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Conserved domains on  [gi|9758252|dbj|BAB08751|]
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calcium-binding transporter-like protein [Arabidopsis thaliana]

Protein Classification

calcium-binding mitochondrial carrier protein( domain architecture ID 12839457)

calcium-binding mitochondrial carrier protein similar to Homo sapiens SCaMC (short calcium-binding mitochondrial carriers), which may function in nucleotide transport in mitochondria, such as ATP-Mg/Pi exchange or related transport systems, in a calcium-regulated mode

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PTZ00169 super family cl36523
ADP/ATP transporter on adenylate translocase; Provisional
 212-485 5.40e-27

ADP/ATP transporter on adenylate translocase; Provisional


The actual alignment was detected with superfamily member PTZ00169:

Pssm-ID: 240302 [Multi-domain]  Cd Length: 300  Bit Score: 110.24  E-value: 5.40e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9758252   212 FIAGGIAGAASRTATAPLDRLKVLLQIQKTDARIREA-----------IKLIWKQGGVRGFFRGNGLNIVKVAPESAIKF 280
Cdd:PTZ00169  11 FLMGGISAAISKTAVAPIERVKMLIQTQDSIPEIKSGkvprysgivncFRRVSKEQGVLSLWRGNTANVIRYFPTQAFNF 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9758252   281 YAYELFKNAIGENmgEDKADIGT--TVRLFAGGMAGAVAQASIYPLDLVKTRLqtyTSQAGVAVPR-----LGTLTKdIL 353
Cdd:PTZ00169  91 AFKDYFKNMFPKY--NQKTDFWKffGVNILSGGLAGASSLLIVYPLDFARTRL---ASDIGKGGDReftglFDCLMK-IS 164

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9758252   354 VHEGPRAFYKGLFPSLLGIIPYAGIDLAAYETLKDL-----SRTYILQDAEPGPLVQLGCGTISgalgatcvYPLQVVRT 428
Cdd:PTZ00169 165 KQTGFLSLYQGFGVSVQGIIVYRGAYFGLYDSAKALlfgndKNTNILYKWAVAQTVTILAGLIS--------YPFDTVRR 236

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 9758252   429 RM--------QAERARTSMSGVFRRTISEEGYRALYKGLLPNLLKVVPAAsITYMVYEAMKKSLE 485
Cdd:PTZ00169 237 RMmmmsgrkaKSEIQYTGTLDCWKKILKNEGLGGFFKGAWANVLRGAGGA-LVLVFYDELQKLLK 300
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
35-168 2.13e-14

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


:

Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 70.21  E-value: 2.13e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9758252   35 EERDLRIRSLFSFFDSENVGYLDCAQIEKGLCALQipsgykyaKELFRVCDANRDGRVDYHEFRRYMDDKELELYR---- 110
Cdd:COG5126   1 DLQRRKLDRRFDLLDADGDGVLERDDFEALFRRLW--------ATLFSEADTDGDGRISREEFVAGMESLFEATVEpfar 72

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 9758252  111 -IFQAIDVEHNGCISPEGLWDSLvkAGIEIKDEELARFVEHVDKDNDGIIMFEEWRDFL 168
Cdd:COG5126  73 aAFDLLDTDGDGKISADEFRRLL--TALGVSEEEADELFARLDTDGDGKISFEEFVAAV 129
 
Name Accession Description Interval E-value
PTZ00169 PTZ00169
ADP/ATP transporter on adenylate translocase; Provisional
 212-485 5.40e-27

ADP/ATP transporter on adenylate translocase; Provisional


Pssm-ID: 240302 [Multi-domain]  Cd Length: 300  Bit Score: 110.24  E-value: 5.40e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9758252   212 FIAGGIAGAASRTATAPLDRLKVLLQIQKTDARIREA-----------IKLIWKQGGVRGFFRGNGLNIVKVAPESAIKF 280
Cdd:PTZ00169  11 FLMGGISAAISKTAVAPIERVKMLIQTQDSIPEIKSGkvprysgivncFRRVSKEQGVLSLWRGNTANVIRYFPTQAFNF 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9758252   281 YAYELFKNAIGENmgEDKADIGT--TVRLFAGGMAGAVAQASIYPLDLVKTRLqtyTSQAGVAVPR-----LGTLTKdIL 353
Cdd:PTZ00169  91 AFKDYFKNMFPKY--NQKTDFWKffGVNILSGGLAGASSLLIVYPLDFARTRL---ASDIGKGGDReftglFDCLMK-IS 164

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9758252   354 VHEGPRAFYKGLFPSLLGIIPYAGIDLAAYETLKDL-----SRTYILQDAEPGPLVQLGCGTISgalgatcvYPLQVVRT 428
Cdd:PTZ00169 165 KQTGFLSLYQGFGVSVQGIIVYRGAYFGLYDSAKALlfgndKNTNILYKWAVAQTVTILAGLIS--------YPFDTVRR 236

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 9758252   429 RM--------QAERARTSMSGVFRRTISEEGYRALYKGLLPNLLKVVPAAsITYMVYEAMKKSLE 485
Cdd:PTZ00169 237 RMmmmsgrkaKSEIQYTGTLDCWKKILKNEGLGGFFKGAWANVLRGAGGA-LVLVFYDELQKLLK 300
Mito_carr pfam00153
Mitochondrial carrier protein;
210-293 2.70e-26

Mitochondrial carrier protein;


Pssm-ID: 395101 [Multi-domain]  Cd Length: 96  Bit Score: 102.35  E-value: 2.70e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9758252    210 NYFIAGGIAGAASRTATAPLDRLKVLLQIQKTDAR-----IREAIKLIWKQGGVRGFFRGNGLNIVKVAPESAIKFYAYE 284
Cdd:pfam00153   7 ASLLAGGIAGAIAVTVTYPLDVVKTRLQVQGGSGKskgrgILDCFKKIYKEEGIRGLYKGLLPNLLRVAPAAAIYFGTYE 86


