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Conserved domains on  [gi|1034675270|ref|XP_016885330|]
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protein S100-G isoform X1 [Homo sapiens]

Protein Classification

S-100 domain-containing protein( domain architecture ID 10082979)

S-100 domain-containing protein contains the Ca-binding EF-hand motif; similar to Homo sapiens S100 proteins that are implicated in intracellular and extracellular regulatory activities

CATH:  1.10.238.10
Gene Ontology:  GO:0005509
PubMed:  2479149|10191494
SCOP:  3001983

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
S-100 cd00213
S-100: S-100 domain, which represents the largest family within the superfamily of proteins ...
 12-79 1.22e-20

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: 77.53  E-value: 1.22e-20
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1034675270 12 RIFEKYAAKEGDPDQLSKDELKLLIQAEFPSLLKG---PNTLDDLFQELDKNGDGEVSFEEFQVLVKKISQ 79
Cdd:cd00213   12 DVFHKYSGKEGDKDTLSKKELKELLETELPNFLKNqkdPEAVDKIMKDLDVNKDGKVDFQEFLVLIGKLAV 82
 
Name Accession Description Interval E-value
S-100 cd00213
S-100: S-100 domain, which represents the largest family within the superfamily of proteins ...
 12-79 1.22e-20

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: 77.53  E-value: 1.22e-20
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1034675270 12 RIFEKYAAKEGDPDQLSKDELKLLIQAEFPSLLKG---PNTLDDLFQELDKNGDGEVSFEEFQVLVKKISQ 79
Cdd:cd00213   12 DVFHKYSGKEGDKDTLSKKELKELLETELPNFLKNqkdPEAVDKIMKDLDVNKDGKVDFQEFLVLIGKLAV 82
S_100 pfam01023
S-100/ICaBP type calcium binding domain; The S-100 domain is a subfamily of the EF-hand ...
 12-47 3.94e-09

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: 47.05  E-value: 3.94e-09
                         10        20        30
                 ....*....|....*....|....*....|....*.
gi 1034675270 12 RIFEKYAAKEGDPDQLSKDELKLLIQAEFPSLLKGP 47
Cdd:pfam01023 10 DVFHKYAGKEGDKDTLSKKELKELLEKELPNFLKNQ 45
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
8-76 1.11e-07

Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 45.55  E-value: 1.11e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1034675270   8 EELKRIFEKYaakegDPD---QLSKDELKLLIQAefpsLLKGPNTLDDLFQELDKNGDGEVSFEEFQVLVKK 76
Cdd:COG5126    69 PFARAAFDLL-----DTDgdgKISADEFRRLLTA----LGVSEEEADELFARLDTDGDGKISFEEFVAAVRD 131
EFh smart00054
EF-hand, calcium binding motif; EF-hands are calcium-binding motifs that occur at least in ...
 50-77 3.44e-06

EF-hand, calcium binding motif; EF-hands are calcium-binding motifs that occur at least in pairs. Links between disease states and genes encoding EF-hands, particularly the S100 subclass, are emerging. Each motif consists of a 12 residue loop flanked on either side by a 12 residue alpha-helix. EF-hands undergo a conformational change unpon binding calcium ions.


Pssm-ID: 197492 [Multi-domain]  Cd Length: 29  Bit Score: 39.28  E-value: 3.44e-06
                          10        20
                  ....*....|....*....|....*...
gi 1034675270  50 LDDLFQELDKNGDGEVSFEEFQVLVKKI 77
Cdd:smart00054  2 LKEAFRLFDKDGDGKIDFEEFKDLLKAL 29
PLN02964 PLN02964
phosphatidylserine decarboxylase
 5-74 4.45e-04

phosphatidylserine decarboxylase


Pssm-ID: 215520 [Multi-domain]  Cd Length: 644  Bit Score: 36.76  E-value: 4.45e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1034675270   5 KSPEELKRIFEKYAAKEGDPD---QLSKDELKLLIQAeFPSLLKGpNTLDDLFQELDKNGDGEVSFEEFQVLV 74
Cdd:PLN02964  171 EDPVETERSFARRILAIVDYDedgQLSFSEFSDLIKA-FGNLVAA-NKKEELFKAADLNGDGVVTIDELAALL 241
XopAW NF041410
XopAW family type III secretion system calcium-binding effector;
27-74 1.98e-03

XopAW family type III secretion system calcium-binding effector;


Pssm-ID: 469301 [Multi-domain]  Cd Length: 227  Bit Score: 34.66  E-value: 1.98e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 1034675270  27 LSKDELKLLIQAEFPSLLKGPNT--LDDLFQELDKNGDGEVSFEEFQVLV 74
Cdd:NF041410   80 LSSDELAAAAPPPPPPPDQAPSTelADDLLSALDTDGDGSISSDELSAGL 129
XopAW NF041410
XopAW family type III secretion system calcium-binding effector;
27-70 6.51e-03

