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Conserved domains on  [gi|545870525|ref|XP_005671124|]
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calcium uptake protein 1, mitochondrial isoform X3 [Sus scrofa]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
EFh_MICU super family cl28896
EF-hand, calcium binding motif, found in mitochondrial calcium uptake proteins MICU1, MICU2, ...
 227-472 5.47e-78

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 cd16173:

Pssm-ID: 333716 [Multi-domain]  Cd Length: 153  Bit Score: 241.08  E-value: 5.47e-78
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545870525 227 NFEIAFKMFDLNGDGEVDMEEFEQVQSIIRSQTSMGMRHRDRSTTGNTLKSGLCSALTTYFFGPDLKGKLTIKNFLEFQR 306
Cdd:cd16173    1 NFEIAFKMFDLNGDGEVDMEEFEQVQSIIRSQTSMGMRHRDRSTTGNTLKTGFSSALTTYFFGADLKGKLTIKNFLEFQR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545870525 307 KLQHDVlkleferhdpvdgriterqfggmllaysgvqskkltamqkqlkkhfkegkgltfqevenfftflkniNDVDTAL 386
Cdd:cd16173   81 KLQHDV-------------------------------------------------------------------NDVDTAL 93

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545870525 387 SFYHMAGASLDKvflrtclhpgavkmppillrhsrnayVTMQQVARTVAKVELSDHVCDVVFALFDCDGNGELSNKEFVS 466
Cdd:cd16173   94 SFYHMAGASLDK--------------------------VTMQQVARTVAKVELSDHVCDVVFALFDCDGNGELSNKEFVA 147


                 ....*.
gi 545870525 467 IMKQRL 472
Cdd:cd16173  148 IMKQRL 153
 
Name Accession Description Interval E-value
EFh_MICU1 cd16173
EF-hand, calcium binding motif, found in calcium uptake protein 1, mitochondrial (MICU1) and ...
 227-472 5.47e-78

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: 241.08  E-value: 5.47e-78
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545870525 227 NFEIAFKMFDLNGDGEVDMEEFEQVQSIIRSQTSMGMRHRDRSTTGNTLKSGLCSALTTYFFGPDLKGKLTIKNFLEFQR 306
Cdd:cd16173    1 NFEIAFKMFDLNGDGEVDMEEFEQVQSIIRSQTSMGMRHRDRSTTGNTLKTGFSSALTTYFFGADLKGKLTIKNFLEFQR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545870525 307 KLQHDVlkleferhdpvdgriterqfggmllaysgvqskkltamqkqlkkhfkegkgltfqevenfftflkniNDVDTAL 386
Cdd:cd16173   81 KLQHDV-------------------------------------------------------------------NDVDTAL 93

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545870525 387 SFYHMAGASLDKvflrtclhpgavkmppillrhsrnayVTMQQVARTVAKVELSDHVCDVVFALFDCDGNGELSNKEFVS 466
Cdd:cd16173   94 SFYHMAGASLDK--------------------------VTMQQVARTVAKVELSDHVCDVVFALFDCDGNGELSNKEFVA 147


                 ....*.
gi 545870525 467 IMKQRL 472
Cdd:cd16173  148 IMKQRL 153
EF-hand_5 pfam13202
EF hand;
228-251 2.78e-04

EF hand;


Pssm-ID: 433035 [Multi-domain]  Cd Length: 25  Bit Score: 38.07  E-value: 2.78e-04
                          10        20
                  ....*....|....*....|....
gi 545870525  228 FEIAFKMFDLNGDGEVDMEEFEQV 251
Cdd:pfam13202   1 LKDTFRQIDLNGDGKISKEELRRL 24
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
207-248 9.31e-04

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


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 39.39  E-value: 9.31e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 545870525 207 GLISFSDYIFLTTVLSTPQRNFEIAFKMFDLNGDGEVDMEEF 248
Cdd:COG5126   84 GKISADEFRRLLTALGVSEEEADELFARLDTDGDGKISFEEF 125
EFh smart00054
EF-hand, calcium binding motif; EF-hands are calcium-binding motifs that occur at least in ...
 231-251 2.50e-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: 35.43  E-value: 2.50e-03
                           10        20
                   ....*....|....*....|.
gi 545870525   231 AFKMFDLNGDGEVDMEEFEQV 251
Cdd:smart00054   5 AFRLFDKDGDGKIDFEEFKDL 25
 
Name Accession Description Interval E-value
EFh_MICU1 cd16173
EF-hand, calcium binding motif, found in calcium uptake protein 1, mitochondrial (MICU1) and ...
 227-472 5.47e-78

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: 241.08  E-value: 5.47e-78
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545870525 227 NFEIAFKMFDLNGDGEVDMEEFEQVQSIIRSQTSMGMRHRDRSTTGNTLKSGLCSALTTYFFGPDLKGKLTIKNFLEFQR 306
Cdd:cd16173    1 NFEIAFKMFDLNGDGEVDMEEFEQVQSIIRSQTSMGMRHRDRSTTGNTLKTGFSSALTTYFFGADLKGKLTIKNFLEFQR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545870525 307 KLQHDVlkleferhdpvdgriterqfggmllaysgvqskkltamqkqlkkhfkegkgltfqevenfftflkniNDVDTAL 386
Cdd:cd16173   81 KLQHDV-------------------------------------------------------------------NDVDTAL 93

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545870525 387 SFYHMAGASLDKvflrtclhpgavkmppillrhsrnayVTMQQVARTVAKVELSDHVCDVVFALFDCDGNGELSNKEFVS 466
Cdd:cd16173   94 SFYHMAGASLDK--------------------------VTMQQVARTVAKVELSDHVCDVVFALFDCDGNGELSNKEFVA 147