                  ....*....
gi 9758252    285 LFKNAIGEN 293
Cdd:pfam00153  87 TLKRLLLKK 95
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
35-168 2.13e-14

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


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 70.21  E-value: 2.13e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9758252   35 EERDLRIRSLFSFFDSENVGYLDCAQIEKGLCALQipsgykyaKELFRVCDANRDGRVDYHEFRRYMDDKELELYR---- 110
Cdd:COG5126   1 DLQRRKLDRRFDLLDADGDGVLERDDFEALFRRLW--------ATLFSEADTDGDGRISREEFVAGMESLFEATVEpfar 72

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 9758252  111 -IFQAIDVEHNGCISPEGLWDSLvkAGIEIKDEELARFVEHVDKDNDGIIMFEEWRDFL 168
Cdd:COG5126  73 aAFDLLDTDGDGKISADEFRRLL--TALGVSEEEADELFARLDTDGDGKISFEEFVAAV 129
PTZ00183 PTZ00183
centrin; Provisional
 35-163 1.71e-12

centrin; Provisional


Pssm-ID: 185503 [Multi-domain]  Cd Length: 158  Bit Score: 65.10  E-value: 1.71e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9758252    35 EERDLRIRSLFSFFDSENVGYLDCAQIEKGLCALQIPSGYKYAKELFRVCDANRDGRVDYHEFRRYM-------DDKElE 107
Cdd:PTZ00183  13 EDQKKEIREAFDLFDTDGSGTIDPKELKVAMRSLGFEPKKEEIKQMIADVDKDGSGKIDFEEFLDIMtkklgerDPRE-E 91

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 9758252   108 LYRIFQAIDVEHNGCISPEGLWDSLVKAGIEIKDEELARFVEHVDKDNDGIIMFEE 163
Cdd:PTZ00183  92 ILKAFRLFDDDKTGKISLKNLKRVAKELGETITDEELQEMIDEADRNGDGEISEEE 147
EFh_PI-PLC cd15898
EF-hand motif found in eukaryotic phosphoinositide-specific phospholipase C (PI-PLC, EC 3.1.4. ...
 40-169 6.41e-09

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: 54.21  E-value: 6.41e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9758252   40 RIRSLFSFFDSENVGYLDCAQIEKGLCALQIPSGYKYAKELFRVCDANRDGRVDYHEFRRYMddKEL----ELYRIFQAI 115
Cdd:cd15898   1 WLRRQWIKADKDGDGKLSLKEIKKLLKRLNIRVSEKELKKLFKEVDTNGDGTLTFDEFEELY--KSLterpELEPIFKKY 78

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 9758252  116 DVEHNGCISPEGLWDSLVKAGIEIKDEELAR--FVEHVDKDNDGIIMFEEWRDFLL 169
Cdd:cd15898  79 AGTNRDYMTLEEFIRFLREEQGENVSEEECEelIEKYEPERENRQLSFEGFTNFLL 134
EF-hand_7 pfam13499
EF-hand domain pair;
107-163 3.26e-06

EF-hand domain pair;


Pssm-ID: 463900 [Multi-domain]  Cd Length: 67  Bit Score: 44.55  E-value: 3.26e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 9758252    107 ELYRIFQAIDVEHNGCISPEGLWDSLVKA--GIEIKDEELARFVEHVDKDNDGIIMFEE 163
Cdd:pfam13499   3 KLKEAFKLLDSDGDGYLDVEELKKLLRKLeeGEPLSDEEVEELFKEFDLDKDGRISFEE 61
EFh smart00054
EF-hand, calcium binding motif; EF-hands are calcium-binding motifs that occur at least in ...
 78-101 4.26e-04

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: 37.36  E-value: 4.26e-04
                           10        20
                   ....*....|....*....|....
gi 9758252      78 KELFRVCDANRDGRVDYHEFRRYM 101
Cdd:smart00054   3 KEAFRLFDKDGDGKIDFEEFKDLL 26
 
Name Accession Description Interval E-value
PTZ00169 PTZ00169
ADP/ATP transporter on adenylate translocase; Provisional
 212-485 5.40e-27

ADP/ATP transporter on adenylate translocase; Provisional


Pssm-ID: 240302 [Multi-domain]  Cd Length: 300  Bit Score: 110.24  E-value: 5.40e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9758252   212 FIAGGIAGAASRTATAPLDRLKVLLQIQKTDARIREA-----------IKLIWKQGGVRGFFRGNGLNIVKVAPESAIKF 280
Cdd:PTZ00169  11 FLMGGISAAISKTAVAPIERVKMLIQTQDSIPEIKSGkvprysgivncFRRVSKEQGVLSLWRGNTANVIRYFPTQAFNF 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9758252   281 YAYELFKNAIGENmgEDKADIGT--TVRLFAGGMAGAVAQASIYPLDLVKTRLqtyTSQAGVAVPR-----LGTLTKdIL 353
Cdd:PTZ00169  91 AFKDYFKNMFPKY--NQKTDFWKffGVNILSGGLAGASSLLIVYPLDFARTRL---ASDIGKGGDReftglFDCLMK-IS 164

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9758252   354 VHEGPRAFYKGLFPSLLGIIPYAGIDLAAYETLKDL-----SRTYILQDAEPGPLVQLGCGTISgalgatcvYPLQVVRT 428
Cdd:PTZ00169 165 KQTGFLSLYQGFGVSVQGIIVYRGAYFGLYDSAKALlfgndKNTNILYKWAVAQTVTILAGLIS--------YPFDTVRR 236

