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Conserved domains on  [gi|1227972837|ref|XP_021917861|]
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calcium uptake protein 1 homolog, mitochondrial-like isoform X1 [Zootermopsis nevadensis]

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, ...
 262-482 2.17e-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: 231.73  E-value: 2.17e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227972837 262 HFEIAFRMFDLNGDGDVDSEEFEKVATLVRQQTSIGSRHRDHANTGNTFKGVNSALTTYFFGPNMNQKLTIEKFLEFQHQ 341
Cdd:cd15900     1 HFEIAFKMFDLDGDGELDKEEFNKVQSIIRSQTSVGQRHRDHTNGESTKLGMNSTLARYFFGKDGKQKLSIEKFLEFQEN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227972837 342 LQREilslefqrkgpdengniteadftelllayagyppkkktrmlkrvkkvfkedakgisrddylkfyhflnnINDVDTA 421
Cdd:cd15900    81 LQEE---------------------------------------------------------------------IDDVDTA 91

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1227972837 422 LTFYHIAGASIDHATLKHVAKTVAHVDLSDHVINVVFTIFDENLDGQLSNREFVAVMKNRL 482
Cdd:cd15900    92 LTFYHLAGASIDRKTFKRAAKVVAGVELSDHVVDVVFTIFDEDGDGILSHKEFISVMKDRL 152
FRQ1 super family cl34916
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
228-283 2.81e-04

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: 40.93  E-value: 2.81e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1227972837 228 ALDEDSifyklgsSGLITFSDYIFLLTVLSTSRRHFEIAFRMFDLNGDGDVDSEEF 283
Cdd:COG5126    77 LLDTDG-------DGKISADEFRRLLTALGVSEEEADELFARLDTDGDGKISFEEF 125
 
Name Accession Description Interval E-value
EFh_MICU cd15900
EF-hand, calcium binding motif, found in mitochondrial calcium uptake proteins MICU1, MICU2, ...
 262-482 2.17e-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: 231.73  E-value: 2.17e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227972837 262 HFEIAFRMFDLNGDGDVDSEEFEKVATLVRQQTSIGSRHRDHANTGNTFKGVNSALTTYFFGPNMNQKLTIEKFLEFQHQ 341
Cdd:cd15900     1 HFEIAFKMFDLDGDGELDKEEFNKVQSIIRSQTSVGQRHRDHTNGESTKLGMNSTLARYFFGKDGKQKLSIEKFLEFQEN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227972837 342 LQREilslefqrkgpdengniteadftelllayagyppkkktrmlkrvkkvfkedakgisrddylkfyhflnnINDVDTA 421
Cdd:cd15900    81 LQEE---------------------------------------------------------------------IDDVDTA 91

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1227972837 422 LTFYHIAGASIDHATLKHVAKTVAHVDLSDHVINVVFTIFDENLDGQLSNREFVAVMKNRL 482
Cdd:cd15900    92 LTFYHLAGASIDRKTFKRAAKVVAGVELSDHVVDVVFTIFDEDGDGILSHKEFISVMKDRL 152
EF-hand_8 pfam13833
EF-hand domain pair;
429-481 8.29e-05

EF-hand domain pair;


Pssm-ID: 404678 [Multi-domain]  Cd Length: 54  Bit Score: 40.38  E-value: 8.29e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1227972837 429 GASIDHATLKHVAKTVAHVDLSDHVINVVFTIFDENLDGQLSNREFVAVMKNR 481
Cdd:pfam13833   2 KGVITREELKRALALLGLKDLSEDEVDILFREFDTDGDGYISFDEFCVLLERR 54
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
228-283 2.81e-04

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


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 40.93  E-value: 2.81e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1227972837 228 ALDEDSifyklgsSGLITFSDYIFLLTVLSTSRRHFEIAFRMFDLNGDGDVDSEEF 283
Cdd:COG5126    77 LLDTDG-------DGKISADEFRRLLTALGVSEEEADELFARLDTDGDGKISFEEF 125
EFh cd00051
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal ...
 240-283 3.67e-04