XopAW family type III secretion system calcium-binding effector;


Pssm-ID: 469301 [Multi-domain]  Cd Length: 227  Bit Score: 33.12  E-value: 6.51e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 1034675270  27 LSKDELK-LLIQAEFPSLLkgpNTLDDLFQELDKNGDGEVSFEEF 70
Cdd:NF041410   44 VSQDELSsALSSKSDDGSL---IDLSELFSDLDSDGDGSLSSDEL 85
 
Name Accession Description Interval E-value
S-100 cd00213
S-100: S-100 domain, which represents the largest family within the superfamily of proteins ...
 12-79 1.22e-20

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: 77.53  E-value: 1.22e-20
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1034675270 12 RIFEKYAAKEGDPDQLSKDELKLLIQAEFPSLLKG---PNTLDDLFQELDKNGDGEVSFEEFQVLVKKISQ 79
Cdd:cd00213   12 DVFHKYSGKEGDKDTLSKKELKELLETELPNFLKNqkdPEAVDKIMKDLDVNKDGKVDFQEFLVLIGKLAV 82
calgranulins cd05030
Calgranulins: S-100 domain found in proteins belonging to the Calgranulin subgroup of the S100 ...
 5-77 2.33e-18

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: 71.61  E-value: 2.33e-18
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1034675270  5 KSPEELKRIFEKYAAKEGDPDQLSKDELKLLIQAEFPSLLKGP---NTLDDLFQELDKNGDGEVSFEEFQVLVKKI 77
Cdd:cd05030    5 KAIETIINVFHQYSVRKGHPDTLYKKEFKQLVEKELPNFLKKEknqKAIDKIFEDLDTNQDGQLSFEEFLVLVIKV 80
S-100A10_like cd05031
S-100A10_like: S-100A10 domain found in proteins similar to S100A10. S100A10 is a member of ...
 5-74 3.12e-15

S-100A10_like: S-100A10 domain found in proteins similar to S100A10. S100A10 is a member of the S100 family of EF-hand superfamily of calcium-binding proteins. Note that the S-100 hierarchy, to which this S-100A1_like group belongs, 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. A unique feature of S100A10 is that it contains mutation in both of the calcium binding sites, making it calcium insensitive. S100A10 has been detected in brain, heart, gastrointestinal tract, kidney, liver, lung, spleen, testes, epidermis, aorta, and thymus. Structural data supports the homo- and hetero-dimeric as well as hetero-tetrameric nature of the protein. S100A10 has multiple binding partners in its calcium free state and is therefore involved in many diverse biological functions.


Pssm-ID: 240157 [Multi-domain]  Cd Length: 94  Bit Score: 63.98  E-value: 3.12e-15
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1034675270  5 KSPEELKRIFEKYAAKEGDPDQLSKDELKLLIQAEFPSLLKG---PNTLDDLFQELDKNGDGEVSFEEFQVLV 74
Cdd:cd05031    5 HAMESLILTFHRYAGKDGDKNTLSRKELKKLMEKELSEFLKNqkdPMAVDKIMKDLDQNRDGKVNFEEFVSLV 77
S-100A1 cd05025
S-100A1: S-100A1 domain found in proteins similar to S100A1. S100A1 is a calcium-binding ...
 8-74 8.89e-14

S-100A1: S-100A1 domain found in proteins similar to S100A1. S100A1 is a calcium-binding protein belonging to a large S100 vertebrate-specific protein family within the EF-hand superfamily of calcium-binding proteins. Note that the S-100 hierarchy, to which this S-100A1 group belongs, contains only S-100 EF-hand domains, other EF-hands have been modeled separately. As is the case with many other members of S100 protein family, S100A1 is implicated in intracellular and extracellular regulatory activities, including interaction with myosin-associated twitchin kinase, actin-capping protein CapZ, sinapsin I, and tubulin. Structural data suggests that S100A1 proteins exist within cells as antiparallel homodimers, while heterodimers with S100A4 and S100B also has been reported. Upon binding calcium S100A1 changes conformation to expose a hydrophobic cleft which is the interaction site of S100A1 with its more that 20 known target proteins.


