NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|237649019|ref|NP_001153682|]
View 

calcium-binding mitochondrial carrier protein Aralar2 isoform 1 [Homo sapiens]

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

Name Accession Description Interval E-value
Mito_carr pfam00153
Mitochondrial carrier protein;
517-608 1.08e-31

Mitochondrial carrier protein;


:

Pssm-ID: 249634  Cd Length: 96  Bit Score: 118.89  E-value: 1.08e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237649019  517 GQVSPGSLLLAGAIAGMPAASLVTPADVIKTRLQVAARAGQTTYSGVIDCFRKILREEGPKALWKGAGARVFRSSPQFGV 596
Cdd:pfam00153   1 SPLSFLASLLAGGIAGAIAATVTYPLDVVKTRLQSSAAGGSRKYKGILDCFKKIYKEEGIRGLYKGLLPNLLRVAPAAAI 80
                          90
                  ....*....|..
gi 237649019  597 TLLTYELLQRWF 608
Cdd:pfam00153  81 YFGTYETLKKLL 92
Mito_carr pfam00153
Mitochondrial carrier protein;
332-424 4.87e-27

Mitochondrial carrier protein;


:

Pssm-ID: 249634  Cd Length: 96  Bit Score: 106.18  E-value: 4.87e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237649019  332 RFGLGSVAGAVGATAVYPIDLVKTRMQNQRSTGSfvgeLMYKNSFDCFKKVLRYEGFFGLYRGLLPQLLGVAPEKAIKLT 411
Cdd:pfam00153   8 SLLAGGIAGAIAATVTYPLDVVKTRLQSSAAGGS----RKYKGILDCFKKIYKEEGIRGLYKGLLPNLLRVAPAAAIYFG 83
                          90
                  ....*....|...
gi 237649019  412 VNDFVRDKFMHKD 424
Cdd:pfam00153  84 TYETLKKLLLKKL 96
Mito_carr pfam00153
Mitochondrial carrier protein;
425-512 1.78e-17

Mitochondrial carrier protein;


:

Pssm-ID: 249634  Cd Length: 96  Bit Score: 78.83  E-value: 1.78e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237649019  425 GSVPLAAEILAGGCAGGSQVIFTNPLEIVKIRLQVAGEIT----TGPRVSALSVVRDLGFFGIYKGAKACFLRDIPFSAI 500
Cdd:pfam00153   1 SPLSFLASLLAGGIAGAIAATVTYPLDVVKTRLQSSAAGGsrkyKGILDCFKKIYKEEGIRGLYKGLLPNLLRVAPAAAI 80
                          90
                  ....*....|..
gi 237649019  501 YFPCYAHVKASF 512
Cdd:pfam00153  81 YFGTYETLKKLL 92
S-100 cd00213
S-100: S-100 domain, which represents the largest family within the superfamily of proteins ...
19-81 3.52e-04

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: 39.40  E-value: 3.52e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 237649019  19 TIFLKYASIEKNGEFfMSPNDF---VTRYLNIFGESQPNPKTVELLSGVVDQTKDGLISFQEFVAF 81
Cdd:cd00213   12 DVFHKYSGKEGDKDT-LSKKELkelLETELPNFLKNQKDPEAVDKIMKDLDVNKDGKVDFQEFLVL 76
PTZ00168 PTZ00168
mitochondrial carrier protein; Provisional
328-591 6.85e-13

mitochondrial carrier protein; Provisional


:

