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Conserved domains on  [gi|21361103|ref|NP_003696|]
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electrogenic aspartate/glutamate antiporter SLC25A12, mitochondrial [Homo sapiens]

Protein Classification

calcium-binding mitochondrial carrier protein( domain architecture ID 12145393)

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
Mito_carr pfam00153
Mitochondrial carrier protein;
514-609 3.23e-29

Mitochondrial carrier protein;


:

Pssm-ID: 395101 [Multi-domain]  Cd Length: 96  Bit Score: 111.21  E-value: 3.23e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361103   514 GHVGGLNLLAAGAMAGVPAASLVTPADVIKTRLQVAARAGQTTYSGVIDCFRKILREEGPSAFWKGTAARVFRSSPQFGV 593
Cdd:pfam00153   1 SELSFLASLLAGGIAGAIAVTVTYPLDVVKTRLQVQGGSGKSKGRGILDCFKKIYKEEGIRGLYKGLLPNLLRVAPAAAI 80

                          90
                  ....*....|....*.
gi 21361103   594 TLVTYELLQRWFYIDF 609
Cdd:pfam00153  81 YFGTYETLKRLLLKKL 96
Mito_carr pfam00153
Mitochondrial carrier protein;
327-420 4.36e-27

Mitochondrial carrier protein;


:

Pssm-ID: 395101 [Multi-domain]  Cd Length: 96  Bit Score: 105.43  E-value: 4.36e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361103   327 AYRFTLGSVAGAVGATAVYPIDLVKTRMQNQRGSGSVVGELMyknsFDCFKKVLRYEGFFGLYRGLIPQLIGVAPEKAIK 406
Cdd:pfam00153   6 LASLLAGGIAGAIAVTVTYPLDVVKTRLQVQGGSGKSKGRGI----LDCFKKIYKEEGIRGLYKGLLPNLLRVAPAAAIY 81

                          90
                  ....*....|....
gi 21361103   407 LTVNDFVRDKFTRR 420
Cdd:pfam00153  82 FGTYETLKRLLLKK 95
Mito_carr pfam00153
Mitochondrial carrier protein;
422-513 2.26e-20

Mitochondrial carrier protein;


:

Pssm-ID: 395101 [Multi-domain]  Cd Length: 96  Bit Score: 86.17  E-value: 2.26e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361103   422 GSVPLPAEVLAGGCAGGSQVIFTNPLEIVKIRLQVAGEITTGPRVSALNVLRDL----GIFGLYKGAKACFLRDIPFSAI 497
Cdd:pfam00153   1 SELSFLASLLAGGIAGAIAVTVTYPLDVVKTRLQVQGGSGKSKGRGILDCFKKIykeeGIRGLYKGLLPNLLRVAPAAAI 80

                          90
                  ....*....|....*.
gi 21361103   498 YFPVYAHCKLLLADEN 513
Cdd:pfam00153  81 YFGTYETLKRLLLKKL 96
EFh_MICU super family cl28896
EF-hand, calcium binding motif, found in mitochondrial calcium uptake proteins MICU1, MICU2, ...
 91-160 5.22e-06

EF-hand, calcium binding motif, found in mitochondrial calcium uptake proteins MICU1, MICU2, MICU3, and similar proteins; This family includes mitochondrial calcium uptake protein MICU1 and its two additional paralogs, MICU2 and MICU3. MICU1 localizes to the inner mitochondrial membrane (IMM). It functions as a gatekeeper of the mitochondrial calcium uniporter (MCU) and regulates MCU-mediated mitochondrial Ca2+ uptake, which is essential for maintaining mitochondrial homoeostasis. MICU1 and MICU2 are physically associated within the uniporter complex and are co-expressed across all tissues. They may play non-redundant roles in the regulation of the mitochondrial calcium uniporter. At present, the precise molecular function of MICU2 and MICU3 remain unclear. MICU2 may play possible roles in Ca2+ sensing and regulation of MCU, calcium buffering with a secondary impact on transport or assembly and stabilization of MCU. MICU3 likely has a role in mitochondrial calcium handling. All members in this family contains an N-terminal mitochondrial targeting sequence (MTS) as well as two evolutionarily conserved canonical Ca2+-binding EF-hands separated by a long stretch of residues predicted to form alpha-helices.