Pssm-ID: 240152 [Multi-domain]  Cd Length: 92  Bit Score: 60.29  E-value: 8.89e-14
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034675270  8 EELKRIFEKYAAKEGDPDQLSKDELKLLIQAEFPSLL---KGPNTLDDLFQELDKNGDGEVSFEEFQVLV 74
Cdd:cd05025    9 ETLINVFHAHSGKEGDKYKLSKKELKDLLQTELSDFLdaqKDADAVDKIMKELDENGDGEVDFQEFVVLV 78
S-100Z cd05026
S-100Z: S-100Z domain found in proteins similar to S100Z. S100Z is a member of the S100 domain ...
 10-78 1.12e-11

S-100Z: S-100Z domain found in proteins similar to S100Z. S100Z is a member of the S100 domain family within the EF-hand Ca2+-binding proteins superfamily. Note that the S-100 hierarchy, to which this S-100Z group belongs, contains only S-100 EF-hand domains, other EF-hands have been modeled separately.S100 proteins exhibit unique patterns of tissue- and cell type-specific expression and have been implicated in the Ca2+-dependent regulation of diverse physiological processes, including cell cycle regulation, differentiation, growth, and metabolic control. S100Z is normally expressed in various tissues, with its highest level of expression being in spleen and leukocytes. The function of S100Z remains unclear. Preliminary structural data suggests that S100Z is homodimer, however a heterodimer with S100P has been reported. S100Z is capable of binding calcium ions. When calcium binds to S110Z, the protein experiences a conformational change, which exposes hydrophobic surfaces on the protein. In comparison with their normal tissue counterparts, S100Z gene expression appears to be deregulated in some tumor tissues.


Pssm-ID: 240153 [Multi-domain]  Cd Length: 93  Bit Score: 54.88  E-value: 1.12e-11
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1034675270 10 LKRIFEKYAAKEGDPDQLSKDELKLLIQAEFPSLL---KGPNTLDDLFQELDKNGDGEVSFEEFQVLVKKIS 78
Cdd:cd05026   12 LIRIFHNYSGKEGDRYKLSKGELKELLQRELTDFLssqKDPMLVDKIMNDLDSNKDNEVDFNEFVVLVAALT 83
S-100A11 cd05023
S-100A11: S-100A11 domain found in proteins similar to S100A11. S100A11 is a member of the ...
 3-74 4.81e-11

S-100A11: S-100A11 domain found in proteins similar to S100A11. S100A11 is a member of the S-100 domain family within EF-hand Ca2+-binding proteins superfamily. Note that the S-100 hierarchy, to which this S-100A11 group belongs, contains only S-100 EF-hand domains, other EF-hands have been modeled separately. S100 proteins exhibit unique patterns of tissue- and cell type-specific expression and have been implicated in the Ca2+-dependent regulation of diverse physiological processes, including cell cycle regulation, differentiation, growth, and metabolic control . S100 proteins have also been associated with a variety of pathological events, including neoplastic transformation and neurodegenerative diseases such as Alzheimer's, usually via over expression of the protein. S100A11 is expressed in smooth muscle and other tissues and involves in calcium-dependent membrane aggregation, which is important for cell vesiculation . As is the case for many other S100 proteins, S100A11 is homodimer, which is able to form a heterodimer with S100B through subunit exchange. Ca2+ binding to S100A11 results in a conformational change in the protein, exposing a hydrophobic surface that interacts with target proteins. In addition to binding to annexin A1 and A6 S100A11 also interacts with actin and transglutaminase.


Pssm-ID: 240150 [Multi-domain]  Cd Length: 89  Bit Score: 53.23  E-value: 4.81e-11
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1034675270  3 TKKSPEELKRIFEKYAAKEGDPDQLSKDELKLLIQAEFPSLLKG---PNTLDDLFQELDKNGDGEVSFEEFQVLV 74
Cdd:cd05023    4 TERCIESLIAVFQKYAGKDGDSYQLSKTEFLSFMNTELASFTKNqkdPGVLDRMMKKLDLNSDGQLDFQEFLNLI 78
S-100B cd05027
S-100B: S-100B domain found in proteins similar to S100B. S100B is a calcium-binding protein ...
 13-78 2.60e-10

S-100B: S-100B domain found in proteins similar to S100B. S100B is a calcium-binding protein belonging to a large S100 vertebrate-specific protein family within the EF-hand superfamily of calcium-binding proteins. Note that the S-100 hierarchy, to which this S-100B group belongs, contains only S-100 EF-hand domains, other EF-hands have been modeled separately. S100B is most abundant in glial cells of the central nervous system, predominately in astrocytes. S100B is involved in signal transduction via the inhibition of protein phoshorylation, regulation of enzyme activity and by affecting the calcium homeostasis. Upon calcium binding the S100B homodimer changes conformation to expose a hydrophobic cleft, which represents the interaction site of S100B with its more than 20 known target proteins. These target proteins include several cellular architecture proteins such as tubulin and GFAP; S100B can inhibit polymerization of these oligomeric molecules. Furthermore, S100B inhibits the phosphorylation of multiple kinase substrates including the Alzheimer protein tau and neuromodulin (GAP-43) through a calcium-sensitive interaction with the protein substrates.