Pssm-ID: 185494 [Multi-domain]  Cd Length: 259  Bit Score: 68.03  E-value: 6.85e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237649019 328 ESAYRFGLGSVAGAVGATAVYPIDLVKTRMQNQRSTgsfvgelmyknSFDCFKKvlryegffgLYRGLLPQLLGVAPEKA 407
Cdd:PTZ00168   2 EHFHNLVTGALSGVIVDAVLYPIDSIKTNIQAKKSF-----------SFSDIKK---------LYSGILPTLVGTVPASA 61
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237649019 408 IKLTVNDFVRDKFMHKDGSVPLAA-EILAGGCAGGSQVIFTNPLEIVKIRLQVAGEITTGPRVSALSVVRDLGFFgIYKG 486
Cdd:PTZ00168  62 FFYCFYELSKKLLTEYRENISKTNlYLISTSIAEITACIVRLPFEIVKQNMQVSGNISVLKTIYEITQREGLPSF-LGKS 140
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237649019 487 AKACFLRDIPFSAIYFPCYAHVKASFANEDGQVS---PG-SLLLAGAIAGMPAASLVTPADVIKTRlqvaaragQTTY-S 561
Cdd:PTZ00168 141 YFVMIVREIPFDCIQYFLWETLKEKAKKDFGKFSkkyPSiTSAICGGLAGGIAGFLTTPVDVIKSR--------QIIYgK 212
                        250       260       270
                 ....*....|....*....|....*....|
gi 237649019 562 GVIDCFRKIlREEGPKALWKGAgarVFRSS 591
Cdd:PTZ00168 213 SYIETVTEI-AEEGYLTFYKGC---CFRSS 238
EF-hand_7 pfam13499
EF-hand domain pair;
29-81 1.09e-03

EF-hand domain pair;


:

Pssm-ID: 257819 [Multi-domain]  Cd Length: 60  Bit Score: 37.75  E-value: 1.09e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 237649019   29 KNGEFFMSPNDFVtRYLNIFGESQPN---PKTVELLSGVVDQTKDGLISFQEFVAF 81
Cdd:pfam13499   5 KDGDGYIDVEELR-KLLKALGLKLTDeevEELLEYDFNEFDKDGDGRISFEEFLEA 59
 
Name Accession Description Interval E-value
Mito_carr pfam00153
Mitochondrial carrier protein;
517-608 1.08e-31

Mitochondrial carrier protein;


Pssm-ID: 249634  Cd Length: 96  Bit Score: 118.89  E-value: 1.08e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237649019  517 GQVSPGSLLLAGAIAGMPAASLVTPADVIKTRLQVAARAGQTTYSGVIDCFRKILREEGPKALWKGAGARVFRSSPQFGV 596
Cdd:pfam00153   1 SPLSFLASLLAGGIAGAIAATVTYPLDVVKTRLQSSAAGGSRKYKGILDCFKKIYKEEGIRGLYKGLLPNLLRVAPAAAI 80
                          90
                  ....*....|..
gi 237649019  597 TLLTYELLQRWF 608
Cdd:pfam00153  81 YFGTYETLKKLL 92
Mito_carr pfam00153
Mitochondrial carrier protein;
332-424 4.87e-27

Mitochondrial carrier protein;


Pssm-ID: 249634  Cd Length: 96  Bit Score: 106.18  E-value: 4.87e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237649019  332 RFGLGSVAGAVGATAVYPIDLVKTRMQNQRSTGSfvgeLMYKNSFDCFKKVLRYEGFFGLYRGLLPQLLGVAPEKAIKLT 411
Cdd:pfam00153   8 SLLAGGIAGAIAATVTYPLDVVKTRLQSSAAGGS----RKYKGILDCFKKIYKEEGIRGLYKGLLPNLLRVAPAAAIYFG 83
                          90
                  ....*....|...
gi 237649019  412 VNDFVRDKFMHKD 424
Cdd:pfam00153  84 TYETLKKLLLKKL 96
Mito_carr pfam00153
Mitochondrial carrier protein;
425-512 1.78e-17

Mitochondrial carrier protein;


Pssm-ID: 249634  Cd Length: 96  Bit Score: 78.83  E-value: 1.78e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237649019  425 GSVPLAAEILAGGCAGGSQVIFTNPLEIVKIRLQVAGEIT----TGPRVSALSVVRDLGFFGIYKGAKACFLRDIPFSAI 500
Cdd:pfam00153   1 SPLSFLASLLAGGIAGAIAATVTYPLDVVKTRLQSSAAGGsrkyKGILDCFKKIYKEEGIRGLYKGLLPNLLRVAPAAAI 80
                          90
                  ....*....|..
gi 237649019  501 YFPCYAHVKASF 512
Cdd:pfam00153  81 YFGTYETLKKLL 92
S-100 cd00213
S-100: S-100 domain, which represents the largest family within the superfamily of proteins ...
19-81 3.52e-04