The actual alignment was detected with superfamily member cd15900:

Pssm-ID: 333716 [Multi-domain]  Cd Length: 152  Bit Score: 46.84  E-value: 5.22e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361103  91 FIVAFQLFDKSGNGEVT---FENVKEIF------GQTIIHHHIPFNWDCE----FIRLHFGHNRKKHLNYTEFTQFLQEL 157
Cdd:cd15900   2 FEIAFKMFDLDGDGELDkeeFNKVQSIIrsqtsvGQRHRDHTNGESTKLGmnstLARYFFGKDGKQKLSIEKFLEFQENL 81


                ...
gi 21361103 158 QLE 160
Cdd:cd15900  82 QEE 84
FRQ1 super family cl34916
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
12-125 1.43e-05

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


The actual alignment was detected with superfamily member COG5126:

Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 45.17  E-value: 1.43e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361103  12 DPHELRNIFLQYAST-----EVDGERYMTPEDFVQryLGLYNDPNSNPKIVQLLAGVADQTKDGLISYQEFLAFESVLCA 86
Cdd:COG5126  23 ERDDFEALFRRLWATlfseaDTDGDGRISREEFVA--GMESLFEATVEPFARAAFDLLDTDGDGKISADEFRRLLTALGV 100

                        90       100       110
                ....*....|....*....|....*....|....*....
gi 21361103  87 PDSMFIVAFQLFDKSGNGEVTFEnvkEiFGQTIIHHHIP 125
Cdd:COG5126 101 SEEEADELFARLDTDGDGKISFE---E-FVAAVRDYYTP 135
 
Name Accession Description Interval E-value
Mito_carr pfam00153
Mitochondrial carrier protein;
514-609 3.23e-29

Mitochondrial carrier protein;


Pssm-ID: 395101 [Multi-domain]  Cd Length: 96  Bit Score: 111.21  E-value: 3.23e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361103   514 GHVGGLNLLAAGAMAGVPAASLVTPADVIKTRLQVAARAGQTTYSGVIDCFRKILREEGPSAFWKGTAARVFRSSPQFGV 593
Cdd:pfam00153   1 SELSFLASLLAGGIAGAIAVTVTYPLDVVKTRLQVQGGSGKSKGRGILDCFKKIYKEEGIRGLYKGLLPNLLRVAPAAAI 80

                          90
                  ....*....|....*.
gi 21361103   594 TLVTYELLQRWFYIDF 609
Cdd:pfam00153  81 YFGTYETLKRLLLKKL 96
Mito_carr pfam00153
Mitochondrial carrier protein;
327-420 4.36e-27

Mitochondrial carrier protein;


Pssm-ID: 395101 [Multi-domain]  Cd Length: 96  Bit Score: 105.43  E-value: 4.36e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361103   327 AYRFTLGSVAGAVGATAVYPIDLVKTRMQNQRGSGSVVGELMyknsFDCFKKVLRYEGFFGLYRGLIPQLIGVAPEKAIK 406
Cdd:pfam00153   6 LASLLAGGIAGAIAVTVTYPLDVVKTRLQVQGGSGKSKGRGI----LDCFKKIYKEEGIRGLYKGLLPNLLRVAPAAAIY 81

                          90
                  ....*....|....
gi 21361103   407 LTVNDFVRDKFTRR 420
Cdd:pfam00153  82 FGTYETLKRLLLKK 95
PTZ00169 PTZ00169
ADP/ATP transporter on adenylate translocase; Provisional
 330-603 2.99e-26