Pssm-ID: 240154 [Multi-domain]  Cd Length: 88  Bit Score: 51.40  E-value: 2.60e-10
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1034675270 13 IFEKYAAKEGDPDQLSKDELKLLIQAEFPSLL---KGPNTLDDLFQELDKNGDGEVSFEEFQVLVKKIS 78
Cdd:cd05027   13 VFHQYSGREGDKHKLKKSELKELINNELSHFLeeiKEQEVVDKVMETLDSDGDGECDFQEFMAFVAMVT 81
S_100 pfam01023
S-100/ICaBP type calcium binding domain; The S-100 domain is a subfamily of the EF-hand ...
 12-47 3.94e-09

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: 47.05  E-value: 3.94e-09
                         10        20        30
                 ....*....|....*....|....*....|....*.
gi 1034675270 12 RIFEKYAAKEGDPDQLSKDELKLLIQAEFPSLLKGP 47
Cdd:pfam01023 10 DVFHKYAGKEGDKDTLSKKELKELLEKELPNFLKNQ 45
S-100A13 cd05022
S-100A13: S-100A13 domain found in proteins similar to S100A13. S100A13 is a calcium-binding ...
 5-79 1.24e-08

S-100A13: S-100A13 domain found in proteins similar to S100A13. S100A13 is a calcium-binding protein belonging to a large S100 vertebrate-specific protein family within the EF-hand superfamily of calcium-binding proteins. Note that the S-100 hierarchy, to which this S-100A13 group belongs, contains only S-100 EF-hand domains, other EF-hands have been modeled separately. S100A13 is involved in the cellular export of interleukin-1 (IL-1) and of fibroblast growth factor-1 (FGF-1), which plays an important role in angiogenesis and tissue regeneration. Export is based on the CuII-dependent formation of multiprotein complexes containing the S100A13 protein. Assembly of these complexes occurs near the inner surface of the plasma membrane. Binding of two Ca(II) ions per monomer triggers key conformational changes leading to the creation of two identical and symmetrical Cu(II)-binding sites on the surface of the protein, close to the interface between the two monomers. These Cu(II)-binding sites are unique among the S100 proteins, which are reported to bind Cu(II) or Zn(II) ions in addition to Ca(II) ions. In addition, the three-dimensional structure of S100A13 differs significantly from those of other S100 proteins; the hydrophobic pocket that largely contributes to protein-protein interactions in other S100 proteins is absent in S100A13. The structure of S100A13 contains a large patch of negatively charged residues flanked by dense cationic clusters, formed mostly from positively charged residues from the C-terminal end, which plays major role in binding FGF-1.


Pssm-ID: 240149 [Multi-domain]  Cd Length: 89  Bit Score: 46.95  E-value: 1.24e-08
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1034675270  5 KSPEELKRIFEKYAaKEGDPDQLSKDELKLLIQAEFPSLLKGPNTLDDLFQELDKNGDGEVSFEEFQVLVKKISQ 79
Cdd:cd05022    5 KAIETLVSNFHKAS-VKGGKESLTASEFQELLTQQLPHLLKDVEGLEEKMKNLDVNQDSKLSFEEFWELIGELAK 78
S-100A6 cd05029
S-100A6: S-100A6 domain found in proteins similar to S100A6. S100A6 is a member of the S100 ...
 13-70 5.16e-08

S-100A6: S-100A6 domain found in proteins similar to S100A6. S100A6 is a member of the S100 domain family within EF-hand Ca2+-binding proteins superfamily. Note that the S-100 hierarchy, to which this S-100A6 group belongs, contains only S-100 EF-hand domains, other EF-hands have been modeled separately. S100 proteins exhibit unique patterns of tissue- and cell type-specific expression and have been implicated in the Ca2+-dependent regulation of diverse physiological processes, including cell cycle regulation, differentiation, growth, and metabolic control . S100A6 is normally expressed in the G1 phase of the cell cycle in neuronal cells. The function of S100A6 remains unclear, but evidence suggests that it is involved in cell cycle regulation and exocytosis. S100A6 may also be involved in tumorigenesis; the protein is overexpressed in several tumors. Ca2+ binding to S100A6 leads to a conformational change in the protein, which exposes a hydrophobic surface for interaction with target proteins. Several such proteins have been identified: glyceraldehyde-3-phosphate dehydrogenase , annexins 2, 6 and 11 and Calcyclin-Binding Protein (CacyBP).


Pssm-ID: 240155 [Multi-domain]  Cd Length: 88  Bit Score: 45.60  E-value: 5.16e-08
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1034675270 13 IFEKYAAKEGDPDQLSKDELKLLIQAEfpsLLKGPNTLD----DLFQELDKNGDGEVSFEEF 70
Cdd:cd05029   15 IFHKYSGREGDKNTLSKKELKELIQKE---LTIGSKLQDaeiaKLMEDLDRNKDQEVNFQEY 73
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
8-76 1.11e-07

Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 45.55  E-value: 1.11e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1034675270   8 EELKRIFEKYaakegDPD---QLSKDELKLLIQAefpsLLKGPNTLDDLFQELDKNGDGEVSFEEFQVLVKK 76
Cdd:COG5126    69 PFARAAFDLL-----DTDgdgKISADEFRRLLTA----LGVSEEEADELFARLDTDGDGKISFEEFVAAVRD 131
EFh cd00051
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal ...
 9-75 2.95e-07

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.