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: 39.40  E-value: 3.52e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 237649019  19 TIFLKYASIEKNGEFfMSPNDF---VTRYLNIFGESQPNPKTVELLSGVVDQTKDGLISFQEFVAF 81
Cdd:cd00213   12 DVFHKYSGKEGDKDT-LSKKELkelLETELPNFLKNQKDPEAVDKIMKDLDVNKDGKVDFQEFLVL 76
PTZ00168 PTZ00168
mitochondrial carrier protein; Provisional
328-591 6.85e-13

mitochondrial carrier protein; Provisional


Pssm-ID: 185494 [Multi-domain]  Cd Length: 259  Bit Score: 68.03  E-value: 6.85e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237649019 328 ESAYRFGLGSVAGAVGATAVYPIDLVKTRMQNQRSTgsfvgelmyknSFDCFKKvlryegffgLYRGLLPQLLGVAPEKA 407
Cdd:PTZ00168   2 EHFHNLVTGALSGVIVDAVLYPIDSIKTNIQAKKSF-----------SFSDIKK---------LYSGILPTLVGTVPASA 61
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237649019 408 IKLTVNDFVRDKFMHKDGSVPLAA-EILAGGCAGGSQVIFTNPLEIVKIRLQVAGEITTGPRVSALSVVRDLGFFgIYKG 486
Cdd:PTZ00168  62 FFYCFYELSKKLLTEYRENISKTNlYLISTSIAEITACIVRLPFEIVKQNMQVSGNISVLKTIYEITQREGLPSF-LGKS 140
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237649019 487 AKACFLRDIPFSAIYFPCYAHVKASFANEDGQVS---PG-SLLLAGAIAGMPAASLVTPADVIKTRlqvaaragQTTY-S 561
Cdd:PTZ00168 141 YFVMIVREIPFDCIQYFLWETLKEKAKKDFGKFSkkyPSiTSAICGGLAGGIAGFLTTPVDVIKSR--------QIIYgK 212
                        250       260       270
                 ....*....|....*....|....*....|
gi 237649019 562 GVIDCFRKIlREEGPKALWKGAgarVFRSS 591
Cdd:PTZ00168 213 SYIETVTEI-AEEGYLTFYKGC---CFRSS 238
EF-hand_7 pfam13499
EF-hand domain pair;
29-81 1.09e-03

EF-hand domain pair;


Pssm-ID: 257819 [Multi-domain]  Cd Length: 60  Bit Score: 37.75  E-value: 1.09e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 237649019   29 KNGEFFMSPNDFVtRYLNIFGESQPN---PKTVELLSGVVDQTKDGLISFQEFVAF 81
Cdd:pfam13499   5 KDGDGYIDVEELR-KLLKALGLKLTDeevEELLEYDFNEFDKDGDGRISFEEFLEA 59
FRQ1 COG5126
Ca2+-binding protein (EF-Hand superfamily) [Signal transduction mechanisms / Cytoskeleton / ...
8-115 1.27e-03

Ca2+-binding protein (EF-Hand superfamily) [Signal transduction mechanisms / Cytoskeleton / Cell division and chromosome partitioning / General function prediction only]


Pssm-ID: 227455 [Multi-domain]  Cd Length: 160  Bit Score: 38.83  E-value: 1.27e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237649019   8 LTKRaDPAELRTIFLKYAsieKNGEFFMSPNDFVTrYLNIFGESQPNPKTVELLSgvVDQTKDGLISFQEFVAFESV-LC 86
Cdd:COG5126   14 LTEE-QIQELKEAFQLFD---RDSDGLIDRNELGK-ILRSLGFNPSEAEINKLFE--EIDAGNETVDFPEFLTVMSVkLK 86
                         90       100       110
                 ....*....|....*....|....*....|.
gi 237649019  87 APDAL--FMVAFQLFDKAGKGEVTFEDVKQV 115
Cdd:COG5126   87 RGDKEeeLREAFKLFDKDHDGYISIGELRRV 117
 
Name Accession Description Interval E-value
Mito_carr pfam00153
Mitochondrial carrier protein;
517-608 1.08e-31

