||||||
| PH | pfam00169 | PH domain; PH stands for pleckstrin homology. |
2194-2290 | 7.13e-08 | ||||||||||||||
PH domain; PH stands for pleckstrin homology. Pssm-ID: 459697 [Multi-domain] Cd Length: 105 Bit Score: 53.34 E-value: 7.13e-08
|
||||||||||||||||||
| LY | smart00135 | Low-density lipoprotein-receptor YWTD domain; Type "B" repeats in low-density lipoprotein (LDL) ... |
3197-3237 | 9.23e-08 | ||||||||||||||
Low-density lipoprotein-receptor YWTD domain; Type "B" repeats in low-density lipoprotein (LDL) receptor that plays a central role in mammalian cholesterol metabolism. Also present in a variety of molecules similar to gp300/megalin. Pssm-ID: 214531 [Multi-domain] Cd Length: 43 Bit Score: 51.06 E-value: 9.23e-08
|
||||||||||||||||||
| LY | smart00135 | Low-density lipoprotein-receptor YWTD domain; Type "B" repeats in low-density lipoprotein (LDL) ... |
3150-3195 | 9.88e-08 | ||||||||||||||
Low-density lipoprotein-receptor YWTD domain; Type "B" repeats in low-density lipoprotein (LDL) receptor that plays a central role in mammalian cholesterol metabolism. Also present in a variety of molecules similar to gp300/megalin. Pssm-ID: 214531 [Multi-domain] Cd Length: 43 Bit Score: 50.68 E-value: 9.88e-08
|
||||||||||||||||||
| SMC_N | pfam02463 | RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
1245-2051 | 1.16e-07 | ||||||||||||||
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination. Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 58.44 E-value: 1.16e-07
|
||||||||||||||||||
| SMC_prok_A | TIGR02169 | chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1020-1406 | 3.07e-07 | ||||||||||||||
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins] Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 57.00 E-value: 3.07e-07
|
||||||||||||||||||
| CH_FLNB_rpt2 | cd21313 | second calponin homology (CH) domain found in filamin-B (FLN-B) and similar proteins; ... |
163-269 | 3.20e-07 | ||||||||||||||
second calponin homology (CH) domain found in filamin-B (FLN-B) and similar proteins; Filamin-B (FLN-B) is also called ABP-278, ABP-280 homolog, actin-binding-like protein, beta-filamin, filamin homolog 1 (Fh1), filamin-3, thyroid autoantigen, truncated actin-binding protein, or truncated ABP. It connects cell membrane constituents to the actin cytoskeleton. It may promote orthogonal branching of actin filaments and links actin filaments to membrane glycoproteins. It anchors various transmembrane proteins to the actin cytoskeleton. FLN-B contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs. Pssm-ID: 409162 Cd Length: 110 Bit Score: 51.63 E-value: 3.20e-07
|
||||||||||||||||||
| PTZ00121 | PTZ00121 | MAEBL; Provisional |
1175-1669 | 3.97e-07 | ||||||||||||||
MAEBL; Provisional Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 57.07 E-value: 3.97e-07
|
||||||||||||||||||
| PRK02224 | PRK02224 | DNA double-strand break repair Rad50 ATPase; |
990-1451 | 4.06e-07 | ||||||||||||||
DNA double-strand break repair Rad50 ATPase; Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 56.59 E-value: 4.06e-07
|
||||||||||||||||||
| CHASE3 | COG5278 | Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms]; |
961-1430 | 4.26e-07 | ||||||||||||||
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms]; Pssm-ID: 444089 [Multi-domain] Cd Length: 530 Bit Score: 56.07 E-value: 4.26e-07
|
||||||||||||||||||
| CH_AtFIM_like_rpt3 | cd21299 | third calponin homology (CH) domain found in the Arabidopsis thaliana fimbrin family; The ... |
52-155 | 5.80e-07 | ||||||||||||||
third calponin homology (CH) domain found in the Arabidopsis thaliana fimbrin family; The Arabidopsis thaliana fimbrin (AtFIM) family includes Fimbrin-1, -2, -3, -4, and -5, which cross-link actin filaments (F-actin) in a calcium independent manner. They stabilize and prevent F-actin depolymerization mediated by profilin. They act as key regulators of actin cytoarchitecture, probably involved in cell cycle, cell division, cell elongation and cytoplasmic tractus. AtFIM5 is an actin bundling factor that is required for pollen germination and pollen tube growth. Members of this family contain four copies of the CH domain. This model corresponds to the third CH domain. CH domains are actin filament (F-actin) binding motifs. Pssm-ID: 409148 Cd Length: 114 Bit Score: 50.96 E-value: 5.80e-07
|
||||||||||||||||||
| GumC | COG3206 | Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
817-1147 | 6.20e-07 | ||||||||||||||
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 55.79 E-value: 6.20e-07
|
||||||||||||||||||
| YhaN | COG4717 | Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
920-1324 | 9.90e-07 | ||||||||||||||
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 55.16 E-value: 9.90e-07
|
||||||||||||||||||
| CH_PLS2_rpt3 | cd21330 | third calponin homology (CH) domain found in plastin-2; Plastin-2, also called L-plastin, or ... |
47-155 | 1.34e-06 | ||||||||||||||
third calponin homology (CH) domain found in plastin-2; Plastin-2, also called L-plastin, or LC64P, or lymphocyte cytosolic protein 1 (LCP-1), is an actin-binding protein that plays a role in the activation of T-cells in response to costimulation through TCR/CD3 and CD2 or CD28. It modulates the cell surface expression of IL2RA/CD25 and CD69. Plastin-2 contains four copies of the CH domain. This model corresponds to the third CH domain. CH domains are actin filament (F-actin) binding motifs. Pssm-ID: 409179 Cd Length: 125 Bit Score: 50.37 E-value: 1.34e-06
|
||||||||||||||||||
| Ldl_recept_a | pfam00057 | Low-density lipoprotein receptor domain class A; |
3584-3613 | 1.52e-06 | ||||||||||||||