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 9758252   429 RM--------QAERARTSMSGVFRRTISEEGYRALYKGLLPNLLKVVPAAsITYMVYEAMKKSLE 485
Cdd:PTZ00169 237 RMmmmsgrkaKSEIQYTGTLDCWKKILKNEGLGGFFKGAWANVLRGAGGA-LVLVFYDELQKLLK 300
Mito_carr pfam00153
Mitochondrial carrier protein;
210-293 2.70e-26

Mitochondrial carrier protein;


Pssm-ID: 395101 [Multi-domain]  Cd Length: 96  Bit Score: 102.35  E-value: 2.70e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9758252    210 NYFIAGGIAGAASRTATAPLDRLKVLLQIQKTDAR-----IREAIKLIWKQGGVRGFFRGNGLNIVKVAPESAIKFYAYE 284
Cdd:pfam00153   7 ASLLAGGIAGAIAVTVTYPLDVVKTRLQVQGGSGKskgrgILDCFKKIYKEEGIRGLYKGLLPNLLRVAPAAAIYFGTYE 86


                  ....*....
gi 9758252    285 LFKNAIGEN 293
Cdd:pfam00153  87 TLKRLLLKK 95
Mito_carr pfam00153
Mitochondrial carrier protein;
399-484 1.39e-25

Mitochondrial carrier protein;


Pssm-ID: 395101 [Multi-domain]  Cd Length: 96  Bit Score: 100.04  E-value: 1.39e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9758252    399 EPGPLVQLGCGTISGALGATCVYPLQVVRTRMQAERART-----SMSGVFRRTISEEGYRALYKGLLPNLLKVVPAASIT 473
Cdd:pfam00153   2 ELSFLASLLAGGIAGAIAVTVTYPLDVVKTRLQVQGGSGkskgrGILDCFKKIYKEEGIRGLYKGLLPNLLRVAPAAAIY 81

                          90
                  ....*....|.
gi 9758252    474 YMVYEAMKKSL 484
Cdd:pfam00153  82 FGTYETLKRLL 92
Mito_carr pfam00153
Mitochondrial carrier protein;
300-389 7.84e-25

Mitochondrial carrier protein;


Pssm-ID: 395101 [Multi-domain]  Cd Length: 96  Bit Score: 98.11  E-value: 7.84e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9758252    300 DIGTTVRLFAGGMAGAVAQASIYPLDLVKTRLQTYTSQAGVAVPRLGTLTKDILVHEGPRAFYKGLFPSLLGIIPYAGID 379
Cdd:pfam00153   2 ELSFLASLLAGGIAGAIAVTVTYPLDVVKTRLQVQGGSGKSKGRGILDCFKKIYKEEGIRGLYKGLLPNLLRVAPAAAIY 81

                          90
                  ....*....|
gi 9758252    380 LAAYETLKDL 389
Cdd:pfam00153  82 FGTYETLKRL 91
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
35-168 2.13e-14

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


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 70.21  E-value: 2.13e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9758252   35 EERDLRIRSLFSFFDSENVGYLDCAQIEKGLCALQipsgykyaKELFRVCDANRDGRVDYHEFRRYMDDKELELYR---- 110
Cdd:COG5126   1 DLQRRKLDRRFDLLDADGDGVLERDDFEALFRRLW--------ATLFSEADTDGDGRISREEFVAGMESLFEATVEpfar 72

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 9758252  111 -IFQAIDVEHNGCISPEGLWDSLvkAGIEIKDEELARFVEHVDKDNDGIIMFEEWRDFL 168
Cdd:COG5126  73 aAFDLLDTDGDGKISADEFRRLL--TALGVSEEEADELFARLDTDGDGKISFEEFVAAV 129
PTZ00183 PTZ00183
centrin; Provisional
 35-163 1.71e-12

centrin; Provisional


Pssm-ID: 185503 [Multi-domain]  Cd Length: 158  Bit Score: 65.10  E-value: 1.71e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9758252    35 EERDLRIRSLFSFFDSENVGYLDCAQIEKGLCALQIPSGYKYAKELFRVCDANRDGRVDYHEFRRYM-------DDKElE 107
Cdd:PTZ00183  13 EDQKKEIREAFDLFDTDGSGTIDPKELKVAMRSLGFEPKKEEIKQMIADVDKDGSGKIDFEEFLDIMtkklgerDPRE-E 91

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 9758252   108 LYRIFQAIDVEHNGCISPEGLWDSLVKAGIEIKDEELARFVEHVDKDNDGIIMFEE 163
Cdd:PTZ00183  92 ILKAFRLFDDDKTGKISLKNLKRVAKELGETITDEELQEMIDEADRNGDGEISEEE 147
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
28-132 1.02e-09

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


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 56.72  E-value: 1.02e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9758252   28 LALRETREERDLRIRSLFSFFDSENVGYLDCAQIEKGLCALQIPSGYKYAKELFRVCDANRDGRVDYHEFRRYMDDKEL- 106
Cdd:COG5126  22 LERDDFEALFRRLWATLFSEADTDGDGRISREEFVAGMESLFEATVEPFARAAFDLLDTDGDGKISADEFRRLLTALGVs 101

                        90       100
                ....*....|....*....|....*...
gi 9758252  107 --ELYRIFQAIDVEHNGCISPEGLWDSL 132
Cdd:COG5126 102 eeEADELFARLDTDGDGKISFEEFVAAV 129
PTZ00168 PTZ00168
mitochondrial carrier protein; Provisional
 307-487 1.80e-09

mitochondrial carrier protein; Provisional


Pssm-ID: 185494 [Multi-domain]  Cd Length: 259  Bit Score: 58.40  E-value: 1.80e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9758252   307 LFAGGMAGAVAQASIYPLDLVKTRLQtytsqagvavprlgtlTKDILVHEGPRAFYKGLFPSLLGIIPYAGIDLAAYEtl 386
Cdd:PTZ00168   7 LVTGALSGVIVDAVLYPIDSIKTNIQ----------------AKKSFSFSDIKKLYSGILPTLVGTVPASAFFYCFYE-- 68

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9758252   387 kdLSRTYILQDAEPGPLVQLGCGTISGALGATCV--YPLQVVRTRMQAERARTSMSGVFRRTISEEGYRALYKGLLPNLL 464
Cdd:PTZ00168  69 --LSKKLLTEYRENISKTNLYLISTSIAEITACIvrLPFEIVKQNMQVSGNISVLKTIYEITQREGLPSFLGKSYFVMIV 146

                        170       180
                 ....*....|....*....|...
gi 9758252   465 KVVPAASITYMVYEAMKKSLELD 487
Cdd:PTZ00168 147 REIPFDCIQYFLWETLKEKAKKD 169
PTZ00168 PTZ00168
mitochondrial carrier protein; Provisional
 212-458 2.77e-09

mitochondrial carrier protein; Provisional


Pssm-ID: 185494 [Multi-domain]  Cd Length: 259  Bit Score: 58.01  E-value: 2.77e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9758252   212 FIAGGIAGAASRTATAPLDRLKVLLQIQKTdarireaikliWKQGGVRGFFRGNGLNIVKVAPESAIKFYAYELFKNAIG 291
Cdd:PTZ00168   7 LVTGALSGVIVDAVLYPIDSIKTNIQAKKS-----------FSFSDIKKLYSGILPTLVGTVPASAFFYCFYELSKKLLT 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9758252   292 ENmgedKADIG-TTVRLFAGGMAGAVAQASIYPLDLVKTRLQTYTSQAGVAVPRLGTLTKDILVHEGprafyKGLFPSLL 370
Cdd:PTZ00168  76 EY----RENISkTNLYLISTSIAEITACIVRLPFEIVKQNMQVSGNISVLKTIYEITQREGLPSFLG-----KSYFVMIV 146

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9758252   371 GIIPYAGIDLAAYETLKDLSRTYILQDAEPGP-LVQLGCGTISGALGATCVYPLQVVRTRmQAERARTSMSGVfrRTISE 449
Cdd:PTZ00168 147 REIPFDCIQYFLWETLKEKAKKDFGKFSKKYPsITSAICGGLAGGIAGFLTTPVDVIKSR-QIIYGKSYIETV--TEIAE 223


                 ....*....
gi 9758252   450 EGYRALYKG 458
Cdd:PTZ00168 224 EGYLTFYKG 232
EFh_PI-PLC cd15898
EF-hand motif found in eukaryotic phosphoinositide-specific phospholipase C (PI-PLC, EC 3.1.4. ...
 40-169 6.41e-09

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: 54.21  E-value: 6.41e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9758252   40 RIRSLFSFFDSENVGYLDCAQIEKGLCALQIPSGYKYAKELFRVCDANRDGRVDYHEFRRYMddKEL----ELYRIFQAI 115
Cdd:cd15898   1 WLRRQWIKADKDGDGKLSLKEIKKLLKRLNIRVSEKELKKLFKEVDTNGDGTLTFDEFEELY--KSLterpELEPIFKKY 78

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 9758252  116 DVEHNGCISPEGLWDSLVKAGIEIKDEELAR--FVEHVDKDNDGIIMFEEWRDFLL 169
Cdd:cd15898  79 AGTNRDYMTLEEFIRFLREEQGENVSEEECEelIEKYEPERENRQLSFEGFTNFLL 134
EFh_HEF cd15902
EF-hand, calcium binding motif, found in the hexa-EF hand proteins family; The hexa-EF hand ...
 20-168 1.28e-08

EF-hand, calcium binding motif, found in the hexa-EF hand proteins family; The hexa-EF hand proteins family, also named the calbindin sub-family, contains a group of six EF-hand Ca2+-binding proteins, including calretinin (CR, also termed 29 kDa calbindin), calbindin D28K (CB, also termed vitamin D-dependent calcium-binding protein, avian-type), and secretagogin (SCGN). CR is a cytosolic hexa-EF-hand calcium-binding protein predominantly expressed in a variety of normal and tumorigenic t-specific neurons of the central and peripheral nervous system. It is a multifunctional protein implicated in many biological processes, including cell proliferation, differentiation, and cell death. CB is highly expressed in brain tissue. It is a strong calcium-binding and buffering protein responsible for preventing a neuronal death as well as maintaining and controlling calcium homeostasis. SCGN is a six EF-hand calcium-binding protein expressed in neuroendocrine, pancreatic endocrine and retinal cells. It plays a crucial role in cell apoptosis, receptor signaling and differentiation. It is also involved in vesicle secretion through binding to various proteins, including interacts with SNAP25, SNAP23, DOC2alpha, ARFGAP2, rootletin, KIF5B, beta-tubulin, DDAH-2, ATP-synthase and myeloid leukemia factor 2. SCGN functions as a Ca2+ sensor/coincidence detector modulating vesicular exocytosis of neurotransmitters, neuropeptides or hormones. Although the family members share a significant amount of secondary sequence homology, they display altered structural and biochemical characteristics, and operate in distinct fashions. CB contains six EF-hand motifs in a single globular domain, where EF-hands 1, 3, 4, 5 bind four calcium ions. CR contains six EF-hand motifs within two independent domains, CR I-II and CR III-VI. They harbor two and four EF-hand motifs, respectively. The first 5 EF-hand motifs are capable of binding calcium ions, while the EF-hand 6 is inactive. SCGN consists of the three globular domains each of which contains a pair of EF-hand motifs. Human SCGN simultaneously binds four calcium ions through its EF-hands 3, 4, 5 and 6 in one high affinity and three low affinity calcium-binding sites. In contrast, SCGNs in other lower eukaryotes, such as D. rerio, X. laevis, M. domestica, G. gallus, O. anatinus, are fully competent in terms of six calcium-binding.


Pssm-ID: 320075 [Multi-domain]  Cd Length: 254  Bit Score: 55.82  E-value: 1.28e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9758252   20 PVSIDHVLLALRETREERDLRIRSLFSFFDSENVGYLDCAQIE---KGLCALQIPSGY-----KYAKELFRVCDANRDGR 91
Cdd:cd15902  71 PTEENFLLLFRREQPLISSVEFMKIWRKYDTDGSGFIEAKELKgflKDLLLKNKKHVSppkldEYTKLILKEFDANKDGK 150

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9758252   92 VDYHEFRRYMDDKELELY----------------RIFQAIDVEHNGCI-SPE--GLWDSL---VKAGIEIKDEELARFV- 148
Cdd:cd15902 151 LELDEMAKLLPVQENFLLkfqilgamdltkedfeKVFEHYDKDNNGVIeGNEldALLKDLlekNKADIDKPDLENFRDAi 230

                       170       180
                ....*....|....*....|.
gi 9758252  149 -EHVDKDNDGIIMFEEWRDFL 168
Cdd:cd15902 231 lRACDKNKDGKIQKTELALFL 251
EFh cd00051
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal ...
 76-168 1.31e-08

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: 51.39  E-value: 1.31e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9758252   76 YAKELFRVCDANRDGRVDYHEFRRYMDdkelelyrifqaidvehngcispeglwdslvKAGIEIKDEELARFVEHVDKDN 155
Cdd:cd00051   1 ELREAFRLFDKDGDGTISADELKAALK-------------------------------SLGEGLSEEEIDEMIREVDKDG 49

                        90
                ....*....|...
gi 9758252  156 DGIIMFEEWRDFL 168
Cdd:cd00051  50 DGKIDFEEFLELM 62
PTZ00184 PTZ00184
calmodulin; Provisional
 32-164 1.12e-07

calmodulin; Provisional


Pssm-ID: 185504 [Multi-domain]  Cd Length: 149  Bit Score: 50.92  E-value: 1.12e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9758252    32 ETREERDLRIRSLFSFFDSENVGYLDCAQIEKGLCAL-QIPSGYKYaKELFRVCDANRDGRVDYHEFRRYM------DDK 104
Cdd:PTZ00184   4 QLTEEQIAEFKEAFSLFDKDGDGTITTKELGTVMRSLgQNPTEAEL-QDMINEVDADGNGTIDFPEFLTLMarkmkdTDS 82

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 9758252   105 ELELYRIFQAIDVEHNGCISPEGLWDSLVKAGIEIKDEELARFVEHVDKDNDGIIMFEEW 164
Cdd:PTZ00184  83 EEEIKEAFKVFDRDGNGFISAAELRHVMTNLGEKLTDEEVDEMIREADVDGDGQINYEEF 142
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
19-103 1.37e-06

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


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 47.48  E-value: 1.37e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9758252   19 GPVSIDhVLLALRETREERDLR--IRSLFSFFDSENVGYLDCAQIEKGLCALQIPSGYkyAKELFRVCDANRDGRVDYHE 96
Cdd:COG5126  48 GRISRE-EFVAGMESLFEATVEpfARAAFDLLDTDGDGKISADEFRRLLTALGVSEEE--ADELFARLDTDGDGKISFEE 124


                ....*..
gi 9758252   97 FRRYMDD 103
Cdd:COG5126 125 FVAAVRD 131
PTZ00183 PTZ00183
centrin; Provisional
 102-174 2.75e-06

centrin; Provisional


Pssm-ID: 185503 [Multi-domain]  Cd Length: 158  Bit Score: 47.38  E-value: 2.75e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 9758252   102 DDKELELYRIFQAIDVEHNGCISPEGLWDSLVKAGIEIKDEELARFVEHVDKDNDGIIMFEEWRDFLLLYPHE 174
Cdd:PTZ00183  13 EDQKKEIREAFDLFDTDGSGTIDPKELKVAMRSLGFEPKKEEIKQMIADVDKDGSGKIDFEEFLDIMTKKLGE 85
EF-hand_7 pfam13499
EF-hand domain pair;
107-163 3.26e-06

EF-hand domain pair;


Pssm-ID: 463900 [Multi-domain]  Cd Length: 67  Bit Score: 44.55  E-value: 3.26e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 9758252    107 ELYRIFQAIDVEHNGCISPEGLWDSLVKA--GIEIKDEELARFVEHVDKDNDGIIMFEE 163
Cdd:pfam13499   3 KLKEAFKLLDSDGDGYLDVEELKKLLRKLeeGEPLSDEEVEELFKEFDLDKDGRISFEE 61
EFh_PEF_Group_II_CAPN_like cd16182
Penta-EF hand, calcium binding motifs, found in PEF calpain family; The PEF calpain family ...
 85-164 7.58e-06

Penta-EF hand, calcium binding motifs, found in PEF calpain family; The PEF calpain family belongs to the second group of penta-EF hand (PEF) proteins. It includes classical (also called conventional or typical) calpain (referring to a calcium-dependent papain-like enzymes, EC 3.4.22.17) large catalytic subunits (CAPN1, 2, 3, 8, 9, 11, 12, 13, 14) and two calpain small subunits (CAPNS1 and CAPNS2), which are largely confined to animals (metazoans). These PEF-containing are nonlysosomal intracellular calcium-activated intracellular cysteine proteases that play important roles in the degradation or functional modulation in a variety of substrates in response to calcium signalling. The classical mu- and m-calpains are heterodimers consisting of homologous but a distinct (large) L-subunit/chain (CAPN1 or CAPN2) and a common (small) S-subunit/chain (CAPNS1 or CAPNS2). These L-subunits (CAPN1 and CAPN2) and S-subunit CAPNS1 are ubiquitously found in all tissues. Other calpains likely consist of an isolated L-subunit/chain alone. Many of them, such as CAPNS2, CAPN3 (in skeletal muscle, or lens), CAPN8 (in stomach), CAPN9 (in digestive tracts), CAPN11 (in testis), CAPN12 (in follicles), are tissue-specific and have specific functions in distinct organs. The L-subunits of similar structure (called CALPA and B) also have been found in Drosophila melanogaster. The S-subunit seems to have a chaperone-like function for proper folding of the L-subunit. The catalytic L-subunits contain a short N-terminal anchor helix, followed by a calpain cysteine protease (CysPc) domain, a C2-domain-like (C2L) domain, and a C-terminal Ca2+-binding penta-EF-hand (PEF) domain. The S-subunits only have the PEF domain following an N-terminal Gly-rich hydrophobic domain. The calpains undergo a rearrangement of the protein backbone upon Ca2+-binding.


Pssm-ID: 320057 [Multi-domain]  Cd Length: 167  Bit Score: 46.06  E-value: 7.58e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9758252   85 DANRDGRVDYHEFRRYMddKELELYR-IFQAIDVEHNGCISPEGLWDSLVKAGIE------------------------- 138
Cdd:cd16182  52 DTNGSGRLDLEEFKTLW--SDLKKWQaIFKKFDTDRSGTLSSYELRKALESAGFHlsnkvlqalvlryadstgritfedf 129

                        90       100       110
                ....*....|....*....|....*....|..
gi 9758252  139 ----IKDEELARFVEHVDKDNDGIIMF--EEW 164
Cdd:cd16182 130 vsclVRLKTAFETFSALDKKNEGVIPLtlEEW 161
EFh cd00051
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal ...
 40-101 1.29e-05

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: 1.29e-05
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 9758252   40 RIRSLFSFFDSENVGYLDCAQIEKGLCALQIPSGYKYAKELFRVCDANRDGRVDYHEFRRYM 101
Cdd:cd00051   1 ELREAFRLFDKDGDGTISADELKAALKSLGEGLSEEEIDEMIREVDKDGDGKIDFEEFLELM 62
PTZ00168 PTZ00168
mitochondrial carrier protein; Provisional
 204-364 5.76e-05

mitochondrial carrier protein; Provisional


Pssm-ID: 185494 [Multi-domain]  Cd Length: 259  Bit Score: 44.92  E-value: 5.76e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9758252   204 KHIKRSN-YFIAGGIAGAASRTATAPLDRLKVLLQIQKTDARIReAIKLIWKQGGVRGFFrGNG--LNIVKVAPESAIKF 280
Cdd:PTZ00168  79 ENISKTNlYLISTSIAEITACIVRLPFEIVKQNMQVSGNISVLK-TIYEITQREGLPSFL-GKSyfVMIVREIPFDCIQY 156

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9758252   281 YAYELFKNAIGENMGEDKADIGTTVRLFAGGMAGAVAQASIYPLDLVKTRLQTYTSQagvavpRLGTLTKdiLVHEGPRA 360
Cdd:PTZ00168 157 FLWETLKEKAKKDFGKFSKKYPSITSAICGGLAGGIAGFLTTPVDVIKSRQIIYGKS------YIETVTE--IAEEGYLT 228


                 ....
gi 9758252   361 FYKG 364
Cdd:PTZ00168 229 FYKG 232
EFh_HEF_CBN cd16179
EF-hand, calcium binding motif, found in Drosophila melanogaster calbindin-32 (CBN) and ...
 48-171 6.55e-05

EF-hand, calcium binding motif, found in Drosophila melanogaster calbindin-32 (CBN) and similar proteins; CBN, the product of the cbn gene, is a Drosophila homolog to vertebrate neuronal six EF-hand calcium binding proteins. It is expressed through most of ontogenesis with a selective distribution in the nervous system and in a few small adult thoracic muscles. Its precise biological role remains unclear. CBN contains six EF-hand motifs, but some of them may not bind calcium ions due to the lack of key residues.


Pssm-ID: 320079 [Multi-domain]  Cd Length: 261  Bit Score: 44.71  E-value: 6.55e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9758252   48 FDSENVGYLDCAQIEKGLCAL-------QIPSGYK---YAKELFRVCDANRDGRVDYHEFRRYMDDKE------------ 105
Cdd:cd16179 104 YDKDNSGYIEADELKNFLKHLlkeakrdNDVSEDKlieYTDTILQLFDRNKDGKLQLSEMARLLPVKEnflcrpifkgag 183

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 9758252  106 ----LELYRIFQAIDVEHNGCISPE---GLWDSLVKAGIEIKDEE-LARFVE----HVDKDNDGIIMFEEWRDFLLLY 171
Cdd:cd16179 184 kltrEDIDRVFALYDRDNNGTIENEeltGFLKDLLELVQEDYDEQdLEEFKEiilrGWDFNNDGKISRKELTMLLLQL 261
EF-hand_7 pfam13499
EF-hand domain pair;
40-101 1.29e-04

EF-hand domain pair;


Pssm-ID: 463900 [Multi-domain]  Cd Length: 67  Bit Score: 39.93  E-value: 1.29e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 9758252     40 RIRSLFSFFDSENVGYLDCAQIEKGL--CALQIPSGYKYAKELFRVCDANRDGRVDYHEFRRYM 101
Cdd:pfam13499   3 KLKEAFKLLDSDGDGYLDVEELKKLLrkLEEGEPLSDEEVEELFKEFDLDKDGRISFEEFLELY 66
EFh smart00054
EF-hand, calcium binding motif; EF-hands are calcium-binding motifs that occur at least in ...
 78-101 4.26e-04

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: 37.36  E-value: 4.26e-04
                           10        20
                   ....*....|....*....|....
gi 9758252      78 KELFRVCDANRDGRVDYHEFRRYM 101
Cdd:smart00054   3 KEAFRLFDKDGDGKIDFEEFKDLL 26
EF-hand_1 pfam00036
EF hand; The EF-hands can be divided into two classes: signalling proteins and buffering ...
 78-101 6.09e-04

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: 36.99  E-value: 6.09e-04
                          10        20
                  ....*....|....*....|....
gi 9758252     78 KELFRVCDANRDGRVDYHEFRRYM 101
Cdd:pfam00036   3 KEIFRLFDKDGDGKIDFEEFKELL 26
EFh_ScPlc1p_like cd16207
EF-hand motif found in Saccharomyces cerevisiae phospholipase C-1 (ScPlc1p) and similar ...
 55-169 6.58e-04

EF-hand motif found in Saccharomyces cerevisiae phospholipase C-1 (ScPlc1p) and similar proteins; This family represents a group of putative phosphoinositide-specific phospholipase C (PI-PLC, EC 3.1.4.11) encoded by PLC1 genes from yeasts, which are homologs of the delta isoforms of mammalian PI-PLC in terms of overall sequence similarity and domain organization. Mammalian PI-PLC is a signaling enzyme that hydrolyzes 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 then phosphorylates other molecules, leading to altered cellular activity. Calcium is required for the catalysis. The prototype of this family is protein Plc1p (also termed 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase 1) encoded by PLC1 genes from Saccharomyces cerevisiae. ScPlc1p contains both highly conserved X- and Y- regions of PLC catalytic core domain, as well as a presumptive EF-hand like calcium binding motif. Experiments show that ScPlc1p displays calcium dependent catalytic properties with high similarity to those of the mammalian PLCs, and plays multiple roles in modulating the membrane/protein interactions in filamentation control. CaPlc1p encoded by CAPLC1 from the closely related yeast Candida albicans, an orthologue of S. cerevisiae Plc1p, is also included in this group. Like SCPlc1p, CaPlc1p has conserved presumptive catalytic domain, shows PLC activity when expressed in E. coli, and is involved in multiple cellular processes. There are two other gene copies of CAPLC1 in C. albicans, CAPLC2 (also named as PIPLC) and CAPLC3. Experiments show CaPlc1p is the only enzyme in C. albicans which functions as PLC. The biological functions of CAPLC2 and CAPLC3 gene products must be clearly different from CaPlc1p, but their exact roles remain unclear. Moreover, CAPLC2 and CAPLC3 gene products are more similar to extracellular bacterial PI-PLC than to the eukaryotic PI-PLC, and they are not included in this subfamily.


Pssm-ID: 320037 [Multi-domain]  Cd Length: 142  Bit Score: 39.92  E-value: 6.58e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9758252   55 YLDCAQIEKgLCA-LQIPSGYKYAKELFRVCDANRDGRVDYHEFRRYMddKEL----ELYRIFQAIDVEHNGCISPEGLW 129
Cdd:cd16207  18 RLDFEDVEK-LCRrLHINCSESYLRELFDKADTDKKGYLNFEEFQEFV--KLLkrrkDIKAIFKQLTKPGSDGLTLEEFL 94

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*
gi 9758252  130 DSLVKA-GIEIKDEEL----ARFVEHVDKDNDGIIMFEEWRDFLL 169
Cdd:cd16207  95 KFLRDVqKEDVDRETWekifEKFARRIDDSDSLTMTLEGFTSFLL 139
EFh_calglandulin_like cd16252
EF-hand, calcium binding motif, found in uncharacterized calglandulin-like proteins; The ...
 32-97 6.75e-04

EF-hand, calcium binding motif, found in uncharacterized calglandulin-like proteins; The family corresponds to a group of uncharacterized calglandulin-like proteins. Although their biological function remain unclear, they show high sequence similarity with human calglandulin-like protein GAGLP, which is an ortholog of calglandulin from the venom glands of Bothrops insularis snake. Both GAGLP and calglandulin are putative Ca2+-binding proteins with four EF-hand motifs. However, members in this family contain only three EF-hand motifs. In this point, they may belong to the parvalbumin-like EF-hand family, which is characterized by the presence of three consecutive EF-hand motifs (helix-loop-helix).


Pssm-ID: 319995 [Multi-domain]  Cd Length: 106  Bit Score: 39.05  E-value: 6.75e-04
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 9758252   32 ETREERDLRIRSLFSFFDSENVGYLDCAQIEKGLCALQI-----PSGYKYAKELFRVCDANRDGRVDYHEF 97
Cdd:cd16252  30 QTSEQQEEAIRKAFQMLDKDKSGFIEWNEIKYILSTVPSsmpvaPLSDEEAEAMIQAADTDGDGRIDFQEF 100
EFh_PEF_ALG-2_like cd16185
EF-hand, calcium binding motif, found in homologs of mammalian apoptosis-linked gene 2 protein ...
 41-164 1.09e-03

EF-hand, calcium binding motif, found in homologs of mammalian apoptosis-linked gene 2 protein (ALG-2); The family includes some homologs of mammalian apoptosis-linked gene 2 protein (ALG-2) mainly found in lower eukaryotes, such as a parasitic protist Leishmarua major and a cellular slime mold Dictyostelium discoideum. These homologs contains five EF-hand motifs. Due to the presence of unfavorable residues at the Ca2+-coordinating positions, their non-canonical EF4 and EF5 hands may not bind Ca2+. Two Dictyostelium PEF proteins are the prototypes of this family. They may bind to cytoskeletal proteins and/or signal-transducing proteins localized to detergent-resistant membranes named lipid rafts, and occur as monomers or weak homo- or heterodimers like ALG-2. They can serve as a mediator for Ca2+ signaling-related Dictyostehum programmed cell death (PCD).


Pssm-ID: 320060 [Multi-domain]  Cd Length: 163  Bit Score: 39.89  E-value: 1.09e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9758252   41 IRSLFSFFDSENVGYLDCAQIEKGLCALQIPSGYKYAKELFRVCDANRDGRVDYHEFR---RYMddkeLELYRIFQAIDV 117
Cdd:cd16185   2 LRQWFRAVDRDRSGSIDVNELQKALAGGGLLFSLATAEKLIRMFDRDGNGTIDFEEFAalhQFL----SNMQNGFEQRDT 77

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*..
gi 9758252  118 EHNGCISPEGLWDSLVKAGIEIKDEELARFVEHVDKDNDGIIMFEEW 164
Cdd:cd16185  78 SRSGRLDANEVHEALAASGFQLDPPAFQALFRKFDPDRGGSLGFDDY 124
EF-hand_8 pfam13833
EF-hand domain pair;
119-171 1.61e-03

EF-hand domain pair;


Pssm-ID: 404678 [Multi-domain]  Cd Length: 54  Bit Score: 36.52  E-value: 1.61e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 9758252    119 HNGCISPEGLWDSLVKAGI-EIKDEELARFVEHVDKDNDGIIMFEEWRDFLLLY 171
Cdd:pfam13833   1 EKGVITREELKRALALLGLkDLSEDEVDILFREFDTDGDGYISFDEFCVLLERR 54
EFh_PI-PLCdelta cd16202
EF-hand motif found in phosphoinositide phospholipase C delta (PI-PLC-delta); PI-PLC-delta ...
 41-156 1.76e-03

EF-hand motif found in phosphoinositide phospholipase C delta (PI-PLC-delta); PI-PLC-delta isozymes represent a class of metazoan PI-PLCs that are some of the most sensitive to calcium among all PLCs. Their activation is modulated by intracellular calcium ion concentration, phospholipids, polyamines, and other proteins, such as RhoAGAP. Like other PI-PLC isozymes, PI-PLC-delta isozymes contain 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 C-terminal C2 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. There are three PI-PLC-delta isozymes (1, 3 and 4). PI-PLC-delta1 is relatively well characterized. It is activated by high calcium levels generated by other PI-PLC family members, and therefore functions as a calcium amplifier within the cell. Different PI-PLC-delta isozymes have different tissue distribution and different subcellular locations. PI-PLC-delta1 is mostly a cytoplasmic protein, PI-PLC-delta3 is located in the membrane, and PI-PLC-delta4 is predominantly detected in the cell nucleus. PI-PLC-delta isozymes is evolutionarily conserved even in non-mammalian species, such as yeast, slime molds and plants.


Pssm-ID: 320032 [Multi-domain]  Cd Length: 140  Bit Score: 38.75  E-value: 1.76e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9758252   41 IRSLFSFFDSENVGYLDCAQIEKGLCALQIPSGYKYAKELFRVCDANRDGRVDYHEF----RRYMDDKELElyRIFQAID 116
Cdd:cd16202   2 LKDQFRKADKNGDGKLSFKECKKLLKKLNVKVDKDYAKKLFQEADTSGEDVLDEEEFvqfyNRLTKRPEIE--ELFKKYS 79

                        90       100       110       120
                ....*....|....*....|....*....|....*....|
gi 9758252  117 vehngcispeglwdslvKAGIEIKDEELARFVEHVDKDND 156
Cdd:cd16202  80 -----------------GDDEALTVEELRRFLQEEQKVKD 102
EFh_CREC_RCN2_like cd16227
EF-hand, calcium binding motif, found in reticulocalbin-2 (RCN2) mainly from protostomes; This ...
 78-169 2.64e-03

EF-hand, calcium binding motif, found in reticulocalbin-2 (RCN2) mainly from protostomes; This family corresponds to a group of uncharacterized RCN2-like proteins, which are mainly found in protostomes. Although their biological function remains unclear, they show high sequence similarity with RCN2 (also known as E6BP or TCBP-49), which is an endoplasmic reticulum resident low-affinity Ca2+-binding protein that has been implicated in immunity, redox homeostasis, cell cycle regulation and coagulation. Members in this family contain six copies of the EF-hand Ca2+-binding motif, but may lack a C-terminal His-Asp-Glu-Leu (HDEL) tetrapeptide that is required for retention of RCN2 in the endoplasmic reticulum (ER).


Pssm-ID: 320025 [Multi-domain]  Cd Length: 263  Bit Score: 39.61  E-value: 2.64e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9758252   78 KELFRVCDANRDGRVDYHEFRRYMDDKE------LELYRIFQAIDVEHNGCIS-PEGLWDslvKAGIEIKDE---ELARF 147
Cdd:cd16227 125 KEMFEAADLNKDGKLDKTEFSAFQHPEEyphmhpVLIEQTLRDKDKDNDGFISfQEFLGD---RAGHEDKEWllvEKDRF 201

                        90       100
                ....*....|....*....|..
gi 9758252  148 VEHVDKDNDGIIMFEEWRDFLL 169
Cdd:cd16227 202 DEDYDKDGDGKLDGEEILSWLV 223
EF-hand_6 pfam13405
EF-hand domain;
78-101 8.94e-03

EF-hand domain;


Pssm-ID: 463869 [Multi-domain]  Cd Length: 30  Bit Score: 33.69  E-value: 8.94e-03
                          10        20
                  ....*....|....*....|....
gi 9758252     78 KELFRVCDANRDGRVDYHEFRRYM 101
Cdd:pfam13405   3 REAFKLFDKDGDGKISLEELRKAL 26
 
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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