Mitochondrial carrier protein;


Pssm-ID: 249634  Cd Length: 96  Bit Score: 118.89  E-value: 1.08e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237649019  517 GQVSPGSLLLAGAIAGMPAASLVTPADVIKTRLQVAARAGQTTYSGVIDCFRKILREEGPKALWKGAGARVFRSSPQFGV 596
Cdd:pfam00153   1 SPLSFLASLLAGGIAGAIAATVTYPLDVVKTRLQSSAAGGSRKYKGILDCFKKIYKEEGIRGLYKGLLPNLLRVAPAAAI 80
                          90
                  ....*....|..
gi 237649019  597 TLLTYELLQRWF 608
Cdd:pfam00153  81 YFGTYETLKKLL 92
Mito_carr pfam00153
Mitochondrial carrier protein;
332-424 4.87e-27

Mitochondrial carrier protein;


Pssm-ID: 249634  Cd Length: 96  Bit Score: 106.18  E-value: 4.87e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237649019  332 RFGLGSVAGAVGATAVYPIDLVKTRMQNQRSTGSfvgeLMYKNSFDCFKKVLRYEGFFGLYRGLLPQLLGVAPEKAIKLT 411
Cdd:pfam00153   8 SLLAGGIAGAIAATVTYPLDVVKTRLQSSAAGGS----RKYKGILDCFKKIYKEEGIRGLYKGLLPNLLRVAPAAAIYFG 83
                          90
                  ....*....|...
gi 237649019  412 VNDFVRDKFMHKD 424
Cdd:pfam00153  84 TYETLKKLLLKKL 96
Mito_carr pfam00153
Mitochondrial carrier protein;
425-512 1.78e-17

Mitochondrial carrier protein;


Pssm-ID: 249634  Cd Length: 96  Bit Score: 78.83  E-value: 1.78e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237649019  425 GSVPLAAEILAGGCAGGSQVIFTNPLEIVKIRLQVAGEIT----TGPRVSALSVVRDLGFFGIYKGAKACFLRDIPFSAI 500
Cdd:pfam00153   1 SPLSFLASLLAGGIAGAIAATVTYPLDVVKTRLQSSAAGGsrkyKGILDCFKKIYKEEGIRGLYKGLLPNLLRVAPAAAI 80
                          90
                  ....*....|..
gi 237649019  501 YFPCYAHVKASF 512
Cdd:pfam00153  81 YFGTYETLKKLL 92
S-100 cd00213
S-100: S-100 domain, which represents the largest family within the superfamily of proteins ...
19-81 3.52e-04

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: 39.40  E-value: 3.52e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 237649019  19 TIFLKYASIEKNGEFfMSPNDF---VTRYLNIFGESQPNPKTVELLSGVVDQTKDGLISFQEFVAF 81
Cdd:cd00213   12 DVFHKYSGKEGDKDT-LSKKELkelLETELPNFLKNQKDPEAVDKIMKDLDVNKDGKVDFQEFLVL 76
EFh cd00051
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal ...
16-81 2.95e-03

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: 36.37  E-value: 2.95e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 237649019  16 ELRTIFLKYasiEKNGEFFMSPNDFVtRYLNIFGESQPNPKTVELLSgVVDQTKDGLISFQEFVAF 81
Cdd:cd00051    1 ELREAFRLF---DKDGDGTISADELK-AALKSLGEGLSEEEIDEMIR-EVDKDGDGKIDFEEFLEL 61
S-100A10_like cd05031
S-100A10_like: S-100A10 domain found in proteins similar to S100A10. S100A10 is a member of ...
17-94 3.52e-03

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: 36.25  E-value: 3.52e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237649019  17 LRTIFLKYASIEKNGEFfMSPND---FVTRYLNIFGESQPNPKTVELLSGVVDQTKDGLISFQEFVAF-ESVLCAPDALF 92
Cdd:cd05031   10 LILTFHRYAGKDGDKNT-LSRKElkkLMEKELSEFLKNQKDPMAVDKIMKDLDQNRDGKVNFEEFVSLvAGLSIACEEYY 88