ADP/ATP transporter on adenylate translocase; Provisional


Pssm-ID: 240302 [Multi-domain]  Cd Length: 300  Bit Score: 109.47  E-value: 2.99e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361103  330 FTLGSVAGAVGATAVYPIDLVKTRMQNQRGSGSVVGELM--YKNSFDCFKKVLRYEGFFGLYRGLIPQLIGVAPEKAIKL 407
Cdd:PTZ00169  11 FLMGGISAAISKTAVAPIERVKMLIQTQDSIPEIKSGKVprYSGIVNCFRRVSKEQGVLSLWRGNTANVIRYFPTQAFNF 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361103  408 TVNDFVRDKFTRRDGSVPL----PAEVLAGGCAGGSQVIFTNPLEIVKIRLqvAGEIT-------TGPRVSALNVLRDLG 476
Cdd:PTZ00169  91 AFKDYFKNMFPKYNQKTDFwkffGVNILSGGLAGASSLLIVYPLDFARTRL--ASDIGkggdrefTGLFDCLMKISKQTG 168

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361103  477 IFGLYKGAKACFLRDIPFSAIYFPVYAHCKLLLADENGHVgglNLLAAGAMAG--VPAASLVT-PADVIKTRLQVAA--- 550
Cdd:PTZ00169 169 FLSLYQGFGVSVQGIIVYRGAYFGLYDSAKALLFGNDKNT---NILYKWAVAQtvTILAGLISyPFDTVRRRMMMMSgrk 245

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|...
gi 21361103  551 RAGQTTYSGVIDCFRKILREEGPSAFWKGTAARVFRSSPQfGVTLVTYELLQR 603
Cdd:PTZ00169 246 AKSEIQYTGTLDCWKKILKNEGLGGFFKGAWANVLRGAGG-ALVLVFYDELQK 297
Mito_carr pfam00153
Mitochondrial carrier protein;
422-513 2.26e-20

Mitochondrial carrier protein;


Pssm-ID: 395101 [Multi-domain]  Cd Length: 96  Bit Score: 86.17  E-value: 2.26e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361103   422 GSVPLPAEVLAGGCAGGSQVIFTNPLEIVKIRLQVAGEITTGPRVSALNVLRDL----GIFGLYKGAKACFLRDIPFSAI 497
Cdd:pfam00153   1 SELSFLASLLAGGIAGAIAVTVTYPLDVVKTRLQVQGGSGKSKGRGILDCFKKIykeeGIRGLYKGLLPNLLRVAPAAAI 80

                          90
                  ....*....|....*.
gi 21361103   498 YFPVYAHCKLLLADEN 513
Cdd:pfam00153  81 YFGTYETLKRLLLKKL 96
EFh_MICU cd15900
EF-hand, calcium binding motif, found in mitochondrial calcium uptake proteins MICU1, MICU2, ...
 91-160 5.22e-06

EF-hand, calcium binding motif, found in mitochondrial calcium uptake proteins MICU1, MICU2, MICU3, and similar proteins; This family includes mitochondrial calcium uptake protein MICU1 and its two additional paralogs, MICU2 and MICU3. MICU1 localizes to the inner mitochondrial membrane (IMM). It functions as a gatekeeper of the mitochondrial calcium uniporter (MCU) and regulates MCU-mediated mitochondrial Ca2+ uptake, which is essential for maintaining mitochondrial homoeostasis. MICU1 and MICU2 are physically associated within the uniporter complex and are co-expressed across all tissues. They may play non-redundant roles in the regulation of the mitochondrial calcium uniporter. At present, the precise molecular function of MICU2 and MICU3 remain unclear. MICU2 may play possible roles in Ca2+ sensing and regulation of MCU, calcium buffering with a secondary impact on transport or assembly and stabilization of MCU. MICU3 likely has a role in mitochondrial calcium handling. All members in this family contains an N-terminal mitochondrial targeting sequence (MTS) as well as two evolutionarily conserved canonical Ca2+-binding EF-hands separated by a long stretch of residues predicted to form alpha-helices.


Pssm-ID: 320080 [Multi-domain]  Cd Length: 152  Bit Score: 46.84  E-value: 5.22e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361103  91 FIVAFQLFDKSGNGEVT---FENVKEIF------GQTIIHHHIPFNWDCE----FIRLHFGHNRKKHLNYTEFTQFLQEL 157
Cdd:cd15900   2 FEIAFKMFDLDGDGELDkeeFNKVQSIIrsqtsvGQRHRDHTNGESTKLGmnstLARYFFGKDGKQKLSIEKFLEFQENL 81


                ...
gi 21361103 158 QLE 160
Cdd:cd15900  82 QEE 84
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
12-125 1.43e-05

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


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 45.17  E-value: 1.43e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361103  12 DPHELRNIFLQYAST-----EVDGERYMTPEDFVQryLGLYNDPNSNPKIVQLLAGVADQTKDGLISYQEFLAFESVLCA 86
Cdd:COG5126  23 ERDDFEALFRRLWATlfseaDTDGDGRISREEFVA--GMESLFEATVEPFARAAFDLLDTDGDGKISADEFRRLLTALGV 100

                        90       100       110
                ....*....|....*....|....*....|....*....
gi 21361103  87 PDSMFIVAFQLFDKSGNGEVTFEnvkEiFGQTIIHHHIP 125
Cdd:COG5126 101 SEEEADELFARLDTDGDGKISFE---E-FVAAVRDYYTP 135
EF-hand_7 pfam13499
EF-hand domain pair;
15-80 5.11e-04

EF-hand domain pair;


Pssm-ID: 463900 [Multi-domain]  Cd Length: 67  Bit Score: 38.77  E-value: 5.11e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 21361103    15 ELRNIFLQYastEVDGERYMTPEDFVQRYLGLYNDPNSNPKIVQLLAGVADQTKDGLISYQEFLAF 80
Cdd:pfam13499   3 KLKEAFKLL---DSDGDGYLDVEELKKLLRKLEEGEPLSDEEVEELFKEFDLDKDGRISFEEFLEL 65
PTZ00183 PTZ00183
centrin; Provisional
 14-119 2.67e-03

centrin; Provisional


Pssm-ID: 185503 [Multi-domain]  Cd Length: 158  Bit Score: 38.90  E-value: 2.67e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361103   14 HELRNIFLQYastEVDGERYMTPEDF--VQRYLGLynDPNsNPKIVQLLAGVaDQTKDGLISYQEFLAFESVLCA---PD 88
Cdd:PTZ00183  17 KEIREAFDLF---DTDGSGTIDPKELkvAMRSLGF--EPK-KEEIKQMIADV-DKDGSGKIDFEEFLDIMTKKLGerdPR 89

                         90       100       110
                 ....*....|....*....|....*....|....
gi 21361103   89 SMFIVAFQLFDKSGNGEVTFENVKEI---FGQTI 119
Cdd:PTZ00183  90 EEILKAFRLFDDDKTGKISLKNLKRVakeLGETI 123
 
Name Accession Description Interval E-value
Mito_carr pfam00153
Mitochondrial carrier protein;
514-609 3.23e-29

Mitochondrial carrier protein;


Pssm-ID: 395101 [Multi-domain]  Cd Length: 96  Bit Score: 111.21  E-value: 3.23e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361103   514 GHVGGLNLLAAGAMAGVPAASLVTPADVIKTRLQVAARAGQTTYSGVIDCFRKILREEGPSAFWKGTAARVFRSSPQFGV 593
Cdd:pfam00153   1 SELSFLASLLAGGIAGAIAVTVTYPLDVVKTRLQVQGGSGKSKGRGILDCFKKIYKEEGIRGLYKGLLPNLLRVAPAAAI 80

                          90
                  ....*....|....*.
gi 21361103   594 TLVTYELLQRWFYIDF 609
Cdd:pfam00153  81 YFGTYETLKRLLLKKL 96
Mito_carr pfam00153
Mitochondrial carrier protein;
327-420 4.36e-27

Mitochondrial carrier protein;


Pssm-ID: 395101 [Multi-domain]  Cd Length: 96  Bit Score: 105.43  E-value: 4.36e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361103   327 AYRFTLGSVAGAVGATAVYPIDLVKTRMQNQRGSGSVVGELMyknsFDCFKKVLRYEGFFGLYRGLIPQLIGVAPEKAIK 406
Cdd:pfam00153   6 LASLLAGGIAGAIAVTVTYPLDVVKTRLQVQGGSGKSKGRGI----LDCFKKIYKEEGIRGLYKGLLPNLLRVAPAAAIY 81