Pssm-ID: 238008 [Multi-domain]  Cd Length: 63  Bit Score: 42.92  E-value: 2.95e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1034675270  9 ELKRIFEKYAaKEGDpDQLSKDELKLLIQAEFPSLLKgpNTLDDLFQELDKNGDGEVSFEEFQVLVK 75
Cdd:cd00051    1 ELREAFRLFD-KDGD-GTISADELKAALKSLGEGLSE--EEIDEMIREVDKDGDGKIDFEEFLELMA 63
EF-hand_7 pfam13499
EF-hand domain pair;
8-75 8.12e-07

EF-hand domain pair;


Pssm-ID: 463900 [Multi-domain]  Cd Length: 67  Bit Score: 41.86  E-value: 8.12e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1034675270  8 EELKRIFEKYaakegDPDQ---LSKDELKLLIQAEFPSLLKGPNTLDDLFQELDKNGDGEVSFEEFQVLVK 75
Cdd:pfam13499  2 EKLKEAFKLL-----DSDGdgyLDVEELKKLLRKLEEGEPLSDEEVEELFKEFDLDKDGRISFEEFLELYS 67
S-100A10 cd05024
S-100A10: A subgroup of the S-100A10 domain found in proteins similar to S100A10. S100A10 is a ...
 6-74 2.20e-06

S-100A10: A subgroup of the S-100A10 domain found in proteins similar to S100A10. S100A10 is a member of the S100 family of EF-hand superfamily of calcium-binding proteins. Note that the S-100 hierarchy, to which this S-100A10 group belongs, 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. A unique feature of S100A10 is that it contains mutation in both of the calcium binding sites, making it calcium insensitive. S100A10 has been detected in brain, heart, gastrointestinal tract, kidney, liver, lung, spleen, testes, epidermis, aorta, and thymus. Structural data supports the homo- and hetero-dimeric as well as hetero-tetrameric nature of the protein. S100A10 has multiple binding partners in its calcium free state and is therefore involved in many diverse biological functions.


Pssm-ID: 240151 [Multi-domain]  Cd Length: 91  Bit Score: 41.37  E-value: 2.20e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1034675270  6 SPEELKRIFEKYAakeGDPDQLSKDELKLLIQAEFPSLLKG---PNTLDDLFQELDKNGDGEVSFEEFQVLV 74
Cdd:cd05024    6 SMEKMMLTFHKFA---GEKNYLNRDDLQKLMEKEFSEFLKNqndPMAVDKIMKDLDDCRDGKVGFQSFFSLI 74
EFh smart00054
EF-hand, calcium binding motif; EF-hands are calcium-binding motifs that occur at least in ...
 50-77 3.44e-06

EF-hand, calcium binding motif; EF-hands are calcium-binding motifs that occur at least in pairs. Links between disease states and genes encoding EF-hands, particularly the S100 subclass, are emerging. Each motif consists of a 12 residue loop flanked on either side by a 12 residue alpha-helix. EF-hands undergo a conformational change unpon binding calcium ions.


Pssm-ID: 197492 [Multi-domain]  Cd Length: 29  Bit Score: 39.28  E-value: 3.44e-06
                          10        20
                  ....*....|....*....|....*...
gi 1034675270  50 LDDLFQELDKNGDGEVSFEEFQVLVKKI 77
Cdd:smart00054  2 LKEAFRLFDKDGDGKIDFEEFKDLLKAL 29
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
6-77 7.24e-06

Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 40.93  E-value: 7.24e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1034675270   6 SPEELKRIFE---KYAAKEGDPD---QLSKDELKLLIQAEFPSLLKgpNTLDDLFQELDKNGDGEVSFEEFQVLVKKI 77
Cdd:COG5126    23 ERDDFEALFRrlwATLFSEADTDgdgRISREEFVAGMESLFEATVE--PFARAAFDLLDTDGDGKISADEFRRLLTAL 98
EF-hand_1 pfam00036
EF hand; The EF-hands can be divided into two classes: signalling proteins and buffering ...
 50-77 9.62e-06

EF hand; The EF-hands can be divided into two classes: signalling proteins and buffering/transport proteins. The first group is the largest and includes the most well-known members of the family such as calmodulin, troponin C and S100B. These proteins typically undergo a calcium-dependent conformational change which opens a target binding site. The latter group is represented by calbindin D9k and do not undergo calcium dependent conformational changes.


Pssm-ID: 425435 [Multi-domain]  Cd Length: 29  Bit Score: 38.15  E-value: 9.62e-06
                         10        20
                 ....*....|....*....|....*...
gi 1034675270 50 LDDLFQELDKNGDGEVSFEEFQVLVKKI 77
Cdd:pfam00036  2 LKEIFRLFDKDGDGKIDFEEFKELLKKL 29
EF-hand_5 pfam13202
EF hand;
50-74 2.96e-05

EF hand;


Pssm-ID: 433035 [Multi-domain]  Cd Length: 25  Bit Score: 36.91  E-value: 2.96e-05
                         10        20
                 ....*....|....*....|....*
gi 1034675270 50 LDDLFQELDKNGDGEVSFEEFQVLV 74
Cdd:pfam13202  1 LKDTFRQIDLNGDGKISKEELRRLL 25
PLN02964 PLN02964
phosphatidylserine decarboxylase
 5-74 4.45e-04

phosphatidylserine decarboxylase


Pssm-ID: 215520 [Multi-domain]  Cd Length: 644  Bit Score: 36.76  E-value: 4.45e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1034675270   5 KSPEELKRIFEKYAAKEGDPD---QLSKDELKLLIQAeFPSLLKGpNTLDDLFQELDKNGDGEVSFEEFQVLV 74
Cdd:PLN02964  171 EDPVETERSFARRILAIVDYDedgQLSFSEFSDLIKA-FGNLVAA-NKKEELFKAADLNGDGVVTIDELAALL 241
EFh_CREC cd15899
EF-hand, calcium binding motif, found in CREC-EF hand family; The CREC (Cab45/reticulocalbin ...
 2-70 1.55e-03

EF-hand, calcium binding motif, found in CREC-EF hand family; The CREC (Cab45/reticulocalbin/ERC45/calumenin)-EF hand family contains a group of six EF-hand, low-affinity Ca2+-binding proteins, including reticulocalbin (RCN-1), ER Ca2+-binding protein of 55 kDa (ERC-55, also known as TCBP-49 or E6BP), reticulocalbin-3 (RCN-3), Ca2+-binding protein of 45 kDa (Cab45 and its splice variant Cab45b), and calumenin ( also known as crocalbin or CBP-50). The proteins are not only localized in various parts of the secretory pathway, but also found in the cytosolic compartment and at the cell surface. They interact with different ligands or proteins and have been implicated in the secretory process, chaperone activity, signal transduction as well as in a large variety of disease processes.


Pssm-ID: 320021 [Multi-domain]  Cd Length: 267  Bit Score: 35.11  E-value: 1.55e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034675270   2 STKKSPEELKRIFEKyAAKEGDPdQLSKDE-LKLLIQAEFPSLLkgPNTLDDLFQELDKNGDGEVSFEEF 70
Cdd:cd15899   117 EYKKLLLKDKKRFEA-ADQDGDL-ILTLEEfLAFLHPEESPYML--DFVIKETLEDLDKNGDGFISLEEF 182
XopAW NF041410
XopAW family type III secretion system calcium-binding effector;
27-74 1.98e-03

XopAW family type III secretion system calcium-binding effector;


Pssm-ID: 469301 [Multi-domain]  Cd Length: 227  Bit Score: 34.66  E-value: 1.98e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 1034675270  27 LSKDELKLLIQAEFPSLLKGPNT--LDDLFQELDKNGDGEVSFEEFQVLV 74
Cdd:NF041410   80 LSSDELAAAAPPPPPPPDQAPSTelADDLLSALDTDGDGSISSDELSAGL 129
EFh_parvalbumin_beta cd16255
EF-hand, calcium binding motif, found in beta-parvalbumin; Beta-parvalbumin, also termed ...
 3-75 3.30e-03

EF-hand, calcium binding motif, found in beta-parvalbumin; Beta-parvalbumin, also termed Oncomodulin-1 (OM), is a small calcium-binding protein that is expressed in hepatomas, as well as in the blastocyst and the cytotrophoblasts of the placenta. It is also found to be expressed in the cochlear outer hair cells of the organ of Corti and frequently expressed in neoplasms. Mammalian beta-parvalbumin is secreted by activated macrophages and neutrophils. It may function as a tissue-specific Ca2+-dependent regulatory protein, and may also serve as a specialized cytosolic Ca2+ buffer. Beta-parvalbumin acts as a potent growth-promoting signal between the innate immune system and neurons in vivo. It has high and specific affinity for its receptor on retinal ganglion cells (RGC) and functions as the principal mediator of optic nerve regeneration. It exerts its effects in a cyclic adenosine monophosphate (cAMP)-dependent manner and can further elevate intracellular cAMP levels. Moreover, beta-parvalbumin is associated with efferent function and outer hair cell electromotility, and can identify different hair cell types in the mammalian inner ear. Beta-parvalbumin is characterized by the presence of three consecutive EF-hand motifs (helix-loop-helix) called AB, CD, and EF, but only CD and EF can chelate metal ions, such as Ca2+ and Mg2+. The EF site displays a high-affinity for Ca2+/Mg2+, and the CD site is a low-affinity Ca2+-specific site. In addition, beta-parvalbumin is distinguished from other parvalbumins by its unusually low isoelectric point (pI = 3.1) and sequence eccentricities (e.g., Y57-L58-D59 instead of F57-I58-E59).


Pssm-ID: 319998 [Multi-domain]  Cd Length: 101  Bit Score: 33.17  E-value: 3.30e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1034675270   3 TKKSPEELKRIFEkyAAKEGDPDQLSKDELKLLIQaEFPSllkGPNTLDD-----LFQELDKNGDGEVSFEEFQVLVK 75
Cdd:cd16255    29 SKKSADDVKKVFE--IIDQDKSGFIEEEELKLFLQ-NFSS---GARELTDaetkaFLKAGDSDGDGKIGVEEFQALVK 100
EFh_PEF cd15897
The penta-EF hand (PEF) family; The penta-EF hand (PEF) family contains a group of five ...
 9-77 4.07e-03

The penta-EF hand (PEF) family; The penta-EF hand (PEF) family contains a group of five EF-hand calcium-binding proteins, including several classical calpain large catalytic subunits (CAPN1, 2, 3, 8, 9, 11, 12, 13, 14), two calpain small subunits (CAPNS1 and CAPNS2), as well as non-calpain PEF proteins, ALG-2 (apoptosis-linked gene 2, also termed programmed cell death protein 6, PDCD6), peflin, sorcin, and grancalcin. Based on the sequence similarity of EF1 hand, ALG-2 and peflin have been classified into group I PEF proteins. Calcium-dependent protease calpain subfamily members, sorcin and grancalcin, are group II PEF proteins. Calpains (EC 3.4.22.17) are calcium-activated intracellular cysteine proteases that play important roles in the degradation or functional modulation in a variety of substrates. They have been implicated in a number of physiological processes such as cell cycle progression, remodeling of cytoskeletal-cell membrane attachments, signal transduction, gene expression and apoptosis. ALG-2 is a pro-apoptotic factor that forms a homodimer in the cell or a heterodimer with its closest paralog peflin through their EF5s. Peflin is a 30-kD PEF protein with a longer N-terminal hydrophobic domain than any other member of the PEF family, and it contains nine nonapeptide (A/PPGGPYGGP) repeats. It exists only as a heterodimer with ALG-2. The dissociation of heterodimer occurs in the presence of Ca2+. ALG-2 interacts with various proteins in a Ca2+-dependent manner. Sorcin (for soluble resistance-related calcium binding protein) is a soluble resistance-related calcium-binding protein that participates in the regulation of calcium homeostasis in cells. Grancalcin is a cytosolic Ca2+-binding protein specifically expressed in neutrophils and monocytes/macrophages. It plays a key role in leukocyte-specific functions that are responsible for host defense. Grancalcin can form a heterodimer together with sorcin. Members in this family contain five EF-hand motifs attached to an N-terminal region of variable length containing one or more short Gly/Pro-rich sequences. These proteins form homodimers or heterodimers through pairing between the 5th EF-hands from the two molecules. Unlike calmodulin, the PEF domains do not undergo major conformational changes upon binding Ca2+.


Pssm-ID: 320054 [Multi-domain]  Cd Length: 165  Bit Score: 33.56  E-value: 4.07e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1034675270   9 ELKRIFEKYAakeGDPDQLSKDEL-KLLIQA--EFPSLLKGPNTLDDLFQELDKNGDGEVSFEEFQVLVKKI 77
Cdd:cd15897     1 QLRNVFQAVA---GDDGEISATELqQALSNVgwTHFDLGFSLETCRSMIAMMDRDHSGKLNFSEFKGLWNYI 69
EF-hand_6 pfam13405
EF-hand domain;
50-77 4.09e-03

EF-hand domain;


Pssm-ID: 463869 [Multi-domain]  Cd Length: 30  Bit Score: 31.76  E-value: 4.09e-03
                         10        20
                 ....*....|....*....|....*...
gi 1034675270 50 LDDLFQELDKNGDGEVSFEEFQVLVKKI 77
Cdd:pfam13405  2 LREAFKLFDKDGDGKISLEELRKALRSL 29
EFh_PI-PLC cd15898
EF-hand motif found in eukaryotic phosphoinositide-specific phospholipase C (PI-PLC, EC 3.1.4. ...
 10-79 5.54e-03