                 ..
gi 237649019  93 MV 94
Cdd:cd05031   89 VK 90
PTZ00168 PTZ00168
mitochondrial carrier protein; Provisional
328-591 6.85e-13

mitochondrial carrier protein; Provisional


Pssm-ID: 185494 [Multi-domain]  Cd Length: 259  Bit Score: 68.03  E-value: 6.85e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237649019 328 ESAYRFGLGSVAGAVGATAVYPIDLVKTRMQNQRSTgsfvgelmyknSFDCFKKvlryegffgLYRGLLPQLLGVAPEKA 407
Cdd:PTZ00168   2 EHFHNLVTGALSGVIVDAVLYPIDSIKTNIQAKKSF-----------SFSDIKK---------LYSGILPTLVGTVPASA 61
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237649019 408 IKLTVNDFVRDKFMHKDGSVPLAA-EILAGGCAGGSQVIFTNPLEIVKIRLQVAGEITTGPRVSALSVVRDLGFFgIYKG 486
Cdd:PTZ00168  62 FFYCFYELSKKLLTEYRENISKTNlYLISTSIAEITACIVRLPFEIVKQNMQVSGNISVLKTIYEITQREGLPSF-LGKS 140
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237649019 487 AKACFLRDIPFSAIYFPCYAHVKASFANEDGQVS---PG-SLLLAGAIAGMPAASLVTPADVIKTRlqvaaragQTTY-S 561
Cdd:PTZ00168 141 YFVMIVREIPFDCIQYFLWETLKEKAKKDFGKFSkkyPSiTSAICGGLAGGIAGFLTTPVDVIKSR--------QIIYgK 212
                        250       260       270
                 ....*....|....*....|....*....|
gi 237649019 562 GVIDCFRKIlREEGPKALWKGAgarVFRSS 591
Cdd:PTZ00168 213 SYIETVTEI-AEEGYLTFYKGC---CFRSS 238
PTZ00169 PTZ00169
ADP/ATP transporter on adenylate translocase; Provisional
333-589 8.13e-25

ADP/ATP transporter on adenylate translocase; Provisional


Pssm-ID: 240302 [Multi-domain]  Cd Length: 300  Bit Score: 104.85  E-value: 8.13e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237649019 333 FGLGSVAGAVGATAVYPIDLVKTRMQNQRSTGSFVGELM--YKNSFDCFKKVLRYEGFFGLYRGLLPQLLGVAPEKAIKL 410
Cdd:PTZ00169  11 FLMGGISAAISKTAVAPIERVKMLIQTQDSIPEIKSGKVprYSGIVNCFRRVSKEQGVLSLWRGNTANVIRYFPTQAFNF 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237649019 411 TVNDFVRDKF----MHKDGSVPLAAEILAGGCAGGSQVIFTNPLEIVKIRLqvAGEIT-------TGPRVSALSVVRDLG 479
Cdd:PTZ00169  91 AFKDYFKNMFpkynQKTDFWKFFGVNILSGGLAGASSLLIVYPLDFARTRL--ASDIGkggdrefTGLFDCLMKISKQTG 168
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237649019 480 FFGIYKGAKACFLRDIPFSAIYFPCYAHVKASFANEDGQVSpgsLLLAGAIAG--MPAASLVT-PADVIKTRLQVAA--- 553
Cdd:PTZ00169 169 FLSLYQGFGVSVQGIIVYRGAYFGLYDSAKALLFGNDKNTN---ILYKWAVAQtvTILAGLISyPFDTVRRRMMMMSgrk 245
                        250       260       270
                 ....*....|....*....|....*....|....*.
gi 237649019 554 RAGQTTYSGVIDCFRKILREEGPKALWKGAGARVFR 589
Cdd:PTZ00169 246 AKSEIQYTGTLDCWKKILKNEGLGGFFKGAWANVLR 281
PTZ00169 PTZ00169
ADP/ATP transporter on adenylate translocase; Provisional
430-587 1.84e-07

