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Conserved domains on  [gi|1133436468|ref|XP_019874459|]
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calcium uptake protein 1 homolog, mitochondrial isoform X3 [Aethina tumida]

Protein Classification

calcium uptake protein( domain architecture ID 11610295)

mitochondrial calcium uptake protein (MICU) may act as a key regulator of mitochondrial calcium uniporter (MCU)

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
EFh_MICU cd15900
EF-hand, calcium binding motif, found in mitochondrial calcium uptake proteins MICU1, MICU2, ...
 235-455 3.77e-74

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: 230.58  E-value: 3.77e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133436468 235 HFEIAFRMFDLNGDGDVDCEEFEKVATLIRQQTSIGSRHRDHANTGNTFKGVNSALTTYFFGPNLKQKLTIEKFLDFQEK 314
Cdd:cd15900     1 HFEIAFKMFDLDGDGELDKEEFNKVQSIIRSQTSVGQRHRDHTNGESTKLGMNSTLARYFFGKDGKQKLSIEKFLEFQEN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133436468 315 LQREilslefqrktpdengniteadftelllayagypqkkkarmlkrvkktfrdhgkgiskedylnffhflnnINDVDTA 394
Cdd:cd15900    81 LQEE---------------------------------------------------------------------IDDVDTA 91

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1133436468 395 LTFYHIAGASIDQPTLKHVAKTVAHVDLSDHVIHVVFTIFDENQDGQLSNKEFIAVMKNRL 455
Cdd:cd15900    92 LTFYHLAGASIDRKTFKRAAKVVAGVELSDHVVDVVFTIFDEDGDGILSHKEFISVMKDRL 152
 
Name Accession Description Interval E-value
EFh_MICU cd15900
EF-hand, calcium binding motif, found in mitochondrial calcium uptake proteins MICU1, MICU2, ...
 235-455 3.77e-74

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: 230.58  E-value: 3.77e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133436468 235 HFEIAFRMFDLNGDGDVDCEEFEKVATLIRQQTSIGSRHRDHANTGNTFKGVNSALTTYFFGPNLKQKLTIEKFLDFQEK 314
Cdd:cd15900     1 HFEIAFKMFDLDGDGELDKEEFNKVQSIIRSQTSVGQRHRDHTNGESTKLGMNSTLARYFFGKDGKQKLSIEKFLEFQEN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133436468 315 LQREilslefqrktpdengniteadftelllayagypqkkkarmlkrvkktfrdhgkgiskedylnffhflnnINDVDTA 394
Cdd:cd15900    81 LQEE---------------------------------------------------------------------IDDVDTA 91

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1133436468 395 LTFYHIAGASIDQPTLKHVAKTVAHVDLSDHVIHVVFTIFDENQDGQLSNKEFIAVMKNRL 455
Cdd:cd15900    92 LTFYHLAGASIDRKTFKRAAKVVAGVELSDHVVDVVFTIFDEDGDGILSHKEFISVMKDRL 152
EF-hand_8 pfam13833
EF-hand domain pair;
402-454 1.30e-05

EF-hand domain pair;


Pssm-ID: 404678 [Multi-domain]  Cd Length: 54  Bit Score: 42.69  E-value: 1.30e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1133436468 402 GASIDQPTLKHVAKTVAHVDLSDHVIHVVFTIFDENQDGQLSNKEFIAVMKNR 454
Cdd:pfam13833   2 KGVITREELKRALALLGLKDLSEDEVDILFREFDTDGDGYISFDEFCVLLERR 54
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
213-256 1.36e-04

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


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 42.09  E-value: 1.36e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 1133436468 213 SSGLITFSDYIFLLTVLSTSRRHFEIAFRMFDLNGDGDVDCEEF 256
Cdd:COG5126    82 GDGKISADEFRRLLTALGVSEEEADELFARLDTDGDGKISFEEF 125
 
Name Accession Description Interval E-value
EFh_MICU cd15900
EF-hand, calcium binding motif, found in mitochondrial calcium uptake proteins MICU1, MICU2, ...
 235-455 3.77e-74

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: 230.58  E-value: 3.77e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133436468 235 HFEIAFRMFDLNGDGDVDCEEFEKVATLIRQQTSIGSRHRDHANTGNTFKGVNSALTTYFFGPNLKQKLTIEKFLDFQEK 314
Cdd:cd15900     1 HFEIAFKMFDLDGDGELDKEEFNKVQSIIRSQTSVGQRHRDHTNGESTKLGMNSTLARYFFGKDGKQKLSIEKFLEFQEN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133436468 315 LQREilslefqrktpdengniteadftelllayagypqkkkarmlkrvkktfrdhgkgiskedylnffhflnnINDVDTA 394
Cdd:cd15900    81 LQEE---------------------------------------------------------------------IDDVDTA 91

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1133436468 395 LTFYHIAGASIDQPTLKHVAKTVAHVDLSDHVIHVVFTIFDENQDGQLSNKEFIAVMKNRL 455
Cdd:cd15900    92 LTFYHLAGASIDRKTFKRAAKVVAGVELSDHVVDVVFTIFDEDGDGILSHKEFISVMKDRL 152
EFh_MICU1 cd16173
EF-hand, calcium binding motif, found in calcium uptake protein 1, mitochondrial (MICU1) and ...
 235-455 4.99e-50

EF-hand, calcium binding motif, found in calcium uptake protein 1, mitochondrial (MICU1) and similar proteins; MICU1, also termed atopy-related autoantigen CALC (ara CALC), or calcium-binding atopy-related autoantigen 1 (CBARA1), or Hom s 4, or EFHA3, 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 its paralog, MICU2, are physically associated within the uniporter complex and are co-expressed across all tissues. They may operate together with MCU to regulate the channel. The mutations in MICU1 are associated with neuromuscular abnormalities in children. MICU1 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: 320081 [Multi-domain]  Cd Length: 153  Bit Score: 167.89  E-value: 4.99e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133436468 235 HFEIAFRMFDLNGDGDVDCEEFEKVATLIRQQTSIGSRHRDHANTGNTFK-GVNSALTTYFFGPNLKQKLTIEKFLDFQE 313
Cdd:cd16173     1 NFEIAFKMFDLNGDGEVDMEEFEQVQSIIRSQTSMGMRHRDRSTTGNTLKtGFSSALTTYFFGADLKGKLTIKNFLEFQR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133436468 314 KLQreilslefqrktpdengniteadftelllayagypqkkkarmlkrvkktfrdhgkgiskedylnffhflNNINDVDT 393
Cdd:cd16173    81 KLQ---------------------------------------------------------------------HDVNDVDT 91

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1133436468 394 ALTFYHIAGASIDQPTLKHVAKTVAHVDLSDHVIHVVFTIFDENQDGQLSNKEFIAVMKNRL 455
Cdd:cd16173    92 ALSFYHMAGASLDKVTMQQVARTVAKVELSDHVCDVVFALFDCDGNGELSNKEFVAIMKQRL 153
EFh_MICU3 cd16175
EF-hand, calcium binding motif, found in calcium uptake protein 3, mitochondrial (MICU3) and ...
 353-455 6.31e-13

EF-hand, calcium binding motif, found in calcium uptake protein 3, mitochondrial (MICU3) and similar proteins; MICU3, also termed EF-hand domain-containing family member A2 (EFHA2), is a paralog of MICU1 and notably found in the central nervous system (CNS) and skeletal muscle. At present, the precise molecular function of MICU3 remains unclear. It likely has a role in mitochondrial calcium handling. MICU3 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: 320083 [Multi-domain]  Cd Length: 128  Bit Score: 65.61  E-value: 6.31e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133436468 353 KKKARMLKRVKKTFRDH---GKGISKEDYLNFFHFLNN----INDVDTALTFYHIAGASIDQPTLKHVAKTVAHVDLSDH 425
Cdd:cd16175    19 KKEFLVLQEIFRTLLVHffgKKGKAELNFEDFYRFMDNlqteVEDFTIAMRMYTFADRSISQDEFARAVKVCTGLKLSPH 98

                          90       100       110
                  ....*....|....*....|....*....|
gi 1133436468 426 VIHVVFTIFDENQDGQLSNKEFIAVMKNRL 455
Cdd:cd16175    99 LVNTVFKIFDVDGDGQLSYKEFIGIMKDRL 128
EFh_MICU2 cd16174
EF-hand, calcium binding motif, found in calcium uptake protein 2, mitochondrial (MICU2) and ...
 236-455 9.61e-09

EF-hand, calcium binding motif, found in calcium uptake protein 2, mitochondrial (MICU2) and similar proteins; MICU2, also termed EF-hand domain-containing family member A1 (EFHA1), is a mitochondrial-localized paralog of MICU1. MICU2 and its paralog, MICU1, are physically associated within the mitochondrial calcium uniporter (MCU) complex and are co-expressed across all tissues. They may operate together with MCU to regulate the channel. At present, the precise molecular function of MICU2 remains unclear. It 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. MICU2 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: 320082 [Multi-domain]  Cd Length: 154  Bit Score: 54.49  E-value: 9.61e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133436468 236 FEIAFRMFDLNGDGDVDCEEFEKVATLIRQQTSIGSRHRDHANTGNTFK--GVNSALTTYFFGPNLKQKLTIEKFLDFQE 313
Cdd:cd16174     2 FHIAFKMLDTDGNEQVEKREFFKLQKIIGKKDDLMTQGGTETYQEASDNsdEVNTTLQVHFFGKDGNEKLQYKEFCRFME 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133436468 314 KLQREIlslefqrktpdengniteadftelllayagypqkkkarmlkrvkktfrdhgkgiskedylnffhflnniNDVDT 393
Cdd:cd16174    82 NLQTEV---------------------------------------------------------------------EDFAI 92

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1133436468 394 ALTFYHIAGASIDQPTLKHVAKTVAHVDLSDHVIHVVFTIFDENQDGQLSNKEFIAVMKNRL 455
Cdd:cd16174    93 AMKMFSEANRPIKLAEFKRAVKVATGQELSDNVLDTVFKIFDLDGDDCLSHGEFLGVLKNRV 154
EF-hand_8 pfam13833
EF-hand domain pair;
402-454 1.30e-05

EF-hand domain pair;


Pssm-ID: 404678 [Multi-domain]  Cd Length: 54  Bit Score: 42.69  E-value: 1.30e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1133436468 402 GASIDQPTLKHVAKTVAHVDLSDHVIHVVFTIFDENQDGQLSNKEFIAVMKNR 454
Cdd:pfam13833   2 KGVITREELKRALALLGLKDLSEDEVDILFREFDTDGDGYISFDEFCVLLERR 54
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
213-256 1.36e-04

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


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 42.09  E-value: 1.36e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 1133436468 213 SSGLITFSDYIFLLTVLSTSRRHFEIAFRMFDLNGDGDVDCEEF 256
Cdd:COG5126    82 GDGKISADEFRRLLTALGVSEEEADELFARLDTDGDGKISFEEF 125
EFh cd00051
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal ...
 213-256 1.60e-03

EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal modulators; most examples in this alignment model have 2 active canonical EF hands. Ca2+ binding induces a conformational change in the EF-hand motif, leading to the activation or inactivation of target proteins. EF-hands tend to occur in pairs or higher copy numbers.


Pssm-ID: 238008 [Multi-domain]  Cd Length: 63  Bit Score: 36.76  E-value: 1.60e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 1133436468 213 SSGLITFSDYIFLLTVLS--TSRRHFEIAFRMFDLNGDGDVDCEEF 256
Cdd:cd00051    13 GDGTISADELKAALKSLGegLSEEEIDEMIREVDKDGDGKIDFEEF 58
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
315-452 3.73e-03

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


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 37.85  E-value: 3.73e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133436468 315 LQREILSLEFQRKTPDENGNITEADFTELLLAYAGypqkkkarmlKRVKKTFRDHGKGISKEDYLNFFHFLNNINDVDTA 394
Cdd:COG5126     2 LQRRKLDRRFDLLDADGDGVLERDDFEALFRRLWA----------TLFSEADTDGDGRISREEFVAGMESLFEATVEPFA 71

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1133436468 395 LTFYHIA-----GaSIDQPTLKHVaktVAHVDLSDHVIHVVFTIFDENQDGQLSNKEFIAVMK 452
Cdd:COG5126    72 RAAFDLLdtdgdG-KISADEFRRL---LTALGVSEEEADELFARLDTDGDGKISFEEFVAAVR 130
 
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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