                          90
                  ....*....|....
gi 21361103   407 LTVNDFVRDKFTRR 420
Cdd:pfam00153  82 FGTYETLKRLLLKK 95
PTZ00169 PTZ00169
ADP/ATP transporter on adenylate translocase; Provisional
 330-603 2.99e-26

ADP/ATP transporter on adenylate translocase; Provisional


Pssm-ID: 240302 [Multi-domain]  Cd Length: 300  Bit Score: 109.47  E-value: 2.99e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361103  330 FTLGSVAGAVGATAVYPIDLVKTRMQNQRGSGSVVGELM--YKNSFDCFKKVLRYEGFFGLYRGLIPQLIGVAPEKAIKL 407
Cdd:PTZ00169  11 FLMGGISAAISKTAVAPIERVKMLIQTQDSIPEIKSGKVprYSGIVNCFRRVSKEQGVLSLWRGNTANVIRYFPTQAFNF 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361103  408 TVNDFVRDKFTRRDGSVPL----PAEVLAGGCAGGSQVIFTNPLEIVKIRLqvAGEIT-------TGPRVSALNVLRDLG 476
Cdd:PTZ00169  91 AFKDYFKNMFPKYNQKTDFwkffGVNILSGGLAGASSLLIVYPLDFARTRL--ASDIGkggdrefTGLFDCLMKISKQTG 168

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361103  477 IFGLYKGAKACFLRDIPFSAIYFPVYAHCKLLLADENGHVgglNLLAAGAMAG--VPAASLVT-PADVIKTRLQVAA--- 550
Cdd:PTZ00169 169 FLSLYQGFGVSVQGIIVYRGAYFGLYDSAKALLFGNDKNT---NILYKWAVAQtvTILAGLISyPFDTVRRRMMMMSgrk 245

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|...
gi 21361103  551 RAGQTTYSGVIDCFRKILREEGPSAFWKGTAARVFRSSPQfGVTLVTYELLQR 603
Cdd:PTZ00169 246 AKSEIQYTGTLDCWKKILKNEGLGGFFKGAWANVLRGAGG-ALVLVFYDELQK 297
Mito_carr pfam00153
Mitochondrial carrier protein;
422-513 2.26e-20

Mitochondrial carrier protein;


Pssm-ID: 395101 [Multi-domain]  Cd Length: 96  Bit Score: 86.17  E-value: 2.26e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361103   422 GSVPLPAEVLAGGCAGGSQVIFTNPLEIVKIRLQVAGEITTGPRVSALNVLRDL----GIFGLYKGAKACFLRDIPFSAI 497
Cdd:pfam00153   1 SELSFLASLLAGGIAGAIAVTVTYPLDVVKTRLQVQGGSGKSKGRGILDCFKKIykeeGIRGLYKGLLPNLLRVAPAAAI 80

                          90
                  ....*....|....*.
gi 21361103   498 YFPVYAHCKLLLADEN 513
Cdd:pfam00153  81 YFGTYETLKRLLLKKL 96
PTZ00168 PTZ00168
mitochondrial carrier protein; Provisional
 325-612 2.11e-12

mitochondrial carrier protein; Provisional


Pssm-ID: 185494 [Multi-domain]  Cd Length: 259  Bit Score: 67.64  E-value: 2.11e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361103  325 ESAYRFTLGSVAGAVGATAVYPIDLVKTRMQNQRGSgsvvgelmyknSFDCFKKvlryegffgLYRGLIPQLIGVAPEKA 404
Cdd:PTZ00168   2 EHFHNLVTGALSGVIVDAVLYPIDSIKTNIQAKKSF-----------SFSDIKK---------LYSGILPTLVGTVPASA 61

