S100 calcium-binding protein, ventral prostate like [Mus musculus]
Protein Classification
List of domain hits
| Name | Accession | Description | Interval | E-value | ||
| S_100 | pfam01023 | S-100/ICaBP type calcium binding domain; The S-100 domain is a subfamily of the EF-hand ... |
9-49 | 2.00e-05 | ||
S-100/ICaBP type calcium binding domain; The S-100 domain is a subfamily of the EF-hand calcium binding proteins. : Pssm-ID: 460028 Cd Length: 45 Bit Score: 38.19 E-value: 2.00e-05
|
||||||
| EFh super family | cl08302 | EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal ... |
30-85 | 8.91e-04 | ||
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal modulators; most examples in this alignment model have 2 active canonical EF hands. Ca2+ binding induces a conformational change in the EF-hand motif, leading to the activation or inactivation of target proteins. EF-hands tend to occur in pairs or higher copy numbers. The actual alignment was detected with superfamily member cd05030: Pssm-ID: 415501 [Multi-domain] Cd Length: 88 Bit Score: 35.02 E-value: 8.91e-04
|
||||||
| Name | Accession | Description | Interval | E-value | |||
| S_100 | pfam01023 | S-100/ICaBP type calcium binding domain; The S-100 domain is a subfamily of the EF-hand ... |
9-49 | 2.00e-05 | |||
S-100/ICaBP type calcium binding domain; The S-100 domain is a subfamily of the EF-hand calcium binding proteins. Pssm-ID: 460028 Cd Length: 45 Bit Score: 38.19 E-value: 2.00e-05
|
|||||||
| S-100 | cd00213 | S-100: S-100 domain, which represents the largest family within the superfamily of proteins ... |
6-85 | 9.02e-05 | |||
S-100: S-100 domain, which represents the largest family within the superfamily of proteins carrying the Ca-binding EF-hand motif. Note that this S-100 hierarchy contains only S-100 EF-hand domains, other EF-hands have been modeled separately. S100 proteins are expressed exclusively in vertebrates, and are implicated in intracellular and extracellular regulatory activities. Intracellularly, S100 proteins act as Ca-signaling or Ca-buffering proteins. The most unusual characteristic of certain S100 proteins is their occurrence in extracellular space, where they act in a cytokine-like manner through RAGE, the receptor for advanced glycation products. Structural data suggest that many S100 members exist within cells as homo- or heterodimers and even oligomers; oligomerization contributes to their functional diversification. Upon binding calcium, most S100 proteins change conformation to a more open structure exposing a hydrophobic cleft. This hydrophobic surface represents the interaction site of S100 proteins with their target proteins. There is experimental evidence showing that many S100 proteins have multiple binding partners with diverse mode of interaction with different targets. In addition to S100 proteins (such as S100A1,-3,-4,-6,-7,-10,-11,and -13), this group includes the ''fused'' gene family, a group of calcium binding S100-related proteins. The ''fused'' gene family includes multifunctional epidermal differentiation proteins - profilaggrin, trichohyalin, repetin, hornerin, and cornulin; functionally these proteins are associated with keratin intermediate filaments and partially crosslinked to the cell envelope. These ''fused'' gene proteins contain N-terminal sequence with two Ca-binding EF-hands motif, which may be associated with calcium signaling in epidermal cells and autoprocessing in a calcium-dependent manner. In contrast to S100 proteins, "fused" gene family proteins contain an extraordinary high number of almost perfect peptide repeats with regular array of polar and charged residues similar to many known cell envelope proteins. Pssm-ID: 238131 [Multi-domain] Cd Length: 88 Bit Score: 37.47 E-value: 9.02e-05
|
|||||||
| calgranulins | cd05030 | Calgranulins: S-100 domain found in proteins belonging to the Calgranulin subgroup of the S100 ... |
30-85 | 8.91e-04 | |||
Calgranulins: S-100 domain found in proteins belonging to the Calgranulin subgroup of the S100 family of EF-hand calcium-modulated proteins, including S100A8, S100A9, and S100A12 . Note that the S-100 hierarchy, to which this Calgranulin group belongs, contains only S-100 EF-hand domains, other EF-hands have been modeled separately. These proteins are expressed mainly in granulocytes, and are involved in inflammation, allergy, and neuritogenesis, as well as in host-parasite response. Calgranulins are modulated not only by calcium, but also by other metals such as zinc and copper. Structural data suggested that calgranulins may exist in multiple structural forms, homodimers, as well as hetero-oligomers. For example, the S100A8/S100A9 complex called calprotectin plays important roles in the regulation of inflammatory processes, wound repair, and regulating zinc-dependent enzymes as well as microbial growth. Pssm-ID: 240156 [Multi-domain] Cd Length: 88 Bit Score: 35.02 E-value: 8.91e-04
|
|||||||
| Name | Accession | Description | Interval | E-value | |||
| S_100 | pfam01023 | S-100/ICaBP type calcium binding domain; The S-100 domain is a subfamily of the EF-hand ... |
9-49 | 2.00e-05 | |||
S-100/ICaBP type calcium binding domain; The S-100 domain is a subfamily of the EF-hand calcium binding proteins. Pssm-ID: 460028 Cd Length: 45 Bit Score: 38.19 E-value: 2.00e-05
|
|||||||
| S-100 | cd00213 | S-100: S-100 domain, which represents the largest family within the superfamily of proteins ... |
6-85 | 9.02e-05 | |||
S-100: S-100 domain, which represents the largest family within the superfamily of proteins carrying the Ca-binding EF-hand motif. Note that this S-100 hierarchy contains only S-100 EF-hand domains, other EF-hands have been modeled separately. S100 proteins are expressed exclusively in vertebrates, and are implicated in intracellular and extracellular regulatory activities. Intracellularly, S100 proteins act as Ca-signaling or Ca-buffering proteins. The most unusual characteristic of certain S100 proteins is their occurrence in extracellular space, where they act in a cytokine-like manner through RAGE, the receptor for advanced glycation products. Structural data suggest that many S100 members exist within cells as homo- or heterodimers and even oligomers; oligomerization contributes to their functional diversification. Upon binding calcium, most S100 proteins change conformation to a more open structure exposing a hydrophobic cleft. This hydrophobic surface represents the interaction site of S100 proteins with their target proteins. There is experimental evidence showing that many S100 proteins have multiple binding partners with diverse mode of interaction with different targets. In addition to S100 proteins (such as S100A1,-3,-4,-6,-7,-10,-11,and -13), this group includes the ''fused'' gene family, a group of calcium binding S100-related proteins. The ''fused'' gene family includes multifunctional epidermal differentiation proteins - profilaggrin, trichohyalin, repetin, hornerin, and cornulin; functionally these proteins are associated with keratin intermediate filaments and partially crosslinked to the cell envelope. These ''fused'' gene proteins contain N-terminal sequence with two Ca-binding EF-hands motif, which may be associated with calcium signaling in epidermal cells and autoprocessing in a calcium-dependent manner. In contrast to S100 proteins, "fused" gene family proteins contain an extraordinary high number of almost perfect peptide repeats with regular array of polar and charged residues similar to many known cell envelope proteins. Pssm-ID: 238131 [Multi-domain] Cd Length: 88 Bit Score: 37.47 E-value: 9.02e-05
|
|||||||
| calgranulins | cd05030 | Calgranulins: S-100 domain found in proteins belonging to the Calgranulin subgroup of the S100 ... |
30-85 | 8.91e-04 | |||
Calgranulins: S-100 domain found in proteins belonging to the Calgranulin subgroup of the S100 family of EF-hand calcium-modulated proteins, including S100A8, S100A9, and S100A12 . Note that the S-100 hierarchy, to which this Calgranulin group belongs, contains only S-100 EF-hand domains, other EF-hands have been modeled separately. These proteins are expressed mainly in granulocytes, and are involved in inflammation, allergy, and neuritogenesis, as well as in host-parasite response. Calgranulins are modulated not only by calcium, but also by other metals such as zinc and copper. Structural data suggested that calgranulins may exist in multiple structural forms, homodimers, as well as hetero-oligomers. For example, the S100A8/S100A9 complex called calprotectin plays important roles in the regulation of inflammatory processes, wound repair, and regulating zinc-dependent enzymes as well as microbial growth. Pssm-ID: 240156 [Multi-domain] Cd Length: 88 Bit Score: 35.02 E-value: 8.91e-04
|
|||||||
| Blast search parameters | ||||
|