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: 38.68  E-value: 3.67e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 1227972837 240 SSGLITFSDYIFLLTVLS--TSRRHFEIAFRMFDLNGDGDVDSEEF 283
Cdd:cd00051    13 GDGTISADELKAALKSLGegLSEEEIDEMIREVDKDGDGKIDFEEF 58
EFh smart00054
EF-hand, calcium binding motif; EF-hands are calcium-binding motifs that occur at least in ...
 266-288 6.51e-03

EF-hand, calcium binding motif; EF-hands are calcium-binding motifs that occur at least in pairs. Links between disease states and genes encoding EF-hands, particularly the S100 subclass, are emerging. Each motif consists of a 12 residue loop flanked on either side by a 12 residue alpha-helix. EF-hands undergo a conformational change unpon binding calcium ions.


Pssm-ID: 197492 [Multi-domain]  Cd Length: 29  Bit Score: 34.28  E-value: 6.51e-03
                           10        20
                   ....*....|....*....|...
gi 1227972837  266 AFRMFDLNGDGDVDSEEFEKVAT 288
Cdd:smart00054   5 AFRLFDKDGDGKIDFEEFKDLLK 27
 
Name Accession Description Interval E-value
EFh_MICU cd15900
EF-hand, calcium binding motif, found in mitochondrial calcium uptake proteins MICU1, MICU2, ...
 262-482 2.17e-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: 231.73  E-value: 2.17e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227972837 262 HFEIAFRMFDLNGDGDVDSEEFEKVATLVRQQTSIGSRHRDHANTGNTFKGVNSALTTYFFGPNMNQKLTIEKFLEFQHQ 341
Cdd:cd15900     1 HFEIAFKMFDLDGDGELDKEEFNKVQSIIRSQTSVGQRHRDHTNGESTKLGMNSTLARYFFGKDGKQKLSIEKFLEFQEN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227972837 342 LQREilslefqrkgpdengniteadftelllayagyppkkktrmlkrvkkvfkedakgisrddylkfyhflnnINDVDTA 421
Cdd:cd15900    81 LQEE---------------------------------------------------------------------IDDVDTA 91

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1227972837 422 LTFYHIAGASIDHATLKHVAKTVAHVDLSDHVINVVFTIFDENLDGQLSNREFVAVMKNRL 482
Cdd:cd15900    92 LTFYHLAGASIDRKTFKRAAKVVAGVELSDHVVDVVFTIFDEDGDGILSHKEFISVMKDRL 152
EFh_MICU1 cd16173
EF-hand, calcium binding motif, found in calcium uptake protein 1, mitochondrial (MICU1) and ...
 262-482 7.21e-49

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: 165.58  E-value: 7.21e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227972837 262 HFEIAFRMFDLNGDGDVDSEEFEKVATLVRQQTSIGSRHRDHANTGNTFK-GVNSALTTYFFGPNMNQKLTIEKFLEFQH 340
Cdd:cd16173     1 NFEIAFKMFDLNGDGEVDMEEFEQVQSIIRSQTSMGMRHRDRSTTGNTLKtGFSSALTTYFFGADLKGKLTIKNFLEFQR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227972837 341 QLQreilslefqrkgpdengniteadftelllayagyppkkktrmlkrvkkvfkedakgisrddylkfyhflNNINDVDT 420
Cdd:cd16173    81 KLQ---------------------------------------------------------------------HDVNDVDT 91

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1227972837 421 ALTFYHIAGASIDHATLKHVAKTVAHVDLSDHVINVVFTIFDENLDGQLSNREFVAVMKNRL 482
Cdd:cd16173    92 ALSFYHMAGASLDKVTMQQVARTVAKVELSDHVCDVVFALFDCDGNGELSNKEFVAIMKQRL 153
EFh_MICU3 cd16175
EF-hand, calcium binding motif, found in calcium uptake protein 3, mitochondrial (MICU3) and ...
 398-482 2.64e-11

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: 60.99  E-value: 2.64e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227972837 398 KGISRDDYLKFYHFLNN----INDVDTALTFYHIAGASIDHATLKHVAKTVAHVDLSDHVINVVFTIFDENLDGQLSNRE 473
Cdd:cd16175    40 KGKAELNFEDFYRFMDNlqteVEDFTIAMRMYTFADRSISQDEFARAVKVCTGLKLSPHLVNTVFKIFDVDGDGQLSYKE 119


                  ....*....
gi 1227972837 474 FVAVMKNRL 482
Cdd:cd16175   120 FIGIMKDRL 128
EFh_MICU2 cd16174
EF-hand, calcium binding motif, found in calcium uptake protein 2, mitochondrial (MICU2) and ...
 263-482 4.45e-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: 55.26  E-value: 4.45e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227972837 263 FEIAFRMFDLNGDGDVDSEEFEKVATLVRQQTSIGSRHRDHANTGNTFK--GVNSALTTYFFGPNMNQKLTIEKFLEFQH 340
Cdd:cd16174     2 FHIAFKMLDTDGNEQVEKREFFKLQKIIGKKDDLMTQGGTETYQEASDNsdEVNTTLQVHFFGKDGNEKLQYKEFCRFME 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227972837 341 QLQREIlslefqrkgpdengniteadftelllayagyppkkktrmlkrvkkvfkedakgisrddylkfyhflnniNDVDT 420
Cdd:cd16174    82 NLQTEV---------------------------------------------------------------------EDFAI 92

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1227972837 421 ALTFYHIAGASIDHATLKHVAKTVAHVDLSDHVINVVFTIFDENLDGQLSNREFVAVMKNRL 482
Cdd:cd16174    93 AMKMFSEANRPIKLAEFKRAVKVATGQELSDNVLDTVFKIFDLDGDDCLSHGEFLGVLKNRV 154
EF-hand_8 pfam13833
EF-hand domain pair;
429-481 8.29e-05

EF-hand domain pair;


Pssm-ID: 404678 [Multi-domain]  Cd Length: 54  Bit Score: 40.38  E-value: 8.29e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1227972837 429 GASIDHATLKHVAKTVAHVDLSDHVINVVFTIFDENLDGQLSNREFVAVMKNR 481
Cdd:pfam13833   2 KGVITREELKRALALLGLKDLSEDEVDILFREFDTDGDGYISFDEFCVLLERR 54
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
228-283 2.81e-04

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


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 40.93  E-value: 2.81e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1227972837 228 ALDEDSifyklgsSGLITFSDYIFLLTVLSTSRRHFEIAFRMFDLNGDGDVDSEEF 283
Cdd:COG5126    77 LLDTDG-------DGKISADEFRRLLTALGVSEEEADELFARLDTDGDGKISFEEF 125
EFh cd00051
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal ...
 240-283 3.67e-04

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: 38.68  E-value: 3.67e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 1227972837 240 SSGLITFSDYIFLLTVLS--TSRRHFEIAFRMFDLNGDGDVDSEEF 283
Cdd:cd00051    13 GDGTISADELKAALKSLGegLSEEEIDEMIREVDKDGDGKIDFEEF 58
EF-hand_5 pfam13202
EF hand;
263-286 2.81e-03

EF hand;


Pssm-ID: 433035 [Multi-domain]  Cd Length: 25  Bit Score: 35.37  E-value: 2.81e-03
                          10        20
                  ....*....|....*....|....
gi 1227972837 263 FEIAFRMFDLNGDGDVDSEEFEKV 286
Cdd:pfam13202   1 LKDTFRQIDLNGDGKISKEELRRL 24
EFh smart00054
EF-hand, calcium binding motif; EF-hands are calcium-binding motifs that occur at least in ...
 266-288 6.51e-03

EF-hand, calcium binding motif; EF-hands are calcium-binding motifs that occur at least in pairs. Links between disease states and genes encoding EF-hands, particularly the S100 subclass, are emerging. Each motif consists of a 12 residue loop flanked on either side by a 12 residue alpha-helix. EF-hands undergo a conformational change unpon binding calcium ions.


Pssm-ID: 197492 [Multi-domain]  Cd Length: 29  Bit Score: 34.28  E-value: 6.51e-03
                           10        20
                   ....*....|....*....|...
gi 1227972837  266 AFRMFDLNGDGDVDSEEFEKVAT 288
Cdd:smart00054   5 AFRLFDKDGDGKIDFEEFKDLLK 27
 
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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