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361103  405 IKLTVNDFVRDKFTRRDGSVPLPAEVL-AGGCAGGSQVIFTNPLEIVKIRLQVAGEITTGPRVSALNVLRDLGIFgLYKG 483
Cdd:PTZ00168  62 FFYCFYELSKKLLTEYRENISKTNLYLiSTSIAEITACIVRLPFEIVKQNMQVSGNISVLKTIYEITQREGLPSF-LGKS 140

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361103  484 AKACFLRDIPFSAIYFPVYAHCKLLLADENGHVG----GLNLLAAGAMAGVPAASLVTPADVIKTRlqvaaragQTTY-S 558
Cdd:PTZ00168 141 YFVMIVREIPFDCIQYFLWETLKEKAKKDFGKFSkkypSITSAICGGLAGGIAGFLTTPVDVIKSR--------QIIYgK 212

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....
gi 21361103  559 GVIDCFRKIlREEGPSAFWKGTAarvFRSSpqfgvtlvtyellqrwfYIDFGGL 612
Cdd:PTZ00168 213 SYIETVTEI-AEEGYLTFYKGCC---FRSS-----------------YLFFGGL 245
EFh_MICU cd15900
EF-hand, calcium binding motif, found in mitochondrial calcium uptake proteins MICU1, MICU2, ...
 91-160 5.22e-06

EF-hand, calcium binding motif, found in mitochondrial calcium uptake proteins MICU1, MICU2, MICU3, and similar proteins; This family includes mitochondrial calcium uptake protein MICU1 and its two additional paralogs, MICU2 and MICU3. MICU1 localizes to the inner mitochondrial membrane (IMM). It functions as a gatekeeper of the mitochondrial calcium uniporter (MCU) and regulates MCU-mediated mitochondrial Ca2+ uptake, which is essential for maintaining mitochondrial homoeostasis. MICU1 and MICU2 are physically associated within the uniporter complex and are co-expressed across all tissues. They may play non-redundant roles in the regulation of the mitochondrial calcium uniporter. At present, the precise molecular function of MICU2 and MICU3 remain unclear. MICU2 may play possible roles in Ca2+ sensing and regulation of MCU, calcium buffering with a secondary impact on transport or assembly and stabilization of MCU. MICU3 likely has a role in mitochondrial calcium handling. All members in this family contains an N-terminal mitochondrial targeting sequence (MTS) as well as two evolutionarily conserved canonical Ca2+-binding EF-hands separated by a long stretch of residues predicted to form alpha-helices.


Pssm-ID: 320080 [Multi-domain]  Cd Length: 152  Bit Score: 46.84  E-value: 5.22e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361103  91 FIVAFQLFDKSGNGEVT---FENVKEIF------GQTIIHHHIPFNWDCE----FIRLHFGHNRKKHLNYTEFTQFLQEL 157
Cdd:cd15900   2 FEIAFKMFDLDGDGELDkeeFNKVQSIIrsqtsvGQRHRDHTNGESTKLGmnstLARYFFGKDGKQKLSIEKFLEFQENL 81


                ...
gi 21361103 158 QLE 160
Cdd:cd15900  82 QEE 84
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
12-125 1.43e-05

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


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 45.17  E-value: 1.43e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361103  12 DPHELRNIFLQYAST-----EVDGERYMTPEDFVQryLGLYNDPNSNPKIVQLLAGVADQTKDGLISYQEFLAFESVLCA 86
Cdd:COG5126  23 ERDDFEALFRRLWATlfseaDTDGDGRISREEFVA--GMESLFEATVEPFARAAFDLLDTDGDGKISADEFRRLLTALGV 100

                        90       100       110
                ....*....|....*....|....*....|....*....
gi 21361103  87 PDSMFIVAFQLFDKSGNGEVTFEnvkEiFGQTIIHHHIP 125
Cdd:COG5126 101 SEEEADELFARLDTDGDGKISFE---E-FVAAVRDYYTP 135
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
28-178 4.58e-05

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


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 43.63  E-value: 4.58e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361103  28 VDGERYMTPEDFVQRYLGlyndpnsnpkIVQLLAGVADQTKDGLISYQEFLAFESVLCAPDSMFIV--AFQLFDKSGNGE 105
Cdd:COG5126  16 ADGDGVLERDDFEALFRR----------LWATLFSEADTDGDGRISREEFVAGMESLFEATVEPFAraAFDLLDTDGDGK 85

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 21361103 106 VTFEnvkeifgqtiihhhipfnwdcefirlhfghnrkkhlnytEFTQFLQELQL--EHARQAFALKDKSKSGMIS 178
Cdd:COG5126  86 ISAD---------------------------------------EFRRLLTALGVseEEADELFARLDTDGDGKIS 121
EFh_PI-PLC cd15898
EF-hand motif found in eukaryotic phosphoinositide-specific phospholipase C (PI-PLC, EC 3.1.4. ...
 64-186 6.51e-05

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: 43.43  E-value: 6.51e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361103  64 ADQTKDGLISYQEFLAFESVL--CAPDSMFIVAFQLFDKSGNGEVTFENVKEIFGQTIIHHHIpfnwdcEFIRLHFGHNR 141
Cdd:cd15898   9 ADKDGDGKLSLKEIKKLLKRLniRVSEKELKKLFKEVDTNGDGTLTFDEFEELYKSLTERPEL------EPIFKKYAGTN 82

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|.
gi 21361103 142 KKHLNYTEFTQFLQELQLEHARQAFALK------DKSKSGMISGLDFSDIM 186
Cdd:cd15898  83 RDYMTLEEFIRFLREEQGENVSEEECEEliekyePERENRQLSFEGFTNFL 133
EF-hand_7 pfam13499
EF-hand domain pair;
15-80 5.11e-04

EF-hand domain pair;


Pssm-ID: 463900 [Multi-domain]  Cd Length: 67  Bit Score: 38.77  E-value: 5.11e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 21361103    15 ELRNIFLQYastEVDGERYMTPEDFVQRYLGLYNDPNSNPKIVQLLAGVADQTKDGLISYQEFLAF 80
Cdd:pfam13499   3 KLKEAFKLL---DSDGDGYLDVEELKKLLRKLEEGEPLSDEEVEELFKEFDLDKDGRISFEEFLEL 65
EFh_CREC cd15899
EF-hand, calcium binding motif, found in CREC-EF hand family; The CREC (Cab45/reticulocalbin ...
 63-187 1.22e-03

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


Pssm-ID: 320021 [Multi-domain]  Cd Length: 267  Bit Score: 41.27  E-value: 1.22e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361103  63 VADQTKDGLISYQEFLAFESVLCAPDSMFIV---AFQLFDKSGNGEVTFEnvkEIFGQTiiHHHIPFNWDCEFI---RLH 136
Cdd:cd15899 131 AADQDGDLILTLEEFLAFLHPEESPYMLDFVikeTLEDLDKNGDGFISLE---EFISDP--YSADENEEEPEWVkveKER 205

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 21361103 137 FGHNRKK----HLNYTEFTQFL----QELQLEHARQAFALKDKSKSGMISG---LDFSDIMV 187
Cdd:cd15899 206 FVELRDKdkdgKLDGEELLSWVdpsnQEIALEEAKHLIAESDENKDGKLSPeeiLDNHELFV 267
PTZ00183 PTZ00183
centrin; Provisional
 14-119 2.67e-03

centrin; Provisional


Pssm-ID: 185503 [Multi-domain]  Cd Length: 158  Bit Score: 38.90  E-value: 2.67e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361103   14 HELRNIFLQYastEVDGERYMTPEDF--VQRYLGLynDPNsNPKIVQLLAGVaDQTKDGLISYQEFLAFESVLCA---PD 88
Cdd:PTZ00183  17 KEIREAFDLF---DTDGSGTIDPKELkvAMRSLGF--EPK-KEEIKQMIADV-DKDGSGKIDFEEFLDIMTKKLGerdPR 89

                         90       100       110
                 ....*....|....*....|....*....|....
gi 21361103   89 SMFIVAFQLFDKSGNGEVTFENVKEI---FGQTI 119
Cdd:PTZ00183  90 EEILKAFRLFDDDKTGKISLKNLKRVakeLGETI 123
 
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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