ADP/ATP transporter on adenylate translocase; Provisional


Pssm-ID: 240302 [Multi-domain]  Cd Length: 300  Bit Score: 52.08  E-value: 1.84e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237649019 430 AAEILAGGCAGGSQVIFTNPLEIVKIRLQVAG---EITTG--PRVSAL-----SVVRDLGFFGIYKGAKACFLRDIPFSA 499
Cdd:PTZ00169   8 ATDFLMGGISAAISKTAVAPIERVKMLIQTQDsipEIKSGkvPRYSGIvncfrRVSKEQGVLSLWRGNTANVIRYFPTQA 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237649019 500 IYFPCYAHVKASFA--NEDGQVSP--GSLLLAGAIAGMPAASLVTPADVIKTRLQV-AARAGQTTYSGVIDCFRKILREE 574
Cdd:PTZ00169  88 FNFAFKDYFKNMFPkyNQKTDFWKffGVNILSGGLAGASSLLIVYPLDFARTRLASdIGKGGDREFTGLFDCLMKISKQT 167
                        170
                 ....*....|...
gi 237649019 575 GPKALWKGAGARV 587
Cdd:PTZ00169 168 GFLSLYQGFGVSV 180
PTZ00169 PTZ00169
ADP/ATP transporter on adenylate translocase; Provisional
526-592 9.83e-05

ADP/ATP transporter on adenylate translocase; Provisional


Pssm-ID: 240302 [Multi-domain]  Cd Length: 300  Bit Score: 43.60  E-value: 9.83e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 237649019 526 LAGAIAGMPAASLVTPADVIKTRLQVA-----ARAGQTT-YSGVIDCFRKILREEGPKALWKGAGARVFRSSP 592
Cdd:PTZ00169  12 LMGGISAAISKTAVAPIERVKMLIQTQdsipeIKSGKVPrYSGIVNCFRRVSKEQGVLSLWRGNTANVIRYFP 84
EF-hand_7 pfam13499
EF-hand domain pair;
29-81 1.09e-03

EF-hand domain pair;


Pssm-ID: 257819 [Multi-domain]  Cd Length: 60  Bit Score: 37.75  E-value: 1.09e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 237649019   29 KNGEFFMSPNDFVtRYLNIFGESQPN---PKTVELLSGVVDQTKDGLISFQEFVAF 81
Cdd:pfam13499   5 KDGDGYIDVEELR-KLLKALGLKLTDeevEELLEYDFNEFDKDGDGRISFEEFLEA 59
FRQ1 COG5126
Ca2+-binding protein (EF-Hand superfamily) [Signal transduction mechanisms / Cytoskeleton / ...
8-115 1.27e-03

Ca2+-binding protein (EF-Hand superfamily) [Signal transduction mechanisms / Cytoskeleton / Cell division and chromosome partitioning / General function prediction only]


Pssm-ID: 227455 [Multi-domain]  Cd Length: 160  Bit Score: 38.83  E-value: 1.27e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237649019   8 LTKRaDPAELRTIFLKYAsieKNGEFFMSPNDFVTrYLNIFGESQPNPKTVELLSgvVDQTKDGLISFQEFVAFESV-LC 86
Cdd:COG5126   14 LTEE-QIQELKEAFQLFD---RDSDGLIDRNELGK-ILRSLGFNPSEAEINKLFE--EIDAGNETVDFPEFLTVMSVkLK 86
                         90       100       110
                 ....*....|....*....|....*....|.
gi 237649019  87 APDAL--FMVAFQLFDKAGKGEVTFEDVKQV 115
Cdd:COG5126   87 RGDKEeeLREAFKLFDKDHDGYISIGELRRV 117
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.13
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Marchler-Bauer A et al. (2015), "CDD: NCBI's conserved domain database.", Nucleic Acids Res.43(D)222-6.
  • Marchler-Bauer A et al. (2011), "CDD: a Conserved Domain Database for the functional annotation of proteins.", Nucleic Acids Res.39(D)225-9.
  • Marchler-Bauer A et al. (2009), "CDD: specific functional annotation with the Conserved Domain Database.", Nucleic Acids Res.37(D)205-10.
  • Marchler-Bauer A, Bryant SH (2004), "CD-Search: protein domain annotations on the fly.", Nucleic Acids Res.32(W)327-331.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH