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Conserved domains on  [gi|56699401|ref|NP_443133|]
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mitochondrial adenyl nucleotide antiporter SLC25A25 isoform a [Homo sapiens]

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
 191-445 3.03e-33

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: 127.58  E-value: 3.03e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56699401  191 VAGGGAGAVSRTCTAPLDRLKVLMQVHAS----RSNNM----GIVGGFTQMIREGGARSLWRGNGINVLKIAPESAIKFM 262
Cdd:PTZ00169  12 LMGGISAAISKTAVAPIERVKMLIQTQDSipeiKSGKVprysGIVNCFRRVSKEQGVLSLWRGNTANVIRYFPTQAFNFA 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56699401  263 AYEQIKRLVGS-DQET---LRIHERLVAGSLAGAIAQSSIYPMEVLKTRMA--LRKTG--QYSGMLDCARRILAREGVAA 334
Cdd:PTZ00169  92 FKDYFKNMFPKyNQKTdfwKFFGVNILSGGLAGASSLLIVYPLDFARTRLAsdIGKGGdrEFTGLFDCLMKISKQTGFLS 171

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56699401  335 FYKGYVPNMLGIIPYAGIDLAVYETLKNAWLQhyavNSADPGVFVLLACGTMSSTCGQLASYPLALVRTRMQAQASIEGA 414
Cdd:PTZ00169 172 LYQGFGVSVQGIIVYRGAYFGLYDSAKALLFG----NDKNTNILYKWAVAQTVTILAGLISYPFDTVRRRMMMMSGRKAK 247

                        250       260       270
                 ....*....|....*....|....*....|....
gi 56699401  415 PEVTMSS---LFKHILRTEGAFGLYRGLAPNFMK 445
Cdd:PTZ00169 248 SEIQYTGtldCWKKILKNEGLGGFFKGAWANVLR 281
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
39-143 8.30e-17

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


:

Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 76.75  E-value: 8.30e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56699401  39 FIPSQEFST-YRQWKQKIVQAGDKDLDGQLDFEEFVHY-----LQDHEKKLRLVFKSLDKKNDGRIDAQEIMQSLRDLGV 112
Cdd:COG5126  21 VLERDDFEAlFRRLWATLFSEADTDGDGRISREEFVAGmeslfEATVEPFARAAFDLLDTDGDGKISADEFRRLLTALGV 100

                        90       100       110
                ....*....|....*....|....*....|....*
gi 56699401 113 kiSEQQAEKILKSMDKNGTMTIDWNE----WRDYH 143
Cdd:COG5126 101 --SEEEADELFARLDTDGDGKISFEEfvaaVRDYY 133
 
Name Accession Description Interval E-value
PTZ00169 PTZ00169
ADP/ATP transporter on adenylate translocase; Provisional
 191-445 3.03e-33

ADP/ATP transporter on adenylate translocase; Provisional


Pssm-ID: 240302 [Multi-domain]  Cd Length: 300  Bit Score: 127.58  E-value: 3.03e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56699401  191 VAGGGAGAVSRTCTAPLDRLKVLMQVHAS----RSNNM----GIVGGFTQMIREGGARSLWRGNGINVLKIAPESAIKFM 262
Cdd:PTZ00169  12 LMGGISAAISKTAVAPIERVKMLIQTQDSipeiKSGKVprysGIVNCFRRVSKEQGVLSLWRGNTANVIRYFPTQAFNFA 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56699401  263 AYEQIKRLVGS-DQET---LRIHERLVAGSLAGAIAQSSIYPMEVLKTRMA--LRKTG--QYSGMLDCARRILAREGVAA 334
Cdd:PTZ00169  92 FKDYFKNMFPKyNQKTdfwKFFGVNILSGGLAGASSLLIVYPLDFARTRLAsdIGKGGdrEFTGLFDCLMKISKQTGFLS 171

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56699401  335 FYKGYVPNMLGIIPYAGIDLAVYETLKNAWLQhyavNSADPGVFVLLACGTMSSTCGQLASYPLALVRTRMQAQASIEGA 414
Cdd:PTZ00169 172 LYQGFGVSVQGIIVYRGAYFGLYDSAKALLFG----NDKNTNILYKWAVAQTVTILAGLISYPFDTVRRRMMMMSGRKAK 247

                        250       260       270
                 ....*....|....*....|....*....|....
gi 56699401  415 PEVTMSS---LFKHILRTEGAFGLYRGLAPNFMK 445
Cdd:PTZ00169 248 SEIQYTGtldCWKKILKNEGLGGFFKGAWANVLR 281
Mito_carr pfam00153
Mitochondrial carrier protein;
276-368 2.67e-28

Mitochondrial carrier protein;


Pssm-ID: 395101 [Multi-domain]  Cd Length: 96  Bit Score: 107.36  E-value: 2.67e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56699401   276 ETLRIHERLVAGSLAGAIAQSSIYPMEVLKTRMAL---RKTGQYSGMLDCARRILAREGVAAFYKGYVPNMLGIIPYAGI 352
Cdd:pfam00153   1 SELSFLASLLAGGIAGAIAVTVTYPLDVVKTRLQVqggSGKSKGRGILDCFKKIYKEEGIRGLYKGLLPNLLRVAPAAAI 80

                          90
                  ....*....|....*.
gi 56699401   353 DLAVYETLKNAWLQHY 368
Cdd:pfam00153  81 YFGTYETLKRLLLKKL 96
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
39-143 8.30e-17

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


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 76.75  E-value: 8.30e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56699401  39 FIPSQEFST-YRQWKQKIVQAGDKDLDGQLDFEEFVHY-----LQDHEKKLRLVFKSLDKKNDGRIDAQEIMQSLRDLGV 112
Cdd:COG5126  21 VLERDDFEAlFRRLWATLFSEADTDGDGRISREEFVAGmeslfEATVEPFARAAFDLLDTDGDGKISADEFRRLLTALGV 100

                        90       100       110
                ....*....|....*....|....*....|....*
gi 56699401 113 kiSEQQAEKILKSMDKNGTMTIDWNE----WRDYH 143
Cdd:COG5126 101 --SEEEADELFARLDTDGDGKISFEEfvaaVRDYY 133
EFh_PEF_ALG-2_like cd16185
EF-hand, calcium binding motif, found in homologs of mammalian apoptosis-linked gene 2 protein ...
 53-139 1.09e-12

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: 65.70  E-value: 1.09e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56699401  53 QKIVQAGDKDLDGQLDFEEFVH---YLQDhekkLRLVFKSLDKKNDGRIDAQEIMQSLRDLGVKISEQQAEKILKSMDKN 129
Cdd:cd16185  39 EKLIRMFDRDGNGTIDFEEFAAlhqFLSN----MQNGFEQRDTSRSGRLDANEVHEALAASGFQLDPPAFQALFRKFDPD 114

                        90
                ....*....|
gi 56699401 130 GTMTIDWNEW 139
Cdd:cd16185 115 RGGSLGFDDY 124
EF-hand_7 pfam13499
EF-hand domain pair;
80-138 6.84e-12

EF-hand domain pair;


Pssm-ID: 463900 [Multi-domain]  Cd Length: 67  Bit Score: 60.73  E-value: 6.84e-12
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 56699401    80 EKKLRLVFKSLDKKNDGRIDAQEIMQSLR--DLGVKISEQQAEKILKSMDKNGTMTIDWNE 138
Cdd:pfam13499   1 EEKLKEAFKLLDSDGDGYLDVEELKKLLRklEEGEPLSDEEVEELFKEFDLDKDGRISFEE 61
PTZ00184 PTZ00184
calmodulin; Provisional
 60-139 1.56e-10

calmodulin; Provisional


Pssm-ID: 185504 [Multi-domain]  Cd Length: 149  Bit Score: 59.39  E-value: 1.56e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56699401   60 DKDLDGQLDFEEFVHYLQ------DHEKKLRLVFKSLDKKNDGRIDAQEIMQSLRDLGVKISEQQAEKILKSMDKNGTMT 133
Cdd:PTZ00184  57 DADGNGTIDFPEFLTLMArkmkdtDSEEEIKEAFKVFDRDGNGFISAAELRHVMTNLGEKLTDEEVDEMIREADVDGDGQ 136


                 ....*.
gi 56699401  134 IDWNEW 139
Cdd:PTZ00184 137 INYEEF 142
 
Name Accession Description Interval E-value
PTZ00169 PTZ00169
ADP/ATP transporter on adenylate translocase; Provisional
 191-445 3.03e-33

ADP/ATP transporter on adenylate translocase; Provisional


Pssm-ID: 240302 [Multi-domain]  Cd Length: 300  Bit Score: 127.58  E-value: 3.03e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56699401  191 VAGGGAGAVSRTCTAPLDRLKVLMQVHAS----RSNNM----GIVGGFTQMIREGGARSLWRGNGINVLKIAPESAIKFM 262
Cdd:PTZ00169  12 LMGGISAAISKTAVAPIERVKMLIQTQDSipeiKSGKVprysGIVNCFRRVSKEQGVLSLWRGNTANVIRYFPTQAFNFA 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56699401  263 AYEQIKRLVGS-DQET---LRIHERLVAGSLAGAIAQSSIYPMEVLKTRMA--LRKTG--QYSGMLDCARRILAREGVAA 334
Cdd:PTZ00169  92 FKDYFKNMFPKyNQKTdfwKFFGVNILSGGLAGASSLLIVYPLDFARTRLAsdIGKGGdrEFTGLFDCLMKISKQTGFLS 171

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56699401  335 FYKGYVPNMLGIIPYAGIDLAVYETLKNAWLQhyavNSADPGVFVLLACGTMSSTCGQLASYPLALVRTRMQAQASIEGA 414
Cdd:PTZ00169 172 LYQGFGVSVQGIIVYRGAYFGLYDSAKALLFG----NDKNTNILYKWAVAQTVTILAGLISYPFDTVRRRMMMMSGRKAK 247

                        250       260       270
                 ....*....|....*....|....*....|....
gi 56699401  415 PEVTMSS---LFKHILRTEGAFGLYRGLAPNFMK 445
Cdd:PTZ00169 248 SEIQYTGtldCWKKILKNEGLGGFFKGAWANVLR 281
Mito_carr pfam00153
Mitochondrial carrier protein;
276-368 2.67e-28

Mitochondrial carrier protein;


Pssm-ID: 395101 [Multi-domain]  Cd Length: 96  Bit Score: 107.36  E-value: 2.67e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56699401   276 ETLRIHERLVAGSLAGAIAQSSIYPMEVLKTRMAL---RKTGQYSGMLDCARRILAREGVAAFYKGYVPNMLGIIPYAGI 352
Cdd:pfam00153   1 SELSFLASLLAGGIAGAIAVTVTYPLDVVKTRLQVqggSGKSKGRGILDCFKKIYKEEGIRGLYKGLLPNLLRVAPAAAI 80

                          90
                  ....*....|....*.
gi 56699401   353 DLAVYETLKNAWLQHY 368
Cdd:pfam00153  81 YFGTYETLKRLLLKKL 96
Mito_carr pfam00153
Mitochondrial carrier protein;
186-274 4.80e-28

Mitochondrial carrier protein;


Pssm-ID: 395101 [Multi-domain]  Cd Length: 96  Bit Score: 106.97  E-value: 4.80e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56699401   186 WWRHLVAGGGAGAVSRTCTAPLDRLKVLMQVHA--SRSNNMGIVGGFTQMIREGGARSLWRGNGINVLKIAPESAIKFMA 263
Cdd:pfam00153   5 FLASLLAGGIAGAIAVTVTYPLDVVKTRLQVQGgsGKSKGRGILDCFKKIYKEEGIRGLYKGLLPNLLRVAPAAAIYFGT 84

                          90
                  ....*....|.
gi 56699401   264 YEQIKRLVGSD 274
Cdd:pfam00153  85 YETLKRLLLKK 95
Mito_carr pfam00153
Mitochondrial carrier protein;
374-465 3.48e-22

Mitochondrial carrier protein;


Pssm-ID: 395101 [Multi-domain]  Cd Length: 96  Bit Score: 90.79  E-value: 3.48e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56699401   374 DPGVFVLLACGTMSSTCGQLASYPLALVRTRMQAQASIEGAPEVTMSSLFKHILRTEGAFGLYRGLAPNFMKVIPAVSIS 453
Cdd:pfam00153   2 ELSFLASLLAGGIAGAIAVTVTYPLDVVKTRLQVQGGSGKSKGRGILDCFKKIYKEEGIRGLYKGLLPNLLRVAPAAAIY 81

                          90
                  ....*....|..
gi 56699401   454 YVVYENLKITLG 465
Cdd:pfam00153  82 FGTYETLKRLLL 93
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
39-143 8.30e-17

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


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 76.75  E-value: 8.30e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56699401  39 FIPSQEFST-YRQWKQKIVQAGDKDLDGQLDFEEFVHY-----LQDHEKKLRLVFKSLDKKNDGRIDAQEIMQSLRDLGV 112
Cdd:COG5126  21 VLERDDFEAlFRRLWATLFSEADTDGDGRISREEFVAGmeslfEATVEPFARAAFDLLDTDGDGKISADEFRRLLTALGV 100

                        90       100       110
                ....*....|....*....|....*....|....*
gi 56699401 113 kiSEQQAEKILKSMDKNGTMTIDWNE----WRDYH 143
Cdd:COG5126 101 --SEEEADELFARLDTDGDGKISFEEfvaaVRDYY 133
EFh_PEF_ALG-2_like cd16185
EF-hand, calcium binding motif, found in homologs of mammalian apoptosis-linked gene 2 protein ...
 53-139 1.09e-12

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: 65.70  E-value: 1.09e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56699401  53 QKIVQAGDKDLDGQLDFEEFVH---YLQDhekkLRLVFKSLDKKNDGRIDAQEIMQSLRDLGVKISEQQAEKILKSMDKN 129
Cdd:cd16185  39 EKLIRMFDRDGNGTIDFEEFAAlhqFLSN----MQNGFEQRDTSRSGRLDANEVHEALAASGFQLDPPAFQALFRKFDPD 114

                        90
                ....*....|
gi 56699401 130 GTMTIDWNEW 139
Cdd:cd16185 115 RGGSLGFDDY 124
EFh cd00051
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal ...
 82-141 2.62e-12

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: 61.79  E-value: 2.62e-12
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 56699401  82 KLRLVFKSLDKKNDGRIDAQEIMQSLRDLGVKISEQQAEKILKSMDKNGTMTIDWNEWRD 141
Cdd:cd00051   1 ELREAFRLFDKDGDGTISADELKAALKSLGEGLSEEEIDEMIREVDKDGDGKIDFEEFLE 60
PTZ00169 PTZ00169
ADP/ATP transporter on adenylate translocase; Provisional
 190-344 4.38e-12

ADP/ATP transporter on adenylate translocase; Provisional


Pssm-ID: 240302 [Multi-domain]  Cd Length: 300  Bit Score: 66.72  E-value: 4.38e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56699401  190 LVAGGGAGAVSRTCTAPLD----RLKVLMQVHASRSNNmGIVGGFTQMIREGGARSLWRGNGINVLKIAPESAIKFMAYE 265
Cdd:PTZ00169 117 ILSGGLAGASSLLIVYPLDfartRLASDIGKGGDREFT-GLFDCLMKISKQTGFLSLYQGFGVSVQGIIVYRGAYFGLYD 195

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56699401  266 QIKRLV-GSDQETLRIHERLVAGS---LAGAIAqssiYPMEVLKTRMAL---RKTG---QYSGMLDCARRILAREGVAAF 335
Cdd:PTZ00169 196 SAKALLfGNDKNTNILYKWAVAQTvtiLAGLIS----YPFDTVRRRMMMmsgRKAKseiQYTGTLDCWKKILKNEGLGGF 271


                 ....*....
gi 56699401  336 YKGYVPNML 344
Cdd:PTZ00169 272 FKGAWANVL 280
EF-hand_7 pfam13499
EF-hand domain pair;
80-138 6.84e-12

EF-hand domain pair;


Pssm-ID: 463900 [Multi-domain]  Cd Length: 67  Bit Score: 60.73  E-value: 6.84e-12
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 56699401    80 EKKLRLVFKSLDKKNDGRIDAQEIMQSLR--DLGVKISEQQAEKILKSMDKNGTMTIDWNE 138
Cdd:pfam13499   1 EEKLKEAFKLLDSDGDGYLDVEELKKLLRklEEGEPLSDEEVEELFKEFDLDKDGRISFEE 61
PTZ00184 PTZ00184
calmodulin; Provisional
 60-139 1.56e-10

calmodulin; Provisional


Pssm-ID: 185504 [Multi-domain]  Cd Length: 149  Bit Score: 59.39  E-value: 1.56e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56699401   60 DKDLDGQLDFEEFVHYLQ------DHEKKLRLVFKSLDKKNDGRIDAQEIMQSLRDLGVKISEQQAEKILKSMDKNGTMT 133
Cdd:PTZ00184  57 DADGNGTIDFPEFLTLMArkmkdtDSEEEIKEAFKVFDRDGNGFISAAELRHVMTNLGEKLTDEEVDEMIREADVDGDGQ 136


                 ....*.
gi 56699401  134 IDWNEW 139
Cdd:PTZ00184 137 INYEEF 142
EFh_PEF_Group_I cd16180
Penta-EF hand, calcium binding motifs, found in Group I PEF proteins; The family corresponds ...
 60-134 2.67e-08

Penta-EF hand, calcium binding motifs, found in Group I PEF proteins; The family corresponds to Group I PEF proteins that have been found not only in higher animals but also in lower animals, plants, fungi and protists. Group I PEF proteins include apoptosis-linked gene 2 protein (ALG-2), peflin and similar proteins. ALG-2, also termed programmed cell death protein 6 (PDCD6), is a widely expressed calcium-binding modulator protein associated with cell proliferation and death, as well as cell survival. It forms a homodimer in the cell or a heterodimer with its closest paralog peflin. Among the PEF proteins, ALG-2 can bind three Ca2+ ions through its EF1, EF3, and EF5 hands, where it is unique in that its EF5 hand binds Ca2+ ion in a canonical coordination. Peflin is a ubiquitously expressed 30-kD PEF protein containing five EF-hand motifs in its C-terminal domain and a longer N-terminal hydrophobic domain (NHB domain) than any other member of the PEF family. The NHB domain harbors nine repeats of a nonapeptide (A/PPGGPYGGP). Peflin may modulate the function of ALG-2 in Ca2+ signaling. It exists only as a heterodimer with ALG-2, and binds two Ca2+ ions through its EF1 and EF3 hands. Its additional EF5 hand is unpaired and does not bind Ca2+ ion but mediates the heterodimerization with ALG-2. The dissociation of heterodimer occurs in the presence of Ca2+.


Pssm-ID: 320055 [Multi-domain]  Cd Length: 164  Bit Score: 53.30  E-value: 2.67e-08
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 56699401  60 DKDLDGQLDFEEFV---HYLQDHEKklrlVFKSLDKKNDGRIDAQEIMQSLRDLGVKISEQQAEKILKSMDKNGTMTI 134
Cdd:cd16180  47 DRDRSGTINFDEFVglwKYIQDWRR----LFRRFDRDRSGSIDFNELQNALSSFGYRLSPQFVQLLVRKFDRRRRGSI 120
EFh_PEF cd15897
The penta-EF hand (PEF) family; The penta-EF hand (PEF) family contains a group of five ...
 53-135 3.05e-08

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: 53.20  E-value: 3.05e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56699401  53 QKIVQAGDKDLDGQLDFEEFvHYLQDHEKKLRLVFKSLDKKNDGRIDAQEIMQSLRDLGVKISEQQAEKILKSMDK-NGT 131
Cdd:cd15897  43 RSMIAMMDRDHSGKLNFSEF-KGLWNYIKAWQEIFRTYDTDGSGTIDSNELRQALSGAGYRLSEQTYDIIIRRYDRgRGN 121


                ....
gi 56699401 132 MTID 135
Cdd:cd15897 122 IDFD 125
EFh_PEF_ALG-2 cd16183
EF-hand, calcium binding motif, found in apoptosis-linked gene 2 protein (ALG-2) and similar ...
 60-135 2.17e-07

EF-hand, calcium binding motif, found in apoptosis-linked gene 2 protein (ALG-2) and similar proteins; ALG-2, also termed programmed cell death protein 6 (PDCD6), or probable calcium-binding protein ALG-2, is one of the prototypic members of the penta EF-hand protein family. It is a widely expressed calcium-binding modulator protein associated with cell proliferation and death, as well as cell survival. ALG-2 acts as a pro-apoptotic factor participating in T cell receptor-, Fas-, and glucocorticoid-induced programmed cell death, and also serves as a useful molecular marker for the prognosis of cancers. Moreover, ALG-2 functions as a calcium ion sensor at endoplasmic reticulum (ER) exit sites, and modulates ER-stress-stimulated cell death and neuronal apoptosis during organ formation. Furthermore, ALG-2 can mediate the pro-apoptotic activity of cisplatin or tumor necrosis factor alpha (TNFalpha) through the down-regulation of nuclear factor-kappaB (NF-kappaB) expression. It also inhibits angiogenesis through PI3K/mTOR/p70S6K pathway by interacting of vascular endothelial growth factor receptor-2 (VEGFR-2). In addition, nuclear ALG-2 may participate in the post-transcriptional regulation of Inositol Trisphosphate Receptor Type 1 (IP3R1) pre-mRNA at least in part by interacting with CHERP (Ca2+ homeostasis endoplasmic reticulum protein) calcium-dependently. ALG-2 contains five serially repeated EF-hand motifs and interacts with various proteins, including ALG-2-interacting protein X (Alix), Fas, annexin XI, death-associated protein kinase 1 (DAPk1), Tumor susceptibility gene 101 (TSG101), Sec31A, phospholipid scramblase 3 (PLSCR3), the P-body component PATL1, and endosomal sorting complex required for transport (ESCRT)-III-related protein IST1, in a calcium-dependent manner. It forms a homodimer in the cell or a heterodimer with its closest paralog peflin. Among the PEF proteins, ALG-2 can bind three Ca2+ ions through its EF1, EF3, and EF5 hands, where it is unique in that its EF5 hand binds Ca2+ ion in a canonical coordination.


Pssm-ID: 320058 [Multi-domain]  Cd Length: 165  Bit Score: 50.72  E-value: 2.17e-07
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 56699401  60 DKDLDGQLDFEEFV---HYLQDHEKklrlVFKSLDKKNDGRIDAQEIMQSLRDLGVKISEQQAEKILKSMDKNGTMTID 135
Cdd:cd16183  47 DRDNSGTINFQEFAalwKYITDWQN----CFRSFDRDNSGNIDKNELKQALTSFGYRLSDQFYDILVRKFDRQGRGTIA 121
EFh_CREC_RCN2_like cd16227
EF-hand, calcium binding motif, found in reticulocalbin-2 (RCN2) mainly from protostomes; This ...
 60-135 2.86e-07

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: 51.55  E-value: 2.86e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56699401  60 DKDLDGQLDFEEFVHYLQDHEKKLRLV-----FKS-LDKKNDGRIDAQEIMQSLRDLGVKISEQQAEKILKS--MDKNGT 131
Cdd:cd16227 169 DKDNDGFISFQEFLGDRAGHEDKEWLLvekdrFDEdYDKDGDGKLDGEEILSWLVPDNEEIAEEEVDHLFASadDDHDDR 248


                ....
gi 56699401 132 MTID 135
Cdd:cd16227 249 LSFD 252
EFh_PI-PLC cd15898
EF-hand motif found in eukaryotic phosphoinositide-specific phospholipase C (PI-PLC, EC 3.1.4. ...
 82-159 3.07e-07

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: 49.59  E-value: 3.07e-07
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 56699401  82 KLRLVFKSLDKKNDGRIDAQEIMQSLRDLGVKISEQQAEKILKSMDKNGTMTIDWNEWRD-YHLLHpveNIPEIILYWK 159
Cdd:cd15898   1 WLRRQWIKADKDGDGKLSLKEIKKLLKRLNIRVSEKELKKLFKEVDTNGDGTLTFDEFEElYKSLT---ERPELEPIFK 76
EFh_PEF_peflin cd16184
EF-hand, calcium binding motif, found in peflin and similar proteins; Peflin, also termed ...
 60-135 1.06e-06

EF-hand, calcium binding motif, found in peflin and similar proteins; Peflin, also termed penta-EF hand (PEF) protein with a long N-terminal hydrophobic domain, or penta-EF hand domain-containing protein 1, is a ubiquitously expressed 30-kD PEF protein containing five EF-hand motifs in its C-terminal domain and a longer N-terminal hydrophobic domain (NHB domain) than any other member of the PEF family. The NHB domain harbors nine repeats of a nonapeptide (A/PPGGPYGGP). Peflin may modulate the function of ALG-2 in Ca2+ signaling. It exists only as a heterodimer with ALG-2, and binds two Ca2+ ions through its EF1 and EF3 hands. Its additional EF5 hand is unpaired and does not bind Ca2+ ion but mediates the heterodimerization with ALG-2. The dissociation of heterodimer occurs in the presence of Ca2+. In lower vertebrates, peflin may interact with transient receptor potential N (TRPN1), suggesting a potential role of peflin in fast transducer channel adaptation.


Pssm-ID: 320059 [Multi-domain]  Cd Length: 165  Bit Score: 48.41  E-value: 1.06e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56699401  60 DKDLDGQLDFEEFV---HYLQdhekKLRLVFKSLDKKNDGRIDAQEIMQSLRDLGVKISEQQAEKILKSMD--KNGTMTI 134
Cdd:cd16184  47 DKDKSGTIDIYEFQalwNYIQ----QWKQVFQQFDRDRSGSIDENELHQALSQMGYRLSPQFVQFLVSKYDprARRSLTL 122


                .
gi 56699401 135 D 135
Cdd:cd16184 123 D 123
EFh_PI-PLC cd15898
EF-hand motif found in eukaryotic phosphoinositide-specific phospholipase C (PI-PLC, EC 3.1.4. ...
 29-135 1.75e-06

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: 47.28  E-value: 1.75e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56699401  29 ELKSIFK-LSVFIPSQEFstyrqwKQKIVQAgDKDLDGQLDFEEFVH-YLQDHEKK-LRLVFKSLDKKNDGRIDAQEIMQ 105
Cdd:cd15898  21 EIKKLLKrLNIRVSEKEL------KKLFKEV-DTNGDGTLTFDEFEElYKSLTERPeLEPIFKKYAGTNRDYMTLEEFIR 93

                        90       100       110
                ....*....|....*....|....*....|....
gi 56699401 106 SLRD-LGVKISEQQAEKILKSMD---KNGTMTID 135
Cdd:cd15898  94 FLREeQGENVSEEECEELIEKYEperENRQLSFE 127
PTZ00168 PTZ00168
mitochondrial carrier protein; Provisional
 284-461 2.67e-06

mitochondrial carrier protein; Provisional


Pssm-ID: 185494 [Multi-domain]  Cd Length: 259  Bit Score: 48.77  E-value: 2.67e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56699401  284 LVAGSLAGAIAQSSIYPMEVLKTRMALRKTGQYSgmldcarrilareGVAAFYKGYVPNMLGIIPYAGIDLAVYEtLKNA 363
Cdd:PTZ00168   7 LVTGALSGVIVDAVLYPIDSIKTNIQAKKSFSFS-------------DIKKLYSGILPTLVGTVPASAFFYCFYE-LSKK 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56699401  364 WLQHYAVNSADPGVFvlLACGTMSSTCGQLASYPLALVRTRMQAQASIegapevtmsSLFKHILRTEGAFGLYRGLAPNF 443
Cdd:PTZ00168  73 LLTEYRENISKTNLY--LISTSIAEITACIVRLPFEIVKQNMQVSGNI---------SVLKTIYEITQREGLPSFLGKSY 141

                        170       180
                 ....*....|....*....|..
gi 56699401  444 M----KVIPAVSISYVVYENLK 461
Cdd:PTZ00168 142 FvmivREIPFDCIQYFLWETLK 163
EFh cd00051
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal ...
 60-105 2.79e-06

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: 44.46  E-value: 2.79e-06
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|.
gi 56699401  60 DKDLDGQLDFEEFVHYLQDH-----EKKLRLVFKSLDKKNDGRIDAQEIMQ 105
Cdd:cd00051  10 DKDGDGTISADELKAALKSLgeglsEEEIDEMIREVDKDGDGKIDFEEFLE 60
PTZ00168 PTZ00168
mitochondrial carrier protein; Provisional
 188-438 7.45e-06

mitochondrial carrier protein; Provisional


Pssm-ID: 185494 [Multi-domain]  Cd Length: 259  Bit Score: 47.23  E-value: 7.45e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56699401  188 RHLVAGGGAGAVSRTCTAPLDRLKVLMQVHASRSnnmgivggFTQMireggaRSLWRGNGINVLKIAPESAIKFMAYEQI 267
Cdd:PTZ00168   5 HNLVTGALSGVIVDAVLYPIDSIKTNIQAKKSFS--------FSDI------KKLYSGILPTLVGTVPASAFFYCFYELS 70

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56699401  268 KRLVGSDQETL-RIHERLVAGSLAGAIAQSSIYPMEVLKTRMalrktgQYSG---MLDCARRILAREGVAAFY-KGYVPN 342
Cdd:PTZ00168  71 KKLLTEYRENIsKTNLYLISTSIAEITACIVRLPFEIVKQNM------QVSGnisVLKTIYEITQREGLPSFLgKSYFVM 144

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56699401  343 MLGIIPYAGIDLAVYETLKNAWLQHYAVNSADPGVFVLLACGTMSSTCGQLASYPLALVRTR--MQAQASIEGAPEVTms 420
Cdd:PTZ00168 145 IVREIPFDCIQYFLWETLKEKAKKDFGKFSKKYPSITSAICGGLAGGIAGFLTTPVDVIKSRqiIYGKSYIETVTEIA-- 222

                        250
                 ....*....|....*...
gi 56699401  421 slfkhilrTEGAFGLYRG 438
Cdd:PTZ00168 223 --------EEGYLTFYKG 232
EFh_calglandulin_like cd16252
EF-hand, calcium binding motif, found in uncharacterized calglandulin-like proteins; The ...
 60-141 7.92e-06

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: 44.44  E-value: 7.92e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56699401  60 DKDLD---------GQLDFEEFVHYLQ------DHEKKLRLVFKSLDKKNDGRIDAQEIMQSLRDL-----GVKISEQQA 119
Cdd:cd16252   1 DKDIDllpsemrhhGSFNYSKFFEYMQkfqtseQQEEAIRKAFQMLDKDKSGFIEWNEIKYILSTVpssmpVAPLSDEEA 80

                        90       100
                ....*....|....*....|..
gi 56699401 120 EKILKSMDKNGTMTIDWNEWRD 141
Cdd:cd16252  81 EAMIQAADTDGDGRIDFQEFSD 102
EFh_PEF_CPNS1_2 cd16188
Penta-EF hand, calcium binding motifs, found in calcium-dependent protease small subunit ...
 55-135 9.06e-06

Penta-EF hand, calcium binding motifs, found in calcium-dependent protease small subunit CAPNS1 and CAPNS2; CAPNS1, also termed calpain small subunit 1 (CSS1), or calcium-activated neutral proteinase small subunit (CANP small subunit), or calcium-dependent protease small subunit (CDPS), or calpain regulatory subunit, is a common 28-kDa regulatory calpain subunit encoded by the calpain small 1 (Capns1, also known as Capn4) gene. It acts as a binding partner to form a heterodimer with the 80 kDa calpain large catalytic subunit and is required in maintaining the activity of calpain. CAPNS1 plays a significant role in tumor progression of human cancer, and functions as a potential therapeutic target in human hepatocellular carcinoma (HCC), nasopharyngeal carcinoma (NPC), glioma, and clear cell renal cell carcinoma (ccRCC). It may be involved in regulating migration and cell survival through binding to the SH3 domain of Ras GTPase-activating protein (RasGAP). It may also modulate Akt/FoxO3A signaling and apoptosis through PP2A. CAPNS1 contains an N-terminal glycine rich domain and a C-terminal PEF-hand domain. CAPNS2, also termed calpain small subunit 2 (CSS2), is a novel tissue-specific 30 kDa calpain small subunit that lacks two oligo-Gly stretches characteristic of the N-terminal Gly-rich domain of CAPNS1. CAPNS2 acts as a chaperone for the calpain large subunit, and appears to be the functional equivalent of CAPNS1. However, CAPNS2 binds the large subunit much more weakly than CAPNS1 and it does not undergo the autolytic conversion typical of CAPNS1.


Pssm-ID: 320063 [Multi-domain]  Cd Length: 169  Bit Score: 45.89  E-value: 9.06e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56699401  55 IVQAGDKDLDGQLDFEEFvHYLQDHEKKLRLVFKSLDKKNDGRIDAQEIMQSLRDLGVKISEQQAEKILKSM-DKNGTMT 133
Cdd:cd16188  48 MVAVMDSDTTGKLGFEEF-KYLWNNIKKWQGIYKQFDTDRSGTIGSQELPGAFEAAGFHLNEQLYQMIIRRYsDEDGNMD 126


                ..
gi 56699401 134 ID 135
Cdd:cd16188 127 FD 128
EF-hand_7 pfam13499
EF-hand domain pair;
60-105 1.15e-05

EF-hand domain pair;


Pssm-ID: 463900 [Multi-domain]  Cd Length: 67  Bit Score: 43.01  E-value: 1.15e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 56699401    60 DKDLDGQLDFEEFVHYLQDH-------EKKLRLVFKSLDKKNDGRIDAQEIMQ 105
Cdd:pfam13499  12 DSDGDGYLDVEELKKLLRKLeegeplsDEEVEELFKEFDLDKDGRISFEEFLE 64
PTZ00183 PTZ00183
centrin; Provisional
 77-141 1.40e-05

centrin; Provisional


Pssm-ID: 185503 [Multi-domain]  Cd Length: 158  Bit Score: 45.07  E-value: 1.40e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 56699401   77 QDHEKKLRLVFKSLDKKNDGRIDAQEIMQSLRDLGVKISEQQAEKILKSMDKNGTMTIDWNEWRD 141
Cdd:PTZ00183  13 EDQKKEIREAFDLFDTDGSGTIDPKELKVAMRSLGFEPKKEEIKQMIADVDKDGSGKIDFEEFLD 77
EFh_PEF_Group_II_sorcin_like cd16181
Penta-EF hand, calcium binding motifs, found in sorcin, grancalcin, and similar proteins; The ...
 60-135 3.73e-05

Penta-EF hand, calcium binding motifs, found in sorcin, grancalcin, and similar proteins; The family corresponds to the second group of penta-EF hand (PEF) proteins that includes sorcin, grancalcin, and similar proteins. Sorcin, also termed 22 kDa Ca2+-binding protein, CP-22, or V19, is a soluble resistance-related calcium-binding protein that is expressed in normal mammalian tissues, such as the liver, lungs and heart. It contains a flexible glycine and proline-rich N-terminal extension and five EF-hand motifs that associate with membranes in a calcium-dependent manner. It may harbor three potential Ca2+ binding sites through its EF1, EF2 and EF3 hands. However, binding of only two Ca2+/monomer suffices to trigger the conformational change that exposes hydrophobic regions and leads to interaction with the respective targets. Sorcin forms homodimers through the association of the unpaired EF5 hand. Among the PEF proteins, sorcin is unique in that it contains potential phosphorylation sites by cAMP-dependent protein kinase (PKA), and it can form a tetramer at slightly acid pH values although remaining a stable dimer at neutral pH. Grancalcin (GCA) is a cytosolic Ca2+-binding protein specifically expressed in neutrophils and monocytes/macrophages. It can strongly interact with sorcin to form a heterodimer and further modulate the function of sorcin. GCA exists as homodimers in solution. It contains five EF-hand motifs attached to an N-terminal region of an approximately 50 residue-long segment rich in glycines and prolines. In contrast with sorcin, GCA binds two Ca2+ ions through its EF1 and EF3 hands.


Pssm-ID: 320056 [Multi-domain]  Cd Length: 165  Bit Score: 43.90  E-value: 3.73e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56699401  60 DKDLDGQLDFEEFvhylqdheKKL-------RLVFKSLDKKNDGRIDAQEIMQSLRDLGVKISEQQAEKILKSMDKNGTM 132
Cdd:cd16181  50 DRDHSGKMGFNEF--------KELwaalnqwKTTFMQYDRDRSGTVEPQELQQAIRSFGYNLSPQALNVIVKRYSKNGRI 121


                ...
gi 56699401 133 TID 135
Cdd:cd16181 122 TFD 124
EFh_PI-PLCdelta cd16202
EF-hand motif found in phosphoinositide phospholipase C delta (PI-PLC-delta); PI-PLC-delta ...
 83-180 3.78e-05

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: 43.37  E-value: 3.78e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56699401  83 LRLVFKSLDKKNDGRIDAQEIMQSLRDLGVKISEQQAEKILKSMDKNGTMTIDWNEWRD-YHLLhpvENIPEIilywkhS 161
Cdd:cd16202   2 LKDQFRKADKNGDGKLSFKECKKLLKKLNVKVDKDYAKKLFQEADTSGEDVLDEEEFVQfYNRL---TKRPEI------E 72

                        90       100
                ....*....|....*....|....*
gi 56699401 162 TIFDV----GENLTVPD--EFTVEE 180
Cdd:cd16202  73 ELFKKysgdDEALTVEElrRFLQEE 97
EFh_PEF_ALG-2_like cd16185
EF-hand, calcium binding motif, found in homologs of mammalian apoptosis-linked gene 2 protein ...
 83-146 3.88e-05

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: 43.74  E-value: 3.88e-05
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 56699401  83 LRLVFKSLDKKNDGRIDAQEIMQSLRDLGVKISEQQAEKILKSMDKNGTMTIDWNEwrdYHLLH 146
Cdd:cd16185   2 LRQWFRAVDRDRSGSIDVNELQKALAGGGLLFSLATAEKLIRMFDRDGNGTIDFEE---FAALH 62
EFh_CREC_RCN2 cd16224
EF-hand, calcium binding motif, found in reticulocalbin-2 (RCN2); RCN2, also termed ...
 60-130 7.54e-05

EF-hand, calcium binding motif, found in reticulocalbin-2 (RCN2); RCN2, also termed calcium-binding protein ERC-55, or E6-binding protein (E6BP), or TCBP-49, is an endoplasmic reticulum resident low-affinity Ca2+-binding protein that has been implicated in immunity, redox homeostasis, cell cycle regulation and coagulation. It is associated with tumorigenesis, in particular with transformation of cells of the cervix induced by human papillomavirus (HPV), through binding to human papillomavirus (HPV) E6 oncogenic protein. It specifically interacts with vitamin D receptor among nuclear receptors. RCN2 contains an N-terminal signal sequence followed by six copies of the EF-hand Ca2+-binding motif, and a C-terminal His-Asp-Glu-Leu (HDEL) tetrapeptide that is required for retention of RCN2 in the endoplasmic reticulum (ER).


Pssm-ID: 320022 [Multi-domain]  Cd Length: 268  Bit Score: 44.35  E-value: 7.54e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56699401  60 DKDLDGQLDFEEFV-HYLQDH----------EKKLRLVfKSLDKKNDGRIDAQEIMQSLRDLGVKISEQQAEKILKSMDK 128
Cdd:cd16224 171 DKDGDGFISLEEFLgDYRKDPtanedpewiiVEKDRFV-NDYDKDNDGKLDPQELLPWVVPNNYGIAQEEALHLIDEMDL 249


                ..
gi 56699401 129 NG 130
Cdd:cd16224 250 NG 251
EFh_PEF_sorcin cd16187
Penta-EF hand, calcium binding motifs, found in sorcin; Sorcin, also termed 22 kDa Ca2 ...
 60-135 7.81e-05

Penta-EF hand, calcium binding motifs, found in sorcin; Sorcin, also termed 22 kDa Ca2+-binding protein, CP-22, or V19, is a soluble resistance-related calcium-binding protein that is expressed in normal mammalian tissues, such as the liver, lungs and heart. The up-regulation of sorcin is correlated with a number of cancer types, including colorectal, gastric and breast cancer. It may represent a therapeutic target for reversing tumor multidrug resistance (MDR). Sorcin participates in the regulation of calcium homeostasis in cells and is necessary for the activation of mitosis and cytokinesis. It enhances metastasis and promotes epithelial-to-mesenchymal transition of colorectal cancer. Moreover, sorcin has been implicated in the regulation of intracellular Ca2+ cycling and cardiac excitation-contraction coupling. It displays the anti-apoptotic properties via the modulation of mitochondrial Ca2+ handling in cardiac myocytes. It can target and activate the sarcolemmal Na+/Ca2+ exchanger (NCX1) in cardiac muscle. Meanwhile, sorcin modulates cardiac L-type Ca2+ current by functional interaction with the alpha1C subunit. It also associates with calcium/calmodulin-dependent protein kinase IIdeltaC (CaMKIIdelta(C)) and further modulates ryanodine receptor (RyR) function in cardiac myocytes. Furthermore, sorcin may act as a Ca2+ sensor for glucose-induced nuclear translocation and the activation of carbohydrate-responsive element-binding protein (ChREBP)-dependent genes. As a mitochondrial chaperone TRAP1 interactor, sorcin involves in mitochondrial metabolism through the TRAP1 pathway. In addition, sorcin may regulate the inhibition of type I interferon response in cells through interacting with foot-and-mouth disease virus (FMDV) VP1. Sorcin contains a flexible glycine and proline-rich N-terminal extension and five EF-hand motifs that associate with membranes in a calcium-dependent manner. It may harbor three potential Ca2+ binding sites through its EF1, EF2 and EF3 hands. However, binding of only two Ca2+/monomer suffices to trigger the conformational change that exposes hydrophobic regions and leads to interaction with the respective targets. Sorcin forms homodimers through the association of the unpaired EF5 hand. Among the PEF proteins, sorcin is unique in that it contains potential phosphorylation sites by cAMP-dependent protein kinase (PKA), and it can form a tetramer at slightly acid pH values although remaining a stable dimer at neutral pH.


Pssm-ID: 320062 [Multi-domain]  Cd Length: 165  Bit Score: 42.97  E-value: 7.81e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56699401  60 DKDLDGQLDFEEFvhylqdheKKLRLV-------FKSLDKKNDGRIDAQEIMQSLRDLGVKISEQQAEKILKSMDKNGTM 132
Cdd:cd16187  50 DRDMSGTMGFNEF--------KELWAVlngwrqhFISFDSDRSGTVDPQELQKALTTMGFRLSPQAVNSIAKRYSTNGKI 121


                ...
gi 56699401 133 TID 135
Cdd:cd16187 122 TFD 124
EFh_CREC cd15899
EF-hand, calcium binding motif, found in CREC-EF hand family; The CREC (Cab45/reticulocalbin ...
 53-143 8.15e-05

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: 44.35  E-value: 8.15e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56699401  53 QKIVQAGDKDLDGQLDFEEFV-------------HYLQDHEKKLRLVFkslDKKNDGRIDAQEIMQSLRDLGVKISEQQA 119
Cdd:cd15899 163 KETLEDLDKNGDGFISLEEFIsdpysadeneeepEWVKVEKERFVELR---DKDKDGKLDGEELLSWVDPSNQEIALEEA 239

                        90       100
                ....*....|....*....|....
gi 56699401 120 EKILKSMDKNGTMTIDWNEWRDYH 143
Cdd:cd15899 240 KHLIAESDENKDGKLSPEEILDNH 263
EFh_CREC_cab45 cd16225
EF-hand, calcium binding motif, found in 45 kDa calcium-binding protein (Cab45); Cab45, also ...
 68-146 1.23e-04

EF-hand, calcium binding motif, found in 45 kDa calcium-binding protein (Cab45); Cab45, also termed stromal cell-derived factor 4 (SDF-4), is a soluble, lumenal Golgi resident low-affinity Ca2+-binding protein that contains six copies of the EF-hand Ca2+-binding motif. It is required for secretory pathway calcium ATPase1 (SPCA1)-dependent Ca2+ import into the trans-Golgi network (TGN) and plays an essential role in Ca2+-dependent secretory cargo sorting at the TGN.


Pssm-ID: 320023 [Multi-domain]  Cd Length: 278  Bit Score: 43.83  E-value: 1.23e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56699401  68 DFEEfvhyLQDHEKKLRL--VFKSLDKKNDGRIDAQE----IMQSLRDlGVKISEQQAEKILKSMDKNGTMTIDWNEWRD 141
Cdd:cd16225  23 EFEE----DSEPKKRKKLkeIFKKVDVNTDGFLSAEEledwIMEKTQE-HFQEAVEENEQIFKAVDTDKDGNVSWEEYRV 97


                ....*
gi 56699401 142 YHLLH 146
Cdd:cd16225  98 HFLLS 102
EF-hand_6 pfam13405
EF-hand domain;
82-111 1.32e-04

EF-hand domain;


Pssm-ID: 463869 [Multi-domain]  Cd Length: 30  Bit Score: 39.08  E-value: 1.32e-04
                          10        20        30
                  ....*....|....*....|....*....|
gi 56699401    82 KLRLVFKSLDKKNDGRIDAQEIMQSLRDLG 111
Cdd:pfam13405   1 ELREAFKLFDKDGDGKISLEELRKALRSLG 30
PTZ00183 PTZ00183
centrin; Provisional
 10-138 1.95e-04

centrin; Provisional


Pssm-ID: 185503 [Multi-domain]  Cd Length: 158  Bit Score: 41.98  E-value: 1.95e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56699401   10 VIGEAQTEFQYFESKGL----PAELKSIFKLSVFIPSQEfstyrQWKQKIVQAgDKDLDGQLDFEEFVHYL------QDH 79
Cdd:PTZ00183  15 QKKEIREAFDLFDTDGSgtidPKELKVAMRSLGFEPKKE-----EIKQMIADV-DKDGSGKIDFEEFLDIMtkklgeRDP 88

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 56699401   80 EKKLRLVFKSLDKKNDGRIDAQEIMQSLRDLGVKISEQQAEKILKSMDKNGTMTIDWNE 138
Cdd:PTZ00183  89 REEILKAFRLFDDDKTGKISLKNLKRVAKELGETITDEELQEMIDEADRNGDGEISEEE 147
EFh_CREC_RCN2_like cd16227
EF-hand, calcium binding motif, found in reticulocalbin-2 (RCN2) mainly from protostomes; This ...
 53-138 1.98e-04

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: 43.07  E-value: 1.98e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56699401  53 QKIVQAGDKDLDGQLDFEEFVHYLQDHEKK------LRLVFKSLDKKNDGRIDAQEIM---QSLRDLGVKISEQqaEKIL 123
Cdd:cd16227 125 KEMFEAADLNKDGKLDKTEFSAFQHPEEYPhmhpvlIEQTLRDKDKDNDGFISFQEFLgdrAGHEDKEWLLVEK--DRFD 202

                        90
                ....*....|....*
gi 56699401 124 KSMDKNGTMTIDWNE 138
Cdd:cd16227 203 EDYDKDGDGKLDGEE 217
EFh_PEF_Group_II_CAPN_like cd16182
Penta-EF hand, calcium binding motifs, found in PEF calpain family; The PEF calpain family ...
 29-135 6.14e-04

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: 40.28  E-value: 6.14e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56699401  29 ELKSIFK---LSVFIPSQEFS--TYRQwkqkIVQAGDKDLDGQLDFEEFvHYLQDHEKKLRLVFKSLDKKNDGRIDAQEI 103
Cdd:cd16182  20 ELQKLLNaslLKDMPKFDGFSleTCRS----LIALMDTNGSGRLDLEEF-KTLWSDLKKWQAIFKKFDTDRSGTLSSYEL 94

                        90       100       110
                ....*....|....*....|....*....|...
gi 56699401 104 MQSLRDLGVKISEQQAEKI-LKSMDKNGTMTID 135
Cdd:cd16182  95 RKALESAGFHLSNKVLQALvLRYADSTGRITFE 127
ELC_N cd22949
N-terminal domain of Myosin essential light chain ELC; ELC is part of the apicomplexan ...
 80-152 6.53e-04

N-terminal domain of Myosin essential light chain ELC; ELC is part of the apicomplexan membrane-associated protein complex called the glideosome, which is essential for parasite motility. The glideosome is composed of six proteins: myosin A (MyoA), essential light chain ELC, myosin light chain MLC1 (also called MTIP), and the glideosome-associated proteins GAP40, GAP45, and GAP50. MyoA is a Class XIV myosin implicated in gliding motility, as well as host cell and tissue invasion by parasites. ELC binds to the MyoA neck region adjacent to the MLC1-binding site, and both myosin light chains co-located to the glideosome. Although ELCs bind to a conserved MyoA sequence, P. falciparum ELC adopts a distinct structure in the free and MyoA-bound state. Therefore ELCs enhance MyoA performance by inducing alpha helical structure formation in MyoA and thus stiffening its lever arm. It has been shown that disruption of MyoA, MLC1, or ELC have dramatic effects on parasite motility but do not affect parasite shape or replication. The ELC N-terminal domain is part of the EF-hand calcium binding motif superfamily. Calcium binding has no effect on the structure of ELCs.


Pssm-ID: 439385 [Multi-domain]  Cd Length: 66  Bit Score: 38.10  E-value: 6.53e-04
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 56699401  80 EKKLRLVFKSLDKKNDGRIDAQEIMQSLRDLGVKISEQQAEKIlksmdkngTMTIDWNEWRDYHLLHPVENIP 152
Cdd:cd22949   2 EEKFREAFILFDRDGDGELTMYEAVLAMRSCGIPLTNDEKDAL--------PASMNWDQFENWAKKKLAYSDP 66
PTZ00184 PTZ00184
calmodulin; Provisional
 87-139 8.55e-04

calmodulin; Provisional


Pssm-ID: 185504 [Multi-domain]  Cd Length: 149  Bit Score: 39.74  E-value: 8.55e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 56699401   87 FKSLDKKNDGRIDAQEIMQSLRDLGVKISEQQAEKILKSMDKNGTMTIDWNEW 139
Cdd:PTZ00184  17 FSLFDKDGDGTITTKELGTVMRSLGQNPTEAELQDMINEVDADGNGTIDFPEF 69
EFh cd00051
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal ...
 29-77 1.14e-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: 37.14  E-value: 1.14e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 56699401  29 ELKSIFKL-----SVFIPSQEF-----STYRQWKQKIVQA----GDKDLDGQLDFEEFVHYLQ 77
Cdd:cd00051   1 ELREAFRLfdkdgDGTISADELkaalkSLGEGLSEEEIDEmireVDKDGDGKIDFEEFLELMA 63
EFh_HEF cd15902
EF-hand, calcium binding motif, found in the hexa-EF hand proteins family; The hexa-EF hand ...
 20-138 2.33e-03

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: 39.64  E-value: 2.33e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56699401  20 YFESKGLPAELKSIFK--LSVFIPSQEFStyrQWKQKIVQAGDKDLDGQLDFEEFVHYLQDHEKKLRL------------ 85
Cdd:cd15902  15 YIEGKELDSFLRELLKalNGKDKTDDEVA---EKKKEFMEKYDENEDGKIEIRELANILPTEENFLLLfrreqplissve 91

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 56699401  86 ---VFKSLDKKNDGRIDAQEIMQSLRDL----GVKISEQQAEK----ILKSMDKNGTMTIDWNE 138
Cdd:cd15902  92 fmkIWRKYDTDGSGFIEAKELKGFLKDLllknKKHVSPPKLDEytklILKEFDANKDGKLELDE 155
EFh_PEF_CalpA_B cd16196
Penta-EF hand, calcium binding motifs, found in Drosophila melanogaster calpain-A (CalpA), ...
 60-115 2.83e-03

Penta-EF hand, calcium binding motifs, found in Drosophila melanogaster calpain-A (CalpA), calpain-B (CalpB), and similar proteins; The family contains two calpains that have been found in Drosophila, CalpA and CalpB. CalpA, also termed calcium-activated neutral proteinase A (CANP A), or calpain-A catalytic subunit, is a Drosophila calpain homolog specifically expressed in a few neurons in the central nervous system, in scattered endocrine cells in the midgut, and in blood cells. CalpB, also termed calcium-activated neutral proteinase B (CANP B), contains calpain-B catalytic subunit 1 and calpain-B catalytic subunit 2. Both CalpA and CalpB are closely related to that of vertebrate calpains, and they share similar domain architecture, which consists of four domains: the N-terminal domain I, the catalytic domain II carrying the three active site residues, Cys, His and Asn, the Ca2+-regulated phospholipid-binding domain III, and penta-EF-hand Ca2+-binding domain IV. Besides, CalpA and CalpB display some distinguishing structural features that are not found in mammalian typical calpains. CalpA harbors a 76 amino acid long hydrophobic stretch inserted in domain IV, which may be involved in membrane attachment of this enzyme. CalpB has an unusually long N-terminal tail of 224 amino acids, which belongs to the class of intrinsically unstructured proteins (IUP) and may become ordered upon binding to target protein(s). Moreover, they do not need small regulatory subunits for their catalytic activity, and their proteolytic function is not regulated by an intrinsic inhibitor as the Drosophila genome contains neither regulatory subunit nor calpastatin orthologs. As a result, they may exist as a monomer or perhaps as a homo- or heterodimer together with a second large subunit. Furthermore, both CalpA and CalpB are dispensable for viability and fertility and do not share vital functions during Drosophila development. Phosphatidylinositol 4,5-diphosphate, phosphatidylinositol 4-monophosphate, phosphatidylinositol, and phosphatidic acid can stimulate the activity and the rate of activation of CalpA, but not CalpB. Calpain A modulates Toll responses by limited Cactus/IkappaB proteolysis. CalpB directly interacts with talin, an important component of the focal adhesion complex, and functions as an important modulator in border cell migration within egg chambers, which may act via the digestion of talin. CalpB can be phosphorylated by cAMP-dependent protein kinase (protein kinase A, PKA; EC 2.7.11.11) at Ser240 and Ser845, as well as by mitogen-activated protein kinase (ERK1 and ERK2; EC 2.7.11.24) at Thr747. The activation of the ERK pathway by extracellular signals results in the phosphorylation and activation of calpain B. In Schneider cells (S2), calpain B was mainly in the cytoplasm and upon a rise in Ca2+ the enzyme adhered to intracellular membranes.


Pssm-ID: 320071 [Multi-domain]  Cd Length: 167  Bit Score: 38.34  E-value: 2.83e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 56699401  60 DKDLDGQLDFEEFVHYLQDhekkLRL---VFKSLDKKNDGRIDAQEIMQSLRDLGVKIS 115
Cdd:cd16196  51 DVDRSGKLGFEEFKKLWED----LRSwkrVFKLFDTDGSGSFSSFELRNALNSAGFRLS 105
EFh_PI-PLCeta cd16205
EF-hand motif found in phosphoinositide phospholipase C eta (PI-PLC-eta); PI-PLC-eta isozymes ...
 83-135 3.30e-03

EF-hand motif found in phosphoinositide phospholipase C eta (PI-PLC-eta); PI-PLC-eta isozymes represent a class of neuron-specific metazoan PI-PLCs that are most abundant in the brain, particularly in the hippocampus, habenula, olfactory bulb, cerebellum, and throughout the cerebral cortex. They are phosphatidylinositol 4,5-bisphosphate-hydrolyzing enzymes that are more sensitive to Ca2+ than other PI-PLC isozymes. They function as calcium sensors activated by small increases in intracellular calcium concentrations. They are also activated through G-protein-coupled receptor (GPCR) stimulation, and further mediate GPCR signalling pathways. PI-PLC-eta isozymes contain an N-terminal pleckstrin homology (PH) domain, four atypical EF-hand motifs, a PLC catalytic core domain, a C2 domain, and a unique C-terminal tail that terminates with a PDZ-binding motif, a potential interaction site for other signaling proteins. The PLC catalytic core domain is a TIM barrel with two highly conserved regions (X and Y) split by a highly degenerate linker sequence. The C-terminal tail harbors a number of proline-rich motifs which may interact with SH3 (Src homology 3) domain-containing proteins, as well as many serine/threonine residues, suggesting possible regulation of interactions by protein kinases/phosphatases. There are two PI-PLC-eta isozymes (1-2). Aside from the PI-PLC-eta isozymes identified in mammals, their eukaryotic homologs are also present in this family.


Pssm-ID: 320035 [Multi-domain]  Cd Length: 141  Bit Score: 37.75  E-value: 3.30e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 56699401  83 LRLVFKSLDKKNDGRIDAQEIMQSLRDLGVKISEQQAEKILKSMD---KNGTMTID 135
Cdd:cd16205   2 LKQTFEEADKNGDGLLSIGEILQLMHKLNVNLPRRKVRQMFKEADtddNQGTLDFE 57
EFh_PI-PLCdelta cd16202
EF-hand motif found in phosphoinositide phospholipase C delta (PI-PLC-delta); PI-PLC-delta ...
 57-110 3.76e-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: 37.59  E-value: 3.76e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 56699401  57 QAGDKDLDGQLDFEEFVHYLQD-----HEKKLRLVFKSLDKKNDGRIDAQEIMQSLRDL 110
Cdd:cd16202   7 RKADKNGDGKLSFKECKKLLKKlnvkvDKDYAKKLFQEADTSGEDVLDEEEFVQFYNRL 65
EFh_PI-PLCdelta1 cd16217
EF-hand motif found in phosphoinositide phospholipase C delta 1 (PI-PLC-delta1); PI-PLC-delta1, ...
 51-135 5.32e-03

EF-hand motif found in phosphoinositide phospholipase C delta 1 (PI-PLC-delta1); PI-PLC-delta1, also termed 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase delta-1 (PLCD1), or phospholipase C-III (PLC-III), or phospholipase C-delta-1 (PLC-delta-1), is present in high abundancy in the brain, heart, lung, skeletal muscle and testis. It is activated by high calcium levels generated by other PI-PLC family members, and therefore functions as a calcium amplifier within the cell. PI-PLC-delta1 is required for maintenance of homeostasis in skin and metabolic tissues. Moreover, it is essential in trophoblasts for placental development. Simultaneous loss of PI-PLC-delta1 may cause placental vascular defects, leading to embryonic lethality. PI-PLC-delta1 can be positively or negatively regulated by several binding partners, including p122/Rho GTPase activating protein (RhoGAP), Gha/Transglutaminase II, RalA, and calmodulin. It is involved in Alzheimer's disease and hypertension. Furthermore, PI-PLC-delta1 regulates cell proliferation and cell-cycle progression from G1- to S-phase by control of cyclin E-CDK2 activity and p27 levels. It can be activated by alpha1-adrenoreceptors (AR) in a calcium-dependent manner and may be important for G protein-coupled receptors (GPCR) responses in vascular smooth muscle (VSM). PI-PLC-delta1 may also be involved in noradrenaline (NA)-induced phosphatidylinositol-4,5-bisphosphate (PIP2) hydrolysis and modulate sustained contraction of mesenteric small arteries. In addition, it inhibits thermogenesis and induces lipid accumulation, and therefore contributes to the development of obesity. PI-PLC-delta1 contains 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. PI-PLC-delta1 can regulate the binding of PH domain to PIP2 in a Ca2+-dependent manner through its functionally important EF-hand domains. In addition, PI-PLC-delta1 possesses a classical leucine-rich nuclear export sequence (NES) located in the EF hand motifs, as well as a nuclear localization signal within its linker region, both of which may be responsible for translocating PI-PLC-delta1 into and out of the cell nucleus.


Pssm-ID: 320047 [Multi-domain]  Cd Length: 139  Bit Score: 37.41  E-value: 5.32e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56699401  51 WKQKIVQAGDKDLDGQLDFEEFVHYLQD-----HEKKLRLVFKSLDKKNDGRIDAQEImqslrDLGVKISEQQAE--KIL 123
Cdd:cd16217   1 WIHSCLRKADKNKDNKMSFKELKDFLKEinievDDDYAEKLFKECDKSKSGFLEGEEI-----EEFYKLLTKREEidVIF 75

                        90
                ....*....|...
gi 56699401 124 -KSMDKNGTMTID 135
Cdd:cd16217  76 gEYAKSDGTMSRN 88
EFh_PEF_CAPN3 cd16190
Calcium-activated neutral; CAPN3, also termed calcium-activated neutral proteinase 3 (CANP 3), ...
 60-139 5.90e-03

Calcium-activated neutral; CAPN3, also termed calcium-activated neutral proteinase 3 (CANP 3), or calpain L3, or calpain p94, or muscle-specific calcium-activated neutral protease 3, or new calpain 1 (nCL-1), is a calpain large subunit that is mainly expressed in skeletal muscle, or lens. The skeletal muscle-specific CAPN3 are pathologically associated with limb girdle muscular dystrophy type 2A (LGMD2A). Its autolytic activity can be positively regulated by calmodulin (CaM), a known transducer of the calcium signal. CAPN3 is also involved in human melanoma tumorigenesis and progression. It impairs cell proliferation and stimulates oxidative stress-mediated cell death in melanoma cells. Moreover, it plays an important role in sarcomere remodeling and mitochondrial protein turnover. Furthermore, the phosphorylated skeletal muscle-specific CAPN3 acts as a myofibril structural component and may participate in myofibril-based signaling pathways. In the eye, the lens-specific CAPN3, together with CAPN2, is responsible for proteolytic cleavages of alpha and beta-crystallin. Overactivated alpha and beta-crystallin can lead to cataract formation. CAPN3 exists as a homodimer, rather than a heterodimer with the calpain small subunit. It may also form heterodimers with other calpain large subunits. CAPN3 contains a long N-terminal region, 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. Ca2+ binding at EF5 of the CAPN3 PEF domain is a distinct feature not observed in other calpain isoforms.


Pssm-ID: 320065 [Multi-domain]  Cd Length: 169  Bit Score: 37.53  E-value: 5.90e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56699401  60 DKDLDGQLDFEEFVHyLQDHEKKLRLVFKSLDKKNDGRIDAQEIMQSLRDLGVKISEQQAEKI-LKSMDKNgtMTIDWNE 138
Cdd:cd16190  53 DTDGSGKLNLQEFRH-LWNKIKQWQKIFKRYDTDKSGTINSYEMRNAVNDAGFRLNNQLYDIItMRYADKH--MNIDFDS 129


                .
gi 56699401 139 W 139
Cdd:cd16190 130 F 130
EFh_PI-PLCdelta3 cd16218
EF-hand motif found in phosphoinositide phospholipase C delta 3 (PI-PLC-delta3); PI-PLC-delta3, ...
 51-110 6.44e-03

EF-hand motif found in phosphoinositide phospholipase C delta 3 (PI-PLC-delta3); PI-PLC-delta3, also termed 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase delta-3 (PLCD3), phospholipase C-delta-3 (PLC-delta-3), is expressed abundantly in brain, skeletal muscle and heart. PI-PLC-delta3 gene expression is down-regulation by cAMP and calcium. PI-PLC-delta3 acts as anchoring of myosin VI on plasma membrane, and further modulates Myosin IV expression and microvilli formation in enterocytes. It negatively regulates RhoA expression, inhibits RhoA/Rho kinase signaling, and plays an essential role in normal neuronal migration by promoting neuronal outgrowth in the developing brain. Moreover, PI-PLC-delta3 is essential in trophoblasts for placental development. Simultaneous loss of PI-PLC-delta3 may cause placental vascular defects, leading to embryonic lethality. PI-PLC-delta3 contains 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. In addition, PI-PLC-delta3 possesses a classical leucine-rich nuclear export sequence (NES) located in the EF hand motifs, which may be responsible transporting PI-PLC-delta3 from the cell nucleus.


Pssm-ID: 320048 [Multi-domain]  Cd Length: 138  Bit Score: 37.03  E-value: 6.44e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 56699401  51 WKQKIVQAGDKDLDGQLDFEEFVHYLQD-----HEKKLRLVFKSLDKKNDGRIDAQEIMQSLRDL 110
Cdd:cd16218   1 WIHEYLRRADLNKDGKMSFEEIKDLLQMinidlNEQYAYQLFKECDRSNDDRLEEHEIEEFCRRL 65
EFh_HEF cd15902
EF-hand, calcium binding motif, found in the hexa-EF hand proteins family; The hexa-EF hand ...
 28-142 6.90e-03

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: 38.10  E-value: 6.90e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56699401  28 AELKSIFK--LSVFIPSQEFSTYRQWKQKIVQAGDKDLDGQLDFEEFVHYLQDHE----------------KKLRLVFKS 89
Cdd:cd15902 110 KELKGFLKdlLLKNKKHVSPPKLDEYTKLILKEFDANKDGKLELDEMAKLLPVQEnfllkfqilgamdltkEDFEKVFEH 189

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 56699401  90 LDKKNDGRIDAQEIMQSLRDLGVK----ISEQQAEK----ILKSMDKNGTMTIDWNEWRDY 142
Cdd:cd15902 190 YDKDNNGVIEGNELDALLKDLLEKnkadIDKPDLENfrdaILRACDKNKDGKIQKTELALF 250
 
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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