EF-hand motif found in eukaryotic phosphoinositide-specific phospholipase C (PI-PLC, EC 3.1.4.11) isozymes; PI-PLC isozymes are signaling enzymes that hydrolyze the membrane phospholipids phosphatidylinositol-4,5-bisphosphate (PIP2) to generate two important second messengers in eukaryotic signal transduction cascades, Inositol 1,4,5-trisphosphate (InsP3) and diacylglycerol (DAG). InsP3 triggers inflow of calcium from intracellular stores, while DAG, together with calcium, activates protein kinase C, which goes on to phosphorylate other molecules, leading to altered cellular activity. Calcium is required for the catalysis. This family corresponds to the four EF-hand motifs containing PI-PLC isozymes, including PI-PLC-beta (1-4), -gamma (1-2), -delta (1,3,4), -epsilon (1), -zeta (1), eta (1-2). Lower eukaryotes such as yeast and slime molds contain only delta-type isozymes. In contrast, other types of isoforms present in higher eukaryotes. This family also includes 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase 1 (PLC1) from fungi. Some homologs from plants contain only two atypical EF-hand motifs and they are not included. All PI-PLC isozymes except sperm-specific PI-PLC-zeta share a core set of domains, including an N-terminal pleckstrin homology (PH) domain, four atypical EF-hand motifs, a PLC catalytic core, and a single C2 domain. PI-PLC-zeta lacks the PH domain. The PLC catalytic core domain is a TIM barrel with two highly conserved regions (X and Y) split by a highly degenerate linker sequence. Most of EF-hand motifs found in PI-PLCs consist of a helix-loop-helix structure, but lack residues critical to metal binding. Moreover, the EF-hand region of most of PI-PLCs may have an important regulatory function, but it has yet to be identified. However, PI-PLC-zeta is a key exception. It is responsible for Ca2+ oscillations in fertilized oocytes and exhibits a high sensitivity to Ca2+ mediated through its EF-hand domain. In addition, PI-PLC-eta2 shows a canonical EF-loop directing Ca2+-sensitivity and thus can amplify transient Ca2+ signals. Also it appears that PI-PLC-delta1 can regulate the binding of PH domain to PIP2 in a Ca2+-dependent manner through its functionally important EF-hand domains. PI-PLCs can be activated by a variety of extracellular ligands, such as growth factors, hormones, cytokines and lipids. Their activation has been implicated in tumorigenesis and/or metastasis linked to migration, proliferation, growth, inflammation, angiogenesis and actin cytoskeleton reorganization. PI-PLC-beta isozymes are activated by G-protein coupled receptor (GPCR) through different mechanisms. However, PI-PLC-gamma isozymes are activated by receptor tyrosine kinase (RTK), such as Rho and Ras GTPases. In contrast, PI-PLC-epsilon are activated by both GPCR and RTK. PI-PLC-delta1 and PLC-eta 1 are activated by GPCR-mediated calcium mobilization. The activation mechanism for PI-PLC-zeta remains unclear.


Pssm-ID: 320029 [Multi-domain]  Cd Length: 137  Bit Score: 33.02  E-value: 5.54e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034675270  10 LKRIFEKyAAKEGDpDQLSKDELKLLIQAEFPSLLKGpnTLDDLFQELDKNGDGEVSFEEFQVLVKKISQ 79
Cdd:cd15898     2 LRRQWIK-ADKDGD-GKLSLKEIKKLLKRLNIRVSEK--ELKKLFKEVDTNGDGTLTFDEFEELYKSLTE 67
PTZ00183 PTZ00183
centrin; Provisional
 1-76 5.80e-03

centrin; Provisional


Pssm-ID: 185503 [Multi-domain]  Cd Length: 158  Bit Score: 33.12  E-value: 5.80e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034675270   1 MSTKKSPEELKRIFEKYaakegDPDQLSKDELKLL--IQAEFpsllkGPNTLDDLFQEL----DKNGDGEVSFEEFQVLV 74
Cdd:PTZ00183   83 LGERDPREEILKAFRLF-----DDDKTGKISLKNLkrVAKEL-----GETITDEELQEMideaDRNGDGEISEEEFYRIM 152


                  ..
gi 1034675270  75 KK 76
Cdd:PTZ00183  153 KK 154
XopAW NF041410
XopAW family type III secretion system calcium-binding effector;
27-70 6.51e-03

XopAW family type III secretion system calcium-binding effector;


Pssm-ID: 469301 [Multi-domain]  Cd Length: 227  Bit Score: 33.12  E-value: 6.51e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 1034675270  27 LSKDELK-LLIQAEFPSLLkgpNTLDDLFQELDKNGDGEVSFEEF 70
Cdd:NF041410   44 VSQDELSsALSSKSDDGSL---IDLSELFSDLDSDGDGSLSSDEL 85
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

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