Low-density lipoprotein receptor domain class A; Pssm-ID: 395011 Cd Length: 37 Bit Score: 47.24 E-value: 1.52e-06
|
||||||||||||||||||
| CwlO1 | COG3883 | Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1239-1464 | 1.73e-06 | ||||||||||||||
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown]; Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 53.68 E-value: 1.73e-06
|
||||||||||||||||||
| CH_FLNA_rpt2 | cd21312 | second calponin homology (CH) domain found in filamin-A (FLN-A) and similar proteins; ... |
161-269 | 1.89e-06 | ||||||||||||||
second calponin homology (CH) domain found in filamin-A (FLN-A) and similar proteins; Filamin-A (FLN-A) is also called actin-binding protein 280 (ABP-280), alpha-filamin, endothelial actin-binding protein, filamin-1, or non-muscle filamin. It promotes orthogonal branching of actin filaments and links actin filaments to membrane glycoproteins. It also anchors various transmembrane proteins to the actin cytoskeleton and serves as a scaffold for a wide range of cytoplasmic signaling proteins. FLN-A contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs. Pssm-ID: 409161 Cd Length: 114 Bit Score: 49.42 E-value: 1.89e-06
|
||||||||||||||||||
| Smc | COG1196 | Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
396-1068 | 1.93e-06 | ||||||||||||||
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 54.56 E-value: 1.93e-06
|
||||||||||||||||||
| CH_NAV2 | cd21285 | calponin homology (CH) domain found in neuron navigator 2; Neuron navigator 2 (NAV2), also ... |
52-149 | 2.77e-06 | ||||||||||||||
calponin homology (CH) domain found in neuron navigator 2; Neuron navigator 2 (NAV2), also called helicase APC down-regulated 1 (HELAD1), pore membrane and/or filament-interacting-like protein 2 (POMFIL2), retinoic acid inducible in neuroblastoma 1 (RAINB1), Steerin-2 (STEERIN2), or Unc-53 homolog 2 (unc53H2), possesses 3' to 5' helicase activity and exonuclease activity. It is involved in neuronal development, specifically in the development of different sensory organs. NAV2 contains a single copy of the CH domain at the N-terminus. CH domains are actin filament (F-actin) binding motifs. Pssm-ID: 409134 Cd Length: 121 Bit Score: 49.19 E-value: 2.77e-06
|
||||||||||||||||||
| CH_ASPM_rpt2 | cd21224 | second calponin homology (CH) domain found in abnormal spindle-like microcephaly-associated ... |
173-266 | 2.77e-06 | ||||||||||||||
second calponin homology (CH) domain found in abnormal spindle-like microcephaly-associated protein (ASPM) and similar proteins; ASPM, also called abnormal spindle protein homolog, or Asp homolog, is involved in mitotic spindle regulation and coordination of mitotic processes. It may also have a preferential role in regulating neurogenesis. Members of this family contain two copies of CH domain in the middle region. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs. Pssm-ID: 409073 [Multi-domain] Cd Length: 138 Bit Score: 49.61 E-value: 2.77e-06
|
||||||||||||||||||
| Smc | COG1196 | Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1259-1819 | 3.43e-06 | ||||||||||||||
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 53.40 E-value: 3.43e-06
|
||||||||||||||||||
| LDLa | cd00112 | Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central ... |
3724-3758 | 3.97e-06 | ||||||||||||||
Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central role in mammalian cholesterol metabolism; the receptor protein binds LDL and transports it into cells by endocytosis; 7 successive cysteine-rich repeats of about 40 amino acids are present in the N-terminal of this multidomain membrane protein; other homologous domains occur in related receptors, including the very low-density lipoprotein receptor and the LDL receptor-related protein/alpha 2-macroglobulin receptor, and in proteins which are functionally unrelated, such as the C9 component of complement; the binding of calcium is required for in vitro formation of the native disulfide isomer and is necessary in establishing and maintaining the modular structure Pssm-ID: 238060 Cd Length: 35 Bit Score: 46.05 E-value: 3.97e-06
|
||||||||||||||||||
| YncE | COG3391 | DNA-binding beta-propeller fold protein YncE [General function prediction only]; |
3077-3238 | 4.64e-06 | ||||||||||||||
DNA-binding beta-propeller fold protein YncE [General function prediction only]; Pssm-ID: 442618 [Multi-domain] Cd Length: 237 Bit Score: 51.23 E-value: 4.64e-06
|
||||||||||||||||||
| NHL | cd05819 | NHL repeat unit of beta-propeller proteins; The NHL(NCL-1, HT2A and LIN-41)-repeat is found in ... |
3115-3276 | 4.65e-06 | ||||||||||||||
NHL repeat unit of beta-propeller proteins; The NHL(NCL-1, HT2A and LIN-41)-repeat is found in multiple tandem copies, typically as 6 instances. It is about 40 residues long and resembles the WD repeat and other beta-propeller structures. The repeats have a catalytic activity in Peptidyl-glycine alpha-amidating monooxygenase; proteolysis has shown that the Peptidyl-alpha-hydroxyglycine alpha-amidating lyase (PAL) activity is localized to the repeats. Tripartite motif-containing protein 32 interacts with the activation domain of Tat. This interaction is mediated by the NHL repeats. Pssm-ID: 271320 [Multi-domain] Cd Length: 269 Bit Score: 51.55 E-value: 4.65e-06
|
||||||||||||||||||
| PH_RhoGap25-like | cd13263 | Rho GTPase activating protein 25 and related proteins Pleckstrin homology (PH) domain; ... |
2210-2298 | 5.81e-06 | ||||||||||||||
Rho GTPase activating protein 25 and related proteins Pleckstrin homology (PH) domain; RhoGAP25 (also called ArhGap25) like other RhoGaps are involved in cell polarity, cell morphology and cytoskeletal organization. They act as GTPase activators for the Rac-type GTPases by converting them to an inactive GDP-bound state and control actin remodeling by inactivating Rac downstream of Rho leading to suppress leading edge protrusion and promotes cell retraction to achieve cellular polarity and are able to suppress RAC1 and CDC42 activity in vitro. Overexpression of these proteins induces cell rounding with partial or complete disruption of actin stress fibers and formation of membrane ruffles, lamellipodia, and filopodia. This hierarchy contains RhoGAP22, RhoGAP24, and RhoGAP25. Members here contain an N-terminal PH domain followed by a RhoGAP domain and either a BAR or TATA Binding Protein (TBP) Associated Factor 4 (TAF4) domain. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes. Pssm-ID: 270083 Cd Length: 114 Bit Score: 48.15 E-value: 5.81e-06
|
||||||||||||||||||
| PH | cd00821 | Pleckstrin homology (PH) domain; PH domains have diverse functions, but in general are ... |
2196-2287 | 6.37e-06 | ||||||||||||||
Pleckstrin homology (PH) domain; PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes. Pssm-ID: 275388 [Multi-domain] Cd Length: 92 Bit Score: 47.54 E-value: 6.37e-06
|
||||||||||||||||||
| YhaN | COG4717 | Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
450-937 | 6.59e-06 | ||||||||||||||
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 52.46 E-value: 6.59e-06
|
||||||||||||||||||
| rad50 | TIGR00606 | rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
772-1710 | 7.15e-06 | ||||||||||||||
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 52.74 E-value: 7.15e-06
|
||||||||||||||||||
| CH_PLS1_rpt3 | cd21329 | third calponin homology (CH) domain found in plastin-1; Plastin-1, also called ... |
47-155 | 7.38e-06 | ||||||||||||||
third calponin homology (CH) domain found in plastin-1; Plastin-1, also called intestine-specific plastin, or I-plastin, is an actin-bundling protein in the absence of calcium. It contains four copies of the CH domain. This model corresponds to the third CH domain. CH domains are actin filament (F-actin) binding motifs. Pssm-ID: 409178 Cd Length: 118 Bit Score: 48.06 E-value: 7.38e-06
|
||||||||||||||||||
| NHL_like_6 | cd14962 | Uncharacterized NHL-repeat domain in bacterial proteins; The NHL (NCL-1, HT2A and LIN-41) ... |
3115-3260 | 7.63e-06 | ||||||||||||||
Uncharacterized NHL-repeat domain in bacterial proteins; The NHL (NCL-1, HT2A and LIN-41) repeat is found in multiple tandem copies, typically as 6 instances. It is about 40 residues long and resembles the WD repeat and other beta-propeller structures. Pssm-ID: 271332 [Multi-domain] Cd Length: 271 Bit Score: 51.05 E-value: 7.63e-06
|
||||||||||||||||||
| Mplasa_alph_rch | TIGR04523 | helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1243-1696 | 8.33e-06 | ||||||||||||||
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown. Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 52.33 E-value: 8.33e-06
|
||||||||||||||||||
| Ldl_recept_b | pfam00058 | Low-density lipoprotein receptor repeat class B; This domain is also known as the YWTD motif ... |
3217-3258 | 8.44e-06 | ||||||||||||||
Low-density lipoprotein receptor repeat class B; This domain is also known as the YWTD motif after the most conserved region of the repeat. The YWTD repeat is found in multiple tandem repeats and has been predicted to form a beta-propeller structure. Pssm-ID: 459654 Cd Length: 42 Bit Score: 45.23 E-value: 8.44e-06
|
||||||||||||||||||
| PRK03918 | PRK03918 | DNA double-strand break repair ATPase Rad50; |
935-1452 | 1.27e-05 | ||||||||||||||
DNA double-strand break repair ATPase Rad50; Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 51.60 E-value: 1.27e-05
|
||||||||||||||||||
| SMC_prok_A | TIGR02169 | chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1216-1984 | 1.44e-05 | ||||||||||||||
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins] Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 51.61 E-value: 1.44e-05
|
||||||||||||||||||
| DR0291 | COG1579 | Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1266-1443 | 1.70e-05 | ||||||||||||||
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only]; Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 49.54 E-value: 1.70e-05
|
||||||||||||||||||
| Spectrin | pfam00435 | Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ... |
1266-1330 | 2.45e-05 | ||||||||||||||
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in cytoskeletal structure. These include spectrin, alpha-actinin and dystrophin. The sequence repeat used in this family is taken from the structural repeat in reference. The spectrin domain- repeat forms a three helix bundle. The second helix is interrupted by proline in some sequences. The repeats are defined by a characteriztic tryptophan (W) residue at position 17 in helix A and a leucine (L) at 2 residues from the carboxyl end of helix C. Although the domain occurs in multiple repeats along sequences, the domains are actually stable on their own - ie they act, biophysically, like domains rather than repeats that along function when aggregated. Pssm-ID: 395348 [Multi-domain] Cd Length: 105 Bit Score: 46.16 E-value: 2.45e-05
|
||||||||||||||||||
| CH_PLS_FIM_rpt2 | cd21218 | second calponin homology (CH) domain found in the plastin/fimbrin family; This family includes ... |
58-149 | 2.80e-05 | ||||||||||||||
second calponin homology (CH) domain found in the plastin/fimbrin family; This family includes plastin and fimbrin. Plastin has three isoforms, plastin-1, -2, and -3, which are all actin-bundling proteins. Plastin-1, also called intestine-specific plastin, or I-plastin, is an actin-bundling protein in the absence of calcium. Plastin-2, also called L-plastin, LC64P, or lymphocyte cytosolic protein 1 (LCP-1), plays a role in the activation of T-cells in response to costimulation through TCR/CD3 and CD2 or CD28. It modulates the cell surface expression of IL2RA/CD25 and CD69. Plastin-3, also called T-plastin, is found in intestinal microvilli, hair cell stereocilia, and fibroblast filopodia. It may play a role in the regulation of bone development. Fimbrin has been found in plants and fungi. Arabidopsis thaliana fimbrin (AtFIM) includes fimbrin-1, -2, -3, -4, and -5; they cross-link actin filaments (F-actin) in a calcium independent manner. They stabilize and prevent F-actin depolymerization mediated by profilin. They act as key regulators of actin cytoarchitecture, probably involved in cell cycle, cell division, cell elongation and cytoplasmic tractus. AtFIM5 is an actin bundling factor that is required for pollen germination and pollen tube growth. Fungal fimbrin binds to actin, and functionally associates with actin structures involved in the development and maintenance of cell polarity. Members of this family contain four copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs. Pssm-ID: 409067 Cd Length: 114 Bit Score: 46.14 E-value: 2.80e-05
|
||||||||||||||||||
| CH_PLS_rpt1 | cd21292 | first calponin homology (CH) domain found in the plastin family; The plastin family includes ... |
52-160 | 4.60e-05 | ||||||||||||||
first calponin homology (CH) domain found in the plastin family; The plastin family includes plastin-1, -2, and -3, which are all actin-bundling proteins. Plastin-1, also called intestine-specific plastin, or I-plastin, is an actin-bundling protein in the absence of calcium. Plastin-2, also called L-plastin, LC64P, or lymphocyte cytosolic protein 1 (LCP-1), plays a role in the activation of T-cells in response to costimulation through TCR/CD3 and CD2 or CD28. It modulates the cell surface expression of IL2RA/CD25 and CD69. Plastin-3, also called T-plastin, is found in intestinal microvilli, hair cell stereocilia, and fibroblast filopodia. It may play a role in the regulation of bone development. Members of this family contain four copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs. Pssm-ID: 409141 Cd Length: 145 Bit Score: 46.50 E-value: 4.60e-05
|
||||||||||||||||||
| LDLa | smart00192 | Low-density lipoprotein receptor domain class A; Cysteine-rich repeat in the low-density ... |
3724-3755 | 5.60e-05 | ||||||||||||||
Low-density lipoprotein receptor domain class A; Cysteine-rich repeat in the low-density lipoprotein (LDL) receptor that plays a central role in mammalian cholesterol metabolism. The N-terminal type A repeats in LDL receptor bind the lipoproteins. Other homologous domains occur in related receptors, including the very low-density lipoprotein receptor and the LDL receptor-related protein/alpha 2-macroglobulin receptor, and in proteins which are functionally unrelated, such as the C9 component of complement. Mutations in the LDL receptor gene cause familial hypercholesterolemia. Pssm-ID: 197566 Cd Length: 33 Bit Score: 43.01 E-value: 5.60e-05
|
||||||||||||||||||
| PH_CNK_mammalian-like | cd01260 | Connector enhancer of KSR (Kinase suppressor of ras) (CNK) pleckstrin homology (PH) domain; ... |
2209-2293 | 6.84e-05 | ||||||||||||||
Connector enhancer of KSR (Kinase suppressor of ras) (CNK) pleckstrin homology (PH) domain; CNK family members function as protein scaffolds, regulating the activity and the subcellular localization of RAS activated RAF. There is a single CNK protein present in Drosophila and Caenorhabditis elegans in contrast to mammals which have 3 CNK proteins (CNK1, CNK2, and CNK3). All of the CNK members contain a sterile a motif (SAM), a conserved region in CNK (CRIC) domain, and a PSD-95/DLG-1/ZO-1 (PDZ) domain, and, with the exception of CNK3, a PH domain. A CNK2 splice variant CNK2A also has a PDZ domain-binding motif at its C terminus and Drosophila CNK (D-CNK) also has a domain known as the Raf-interacting region (RIR) that mediates binding of the Drosophila Raf kinase. This cd contains CNKs from mammals, chickens, amphibians, fish, and crustacea. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes. Pssm-ID: 269962 Cd Length: 114 Bit Score: 45.09 E-value: 6.84e-05
|
||||||||||||||||||
| FN3 | cd00063 | Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ... |
3960-4043 | 6.88e-05 | ||||||||||||||
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases. Pssm-ID: 238020 [Multi-domain] Cd Length: 93 Bit Score: 44.41 E-value: 6.88e-05
|
||||||||||||||||||
| CH_jitterbug-like_rpt3 | cd21185 | third calponin homology (CH) domain found in Drosophila melanogaster protein jitterbug and ... |
188-271 | 8.58e-05 | ||||||||||||||
third calponin homology (CH) domain found in Drosophila melanogaster protein jitterbug and similar proteins; Protein jitterbug (Jbug) is an actin-meshwork organizing protein. It is required to maintain the shape and cell orientation of the Drosophila notum epithelium during flight muscle attachment to tendon cells. Jbug contains three copies of the CH domain. This model corresponds to the third CH domain. CH domains are actin filament (F-actin) binding motifs. Pssm-ID: 409034 Cd Length: 98 Bit Score: 44.22 E-value: 8.58e-05
|
||||||||||||||||||
| Smc | COG1196 | Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
393-858 | 9.04e-05 | ||||||||||||||
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 48.78 E-value: 9.04e-05
|
||||||||||||||||||
| rad50 | TIGR00606 | rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
578-1440 | 9.45e-05 | ||||||||||||||
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 48.89 E-value: 9.45e-05
|
||||||||||||||||||
| NHL | cd05819 | NHL repeat unit of beta-propeller proteins; The NHL(NCL-1, HT2A and LIN-41)-repeat is found in ... |
3115-3276 | 1.06e-04 | ||||||||||||||
NHL repeat unit of beta-propeller proteins; The NHL(NCL-1, HT2A and LIN-41)-repeat is found in multiple tandem copies, typically as 6 instances. It is about 40 residues long and resembles the WD repeat and other beta-propeller structures. The repeats have a catalytic activity in Peptidyl-glycine alpha-amidating monooxygenase; proteolysis has shown that the Peptidyl-alpha-hydroxyglycine alpha-amidating lyase (PAL) activity is localized to the repeats. Tripartite motif-containing protein 32 interacts with the activation domain of Tat. This interaction is mediated by the NHL repeats. Pssm-ID: 271320 [Multi-domain] Cd Length: 269 Bit Score: 47.31 E-value: 1.06e-04
|
||||||||||||||||||
| Myosin_tail_1 | pfam01576 | Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1202-1642 | 1.17e-04 | ||||||||||||||
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament. Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 48.63 E-value: 1.17e-04
|
||||||||||||||||||
| Sortilin-Vps10 | pfam15902 | Sortilin, neurotensin receptor 3,; Sortilin, also known in mammals as neurotensin receptor-3, ... |
2798-2915 | 1.55e-04 | ||||||||||||||
Sortilin, neurotensin receptor 3,; Sortilin, also known in mammals as neurotensin receptor-3, is the archetypical member of a Vps10-domain (Vps10-D) that binds neurotrophic factors and neuropeptides. This domain constitutes the entire luminal part of Sortilin and is activated in the trans-Golgi network by enzymatic propeptide cleavage. The structure of the domain has been determined as a ten-bladed propeller, with up to 9 BNR or beta-hairpin turns in it. The mature receptor binds various ligands, including its own propeptide (Sort-pro), neurotensin, the pro-forms of nerve growth factor-beta (NGF)6 and brain-derived neurotrophic factor (BDNF)7, lipoprotein lipase (LpL), apo lipoprotein AV14 and the receptor-associated protein (RAP)1. Pssm-ID: 464929 [Multi-domain] Cd Length: 444 Bit Score: 47.58 E-value: 1.55e-04
|
||||||||||||||||||
| Smc | COG1196 | Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1341-1748 | 1.64e-04 | ||||||||||||||
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 48.01 E-value: 1.64e-04
|
||||||||||||||||||
| COG1340 | COG1340 | Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
1243-1453 | 1.99e-04 | ||||||||||||||
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 46.83 E-value: 1.99e-04
|
||||||||||||||||||
| PRK03918 | PRK03918 | DNA double-strand break repair ATPase Rad50; |
1290-1825 | 2.69e-04 | ||||||||||||||
DNA double-strand break repair ATPase Rad50; Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 47.37 E-value: 2.69e-04
|
||||||||||||||||||
| CH_PLS3_rpt1 | cd21325 | first calponin homology (CH) domain found in plastin-3; Plastin-3, also called T-plastin, is ... |
52-150 | 2.93e-04 | ||||||||||||||
first calponin homology (CH) domain found in plastin-3; Plastin-3, also called T-plastin, is an actin-bundling protein found in intestinal microvilli, hair cell stereocilia, and fibroblast filopodia. It may play a role in the regulation of bone development. Plastin- 3 contains four copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs. Pssm-ID: 409174 Cd Length: 148 Bit Score: 44.28 E-value: 2.93e-04
|
||||||||||||||||||
| Smc | COG1196 | Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
393-947 | 3.31e-04 | ||||||||||||||
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 47.24 E-value: 3.31e-04
|
||||||||||||||||||
| PH1_PH_fungal | cd13298 | Fungal proteins Pleckstrin homology (PH) domain, repeat 1; The functions of these fungal ... |
2194-2292 | 4.20e-04 | ||||||||||||||
Fungal proteins Pleckstrin homology (PH) domain, repeat 1; The functions of these fungal proteins are unknown, but they all contain 2 PH domains. This cd represents the first PH repeat. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes. Pssm-ID: 270110 Cd Length: 106 Bit Score: 42.61 E-value: 4.20e-04
|
||||||||||||||||||
| COG4372 | COG4372 | Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
987-1337 | 4.47e-04 | ||||||||||||||
Uncharacterized protein, contains DUF3084 domain [Function unknown]; Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 46.05 E-value: 4.47e-04
|
||||||||||||||||||
| PRK03918 | PRK03918 | DNA double-strand break repair ATPase Rad50; |
774-1319 | 4.73e-04 | ||||||||||||||
DNA double-strand break repair ATPase Rad50; Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 46.60 E-value: 4.73e-04
|
||||||||||||||||||
| YhaN | COG4717 | Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
578-1099 | 4.88e-04 | ||||||||||||||
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 46.30 E-value: 4.88e-04
|
||||||||||||||||||
| CH_PLS2_rpt1 | cd21324 | first calponin homology (CH) domain found in plastin-2; Plastin-2, also called L-plastin, or ... |
52-150 | 4.98e-04 | ||||||||||||||
first calponin homology (CH) domain found in plastin-2; Plastin-2, also called L-plastin, or LC64P, or lymphocyte cytosolic protein 1 (LCP-1), is an actin-binding protein that plays a role in the activation of T-cells in response to costimulation through TCR/CD3 and CD2 or CD28. It modulates the cell surface expression of IL2RA/CD25 and CD69. Plastin-2 contains four copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs. Pssm-ID: 409173 Cd Length: 145 Bit Score: 43.46 E-value: 4.98e-04
|
||||||||||||||||||
| CH_PLS_FIM_rpt2 | cd21218 | second calponin homology (CH) domain found in the plastin/fimbrin family; This family includes ... |
161-271 | 5.03e-04 | ||||||||||||||
second calponin homology (CH) domain found in the plastin/fimbrin family; This family includes plastin and fimbrin. Plastin has three isoforms, plastin-1, -2, and -3, which are all actin-bundling proteins. Plastin-1, also called intestine-specific plastin, or I-plastin, is an actin-bundling protein in the absence of calcium. Plastin-2, also called L-plastin, LC64P, or lymphocyte cytosolic protein 1 (LCP-1), plays a role in the activation of T-cells in response to costimulation through TCR/CD3 and CD2 or CD28. It modulates the cell surface expression of IL2RA/CD25 and CD69. Plastin-3, also called T-plastin, is found in intestinal microvilli, hair cell stereocilia, and fibroblast filopodia. It may play a role in the regulation of bone development. Fimbrin has been found in plants and fungi. Arabidopsis thaliana fimbrin (AtFIM) includes fimbrin-1, -2, -3, -4, and -5; they cross-link actin filaments (F-actin) in a calcium independent manner. They stabilize and prevent F-actin depolymerization mediated by profilin. They act as key regulators of actin cytoarchitecture, probably involved in cell cycle, cell division, cell elongation and cytoplasmic tractus. AtFIM5 is an actin bundling factor that is required for pollen germination and pollen tube growth. Fungal fimbrin binds to actin, and functionally associates with actin structures involved in the development and maintenance of cell polarity. Members of this family contain four copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs. Pssm-ID: 409067 Cd Length: 114 Bit Score: 42.67 E-value: 5.03e-04
|
||||||||||||||||||
| COG4372 | COG4372 | Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1234-1609 | 5.32e-04 | ||||||||||||||
Uncharacterized protein, contains DUF3084 domain [Function unknown]; Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 45.66 E-value: 5.32e-04
|
||||||||||||||||||
| NHL_like_5 | cd14963 | Uncharacterized NHL-repeat domain in bacterial proteins; The NHL (NCL-1, HT2A and LIN-41) ... |
3116-3276 | 5.46e-04 | ||||||||||||||
Uncharacterized NHL-repeat domain in bacterial proteins; The NHL (NCL-1, HT2A and LIN-41) repeat is found in multiple tandem copies, typically as 6 instances. It is about 40 residues long and resembles the WD repeat and other beta-propeller structures. Pssm-ID: 271333 [Multi-domain] Cd Length: 268 Bit Score: 44.97 E-value: 5.46e-04
|
||||||||||||||||||
| CH_FIMB_rpt1 | cd21294 | first calponin homology (CH) domain found in Saccharomyces cerevisiae fimbrin and similar ... |
74-152 | 5.52e-04 | ||||||||||||||
first calponin homology (CH) domain found in Saccharomyces cerevisiae fimbrin and similar proteins; Fimbrin binds to actin, and functionally associates with actin structures involved in the development and maintenance of cell polarity. Members of this family contain four copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs. Pssm-ID: 409143 Cd Length: 125 Bit Score: 42.82 E-value: 5.52e-04
|
||||||||||||||||||
| CH_PLS1_rpt1 | cd21323 | first calponin homology (CH) domain found in plastin-1; Plastin-1, also called ... |
52-160 | 5.72e-04 | ||||||||||||||
first calponin homology (CH) domain found in plastin-1; Plastin-1, also called intestine-specific plastin, or I-plastin, is an actin-bundling protein in the absence of calcium. It contains four copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs. Pssm-ID: 409172 Cd Length: 145 Bit Score: 43.11 E-value: 5.72e-04
|
||||||||||||||||||
| NHL_like_3 | cd14956 | Uncharacterized NHL-repeat domain in bacterial proteins; The NHL (NCL-1, HT2A and LIN-41) ... |
3112-3193 | 6.63e-04 | ||||||||||||||
Uncharacterized NHL-repeat domain in bacterial proteins; The NHL (NCL-1, HT2A and LIN-41) repeat is found in multiple tandem copies, typically as 6 instances. It is about 40 residues long and resembles the WD repeat and other beta-propeller structures. Pssm-ID: 271326 [Multi-domain] Cd Length: 274 Bit Score: 44.97 E-value: 6.63e-04
|
||||||||||||||||||
| Ldl_recept_a | pfam00057 | Low-density lipoprotein receptor domain class A; |
3729-3758 | 7.45e-04 | ||||||||||||||
Low-density lipoprotein receptor domain class A; Pssm-ID: 395011 Cd Length: 37 Bit Score: 39.92 E-value: 7.45e-04
|
||||||||||||||||||
| TolA | COG3064 | Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis]; |
1245-1761 | 8.26e-04 | ||||||||||||||
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis]; Pssm-ID: 442298 [Multi-domain] Cd Length: 485 Bit Score: 45.42 E-value: 8.26e-04
|
||||||||||||||||||
| PH_CNK_insect-like | cd13326 | Connector enhancer of KSR (Kinase suppressor of ras) (CNK) pleckstrin homology (PH) domain; ... |
2210-2284 | 8.78e-04 | ||||||||||||||
Connector enhancer of KSR (Kinase suppressor of ras) (CNK) pleckstrin homology (PH) domain; CNK family members function as protein scaffolds, regulating the activity and the subcellular localization of RAS activated RAF. There is a single CNK protein present in Drosophila and Caenorhabditis elegans in contrast to mammals which have 3 CNK proteins (CNK1, CNK2, and CNK3). All of the CNK members contain a sterile a motif (SAM), a conserved region in CNK (CRIC) domain, and a PSD-95/DLG-1/ZO-1 (PDZ) domain, and a PH domain. A CNK2 splice variant CNK2A also has a PDZ domain-binding motif at its C terminus and Drosophila CNK (D-CNK) also has a domain known as the Raf-interacting region (RIR) that mediates binding of the Drosophila Raf kinase. This cd contains CNKs from insects, spiders, mollusks, and nematodes. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes. Pssm-ID: 270135 Cd Length: 91 Bit Score: 41.18 E-value: 8.78e-04
|
||||||||||||||||||
| CHASE3 | COG5278 | Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms]; |
1588-2037 | 9.48e-04 | ||||||||||||||
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms]; Pssm-ID: 444089 [Multi-domain] Cd Length: 530 Bit Score: 45.28 E-value: 9.48e-04
|
||||||||||||||||||
| NHL_like_6 | cd14962 | Uncharacterized NHL-repeat domain in bacterial proteins; The NHL (NCL-1, HT2A and LIN-41) ... |
3069-3227 | 1.25e-03 | ||||||||||||||
Uncharacterized NHL-repeat domain in bacterial proteins; The NHL (NCL-1, HT2A and LIN-41) repeat is found in multiple tandem copies, typically as 6 instances. It is about 40 residues long and resembles the WD repeat and other beta-propeller structures. Pssm-ID: 271332 [Multi-domain] Cd Length: 271 Bit Score: 44.12 E-value: 1.25e-03
|
||||||||||||||||||
| CH_PARV_rpt1 | cd21221 | first calponin homology (CH) domain found in the parvin family; The parvin family includes ... |
59-137 | 1.36e-03 | ||||||||||||||
first calponin homology (CH) domain found in the parvin family; The parvin family includes alpha-parvin, beta-parvin, and gamma-parvin. Alpha-parvin, also called actopaxin, calponin-like integrin-linked kinase-binding protein (CH-ILKBP), or matrix-remodeling-associated protein 2, plays a role in sarcomere organization and in smooth muscle cell contraction. It is required for normal development of the embryonic cardiovascular system, and for normal septation of the heart outflow tract. Beta-parvin, also called affixin, is an adapter protein that plays a role in integrin signaling via ILK and in activation of the GTPases Cdc42 and Rac1 by guanine exchange factors, such as ARHGEF6. Both alpha-parvin and beta-parvin are involved in the reorganization of the actin cytoskeleton and the formation of lamellipodia, and both play roles in cell adhesion, cell spreading, establishment or maintenance of cell polarity, and cell migration. Gamma-parvin probably plays a role in the regulation of cell adhesion and cytoskeleton organization. Members of this family contain two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs. Pssm-ID: 409070 Cd Length: 106 Bit Score: 41.10 E-value: 1.36e-03
|
||||||||||||||||||
| LY | smart00135 | Low-density lipoprotein-receptor YWTD domain; Type "B" repeats in low-density lipoprotein (LDL) ... |
3240-3278 | 1.36e-03 | ||||||||||||||
Low-density lipoprotein-receptor YWTD domain; Type "B" repeats in low-density lipoprotein (LDL) receptor that plays a central role in mammalian cholesterol metabolism. Also present in a variety of molecules similar to gp300/megalin. Pssm-ID: 214531 [Multi-domain] Cd Length: 43 Bit Score: 39.12 E-value: 1.36e-03
|
||||||||||||||||||
| Vgb | COG4257 | Streptogramin lyase [Defense mechanisms]; |
3046-3213 | 1.38e-03 | ||||||||||||||
Streptogramin lyase [Defense mechanisms]; Pssm-ID: 443399 [Multi-domain] Cd Length: 270 Bit Score: 43.85 E-value: 1.38e-03
|
||||||||||||||||||
| YhaN | COG4717 | Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1390-1825 | 1.52e-03 | ||||||||||||||
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 44.76 E-value: 1.52e-03
|
||||||||||||||||||
| FN3 | smart00060 | Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ... |
3960-4034 | 1.53e-03 | ||||||||||||||
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, fibronectin. The tenth fibronectin type III repeat contains a RGD cell recognition sequence in a flexible loop between 2 strands. Type III modules are present in both extracellular and intracellular proteins. Pssm-ID: 214495 [Multi-domain] Cd Length: 83 Bit Score: 40.29 E-value: 1.53e-03
|
||||||||||||||||||
| COG4913 | COG4913 | Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
387-1085 | 1.63e-03 | ||||||||||||||
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 44.91 E-value: 1.63e-03
|
||||||||||||||||||
| EnvC | COG4942 | Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
772-1021 | 1.78e-03 | ||||||||||||||
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning]; Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 43.98 E-value: 1.78e-03
|
||||||||||||||||||
| PRK03918 | PRK03918 | DNA double-strand break repair ATPase Rad50; |
380-842 | 2.04e-03 | ||||||||||||||
DNA double-strand break repair ATPase Rad50; Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 44.28 E-value: 2.04e-03
|
||||||||||||||||||
| YhaN | COG4717 | Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1501-1980 | 2.12e-03 | ||||||||||||||
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 44.37 E-value: 2.12e-03
|
||||||||||||||||||
| PH_TAAP2-like | cd13255 | Tandem PH-domain-containing protein 2 Pleckstrin homology (PH) domain; The binding of TAPP2 ... |
2210-2292 | 2.46e-03 | ||||||||||||||
Tandem PH-domain-containing protein 2 Pleckstrin homology (PH) domain; The binding of TAPP2 (also called PLEKHA2) adaptors to PtdIns(3,4)P(2), but not PI(3,4, 5)P3, function as negative regulators of insulin and PI3K signalling pathways (i.e. TAPP/utrophin/syntrophin complex). TAPP2 contains two sequential PH domains in which the C-terminal PH domain specifically binds PtdIns(3,4)P2 with high affinity. The N-terminal PH domain does not interact with any phosphoinositide tested. They also contain a C-terminal PDZ-binding motif that interacts with several PDZ-binding proteins, including PTPN13 (known previously as PTPL1 or FAP-1) as well as the scaffolding proteins MUPP1 (multiple PDZ-domain-containing protein 1), syntrophin and utrophin. The members here are most sequence similar to TAPP2 proteins, but may not be actual TAPP2 proteins. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes. Pssm-ID: 270075 Cd Length: 110 Bit Score: 40.47 E-value: 2.46e-03
|
||||||||||||||||||
| GimC | COG1382 | Prefoldin, chaperonin cofactor [Posttranslational modification, protein turnover, chaperones]; |
1266-1399 | 2.75e-03 | ||||||||||||||
Prefoldin, chaperonin cofactor [Posttranslational modification, protein turnover, chaperones]; Pssm-ID: 440992 [Multi-domain] Cd Length: 121 Bit Score: 40.64 E-value: 2.75e-03
|
||||||||||||||||||
| FN3 | cd00063 | Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ... |
4064-4145 | 2.76e-03 | ||||||||||||||
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases. Pssm-ID: 238020 [Multi-domain] Cd Length: 93 Bit Score: 39.79 E-value: 2.76e-03
|
||||||||||||||||||
| COG1340 | COG1340 | Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
771-951 | 2.91e-03 | ||||||||||||||
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 42.98 E-value: 2.91e-03
|
||||||||||||||||||
| PH_PEPP1_2_3 | cd13248 | Phosphoinositol 3-phosphate binding proteins 1, 2, and 3 pleckstrin homology (PH) domain; ... |
2215-2291 | 3.11e-03 | ||||||||||||||
Phosphoinositol 3-phosphate binding proteins 1, 2, and 3 pleckstrin homology (PH) domain; PEPP1 (also called PLEKHA4/PH domain-containing family A member 4 and RHOXF1/Rhox homeobox family member 1), and related homologs PEPP2 (also called PLEKHA5/PH domain-containing family A member 5) and PEPP3 (also called PLEKHA6/PH domain-containing family A member 6), have PH domains that interact specifically with PtdIns(3,4)P3. Other proteins that bind PtdIns(3,4)P3 specifically are: TAPP1 (tandem PH-domain-containing protein-1) and TAPP2], PtdIns3P AtPH1, and Ptd- Ins(3,5)P2 (centaurin-beta2). All of these proteins contain at least 5 of the 6 conserved amino acids that make up the putative phosphatidylinositol 3,4,5- trisphosphate-binding motif (PPBM) located at their N-terminus. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes. Pssm-ID: 270068 Cd Length: 104 Bit Score: 39.95 E-value: 3.11e-03
|
||||||||||||||||||
| LY | smart00135 | Low-density lipoprotein-receptor YWTD domain; Type "B" repeats in low-density lipoprotein (LDL) ... |
3103-3141 | 3.30e-03 | ||||||||||||||
Low-density lipoprotein-receptor YWTD domain; Type "B" repeats in low-density lipoprotein (LDL) receptor that plays a central role in mammalian cholesterol metabolism. Also present in a variety of molecules similar to gp300/megalin. Pssm-ID: 214531 [Multi-domain] Cd Length: 43 Bit Score: 37.97 E-value: 3.30e-03
|
||||||||||||||||||
| PTZ00440 | PTZ00440 | reticulocyte binding protein 2-like protein; Provisional |
1205-1541 | 3.39e-03 | ||||||||||||||
reticulocyte binding protein 2-like protein; Provisional Pssm-ID: 240419 [Multi-domain] Cd Length: 2722 Bit Score: 44.05 E-value: 3.39e-03
|
||||||||||||||||||
| SAC6 | COG5069 | Ca2+-binding actin-bundling protein fimbrin/plastin (EF-Hand superfamily) [Cytoskeleton]; |
46-194 | 3.46e-03 | ||||||||||||||
Ca2+-binding actin-bundling protein fimbrin/plastin (EF-Hand superfamily) [Cytoskeleton]; Pssm-ID: 227401 [Multi-domain] Cd Length: 612 Bit Score: 43.39 E-value: 3.46e-03
|
||||||||||||||||||
| CH_PARV_rpt2 | cd21222 | second calponin homology (CH) domain found in the parvin family; The parvin family includes ... |
53-153 | 4.93e-03 | ||||||||||||||
second calponin homology (CH) domain found in the parvin family; The parvin family includes alpha-parvin, beta-parvin, and gamma-parvin. Alpha-parvin, also called actopaxin, calponin-like integrin-linked kinase-binding protein (CH-ILKBP), or matrix-remodeling-associated protein 2, plays a role in sarcomere organization and in smooth muscle cell contraction. It is required for normal development of the embryonic cardiovascular system, and for normal septation of the heart outflow tract. Beta-parvin, also called affixin, is an adapter protein that plays a role in integrin signaling via ILK and in activation of the GTPases Cdc42 and Rac1 by guanine exchange factors, such as ARHGEF6. Both alpha-parvin and beta-parvin are involved in the reorganization of the actin cytoskeleton and the formation of lamellipodia, and both play roles in cell adhesion, cell spreading, establishment or maintenance of cell polarity, and cell migration. Gamma-parvin probably plays a role in the regulation of cell adhesion and cytoskeleton organization. Members of this family contain two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs. Pssm-ID: 409071 Cd Length: 121 Bit Score: 39.88 E-value: 4.93e-03
|
||||||||||||||||||
| FN3 | smart00060 | Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ... |
4152-4228 | 6.07e-03 | ||||||||||||||
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, fibronectin. The tenth fibronectin type III repeat contains a RGD cell recognition sequence in a flexible loop between 2 strands. Type III modules are present in both extracellular and intracellular proteins. Pssm-ID: 214495 [Multi-domain] Cd Length: 83 Bit Score: 38.75 E-value: 6.07e-03
|
||||||||||||||||||
| NHL_like_5 | cd14963 | Uncharacterized NHL-repeat domain in bacterial proteins; The NHL (NCL-1, HT2A and LIN-41) ... |
3152-3276 | 8.70e-03 | ||||||||||||||
Uncharacterized NHL-repeat domain in bacterial proteins; The NHL (NCL-1, HT2A and LIN-41) repeat is found in multiple tandem copies, typically as 6 instances. It is about 40 residues long and resembles the WD repeat and other beta-propeller structures. Pssm-ID: 271333 [Multi-domain] Cd Length: 268 Bit Score: 41.51 E-value: 8.70e-03
|
||||||||||||||||||
| COG4372 | COG4372 | Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
920-1056 | 9.23e-03 | ||||||||||||||
Uncharacterized protein, contains DUF3084 domain [Function unknown]; Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 41.81 E-value: 9.23e-03
|
||||||||||||||||||
| Blast search parameters | ||||
|