                 ....*.
gi 545870525 467 IMKQRL 472
Cdd:cd16173  148 IMKQRL 153
EFh_MICU cd15900
EF-hand, calcium binding motif, found in mitochondrial calcium uptake proteins MICU1, MICU2, ...
 227-472 2.38e-62

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: 200.53  E-value: 2.38e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545870525 227 NFEIAFKMFDLNGDGEVDMEEFEQVQSIIRSQTSMGMRHRDRSTTGNTlKSGLCSALTTYFFGPDLKGKLTIKNFLEFQR 306
Cdd:cd15900    1 HFEIAFKMFDLDGDGELDKEEFNKVQSIIRSQTSVGQRHRDHTNGEST-KLGMNSTLARYFFGKDGKQKLSIEKFLEFQE 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545870525 307 KLQHDvlkleferhdpvdgriterqfggmllaysgvqskkltamqkqlkkhfkegkgltfqevenfftflknINDVDTAL 386
Cdd:cd15900   80 NLQEE-------------------------------------------------------------------IDDVDTAL 92

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545870525 387 SFYHMAGASLDKvflrtclhpgavkmppillrhsrnayVTMQQVARTVAKVELSDHVCDVVFALFDCDGNGELSNKEFVS 466
Cdd:cd15900   93 TFYHLAGASIDR--------------------------KTFKRAAKVVAGVELSDHVVDVVFTIFDEDGDGILSHKEFIS 146


                 ....*.
gi 545870525 467 IMKQRL 472
Cdd:cd15900  147 VMKDRL 152
EFh_MICU3 cd16175
EF-hand, calcium binding motif, found in calcium uptake protein 3, mitochondrial (MICU3) and ...
 228-472 1.30e-08

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: 53.29  E-value: 1.30e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545870525 228 FEIAFKMFDLNGDGEVDMEEFEQVQSIIRSqtsmgmrhrdrsttgntlksglcsaLTTYFFGPDLKGKLTIKNFLEFQRK 307
Cdd:cd16175    2 FRIAFNMFDTDGNEMVDKKEFLVLQEIFRT-------------------------LLVHFFGKKGKAELNFEDFYRFMDN 56

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545870525 308 LQhdvlkleferhdpvdgriterqfggmllaysgvqskkltamqkqlkkhfkegkgltfQEVENFftflknindvDTALS 387
Cdd:cd16175   57 LQ---------------------------------------------------------TEVEDF----------TIAMR 69

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545870525 388 FYHMAGASLDKVflrtclhpgavkmppillRHSRNAYVTMQQvartvakvELSDHVCDVVFALFDCDGNGELSNKEFVSI 467
Cdd:cd16175   70 MYTFADRSISQD------------------EFARAVKVCTGL--------KLSPHLVNTVFKIFDVDGDGQLSYKEFIGI 123


                 ....*
gi 545870525 468 MKQRL 472
Cdd:cd16175  124 MKDRL 128
EFh_MICU2 cd16174
EF-hand, calcium binding motif, found in calcium uptake protein 2, mitochondrial (MICU2) and ...
 228-312 1.47e-07

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: 51.02  E-value: 1.47e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545870525 228 FEIAFKMFDLNGDGEVDMEEFEQVQSIIRSQTSMGMRHRDRSTTGNTLKS-GLCSALTTYFFGPDLKGKLTIKNFLEFQR 306
Cdd:cd16174    2 FHIAFKMLDTDGNEQVEKREFFKLQKIIGKKDDLMTQGGTETYQEASDNSdEVNTTLQVHFFGKDGNEKLQYKEFCRFME 81


                 ....*.
gi 545870525 307 KLQHDV 312
Cdd:cd16174   82 NLQTEV 87
EF-hand_5 pfam13202
EF hand;
228-251 2.78e-04

EF hand;


Pssm-ID: 433035 [Multi-domain]  Cd Length: 25  Bit Score: 38.07  E-value: 2.78e-04
                          10        20
                  ....*....|....*....|....
gi 545870525  228 FEIAFKMFDLNGDGEVDMEEFEQV 251
Cdd:pfam13202   1 LKDTFRQIDLNGDGKISKEELRRL 24
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
207-248 9.31e-04

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


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 39.39  E-value: 9.31e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 545870525 207 GLISFSDYIFLTTVLSTPQRNFEIAFKMFDLNGDGEVDMEEF 248
Cdd:COG5126   84 GKISADEFRRLLTALGVSEEEADELFARLDTDGDGKISFEEF 125
EFh_PEF_ALG-2_like cd16185
EF-hand, calcium binding motif, found in homologs of mammalian apoptosis-linked gene 2 protein ...
 217-273 1.01e-03

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


Pssm-ID: 320060 [Multi-domain]  Cd Length: 163  Bit Score: 39.89  E-value: 1.01e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 545870525 217 LTTVLSTPQRNFEIA-----FKMFDLNGDGEVDMEEFEQVQSIIrSQTSMGMRHRDRSTTGN 273
Cdd:cd16185   22 LQKALAGGGLLFSLAtaeklIRMFDRDGNGTIDFEEFAALHQFL-SNMQNGFEQRDTSRSGR 82
EFh smart00054
EF-hand, calcium binding motif; EF-hands are calcium-binding motifs that occur at least in ...
 231-251 2.50e-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: 35.43  E-value: 2.50e-03
                           10        20
                   ....*....|....*....|.
gi 545870525   231 AFKMFDLNGDGEVDMEEFEQV 251
Cdd:smart00054   5 AFRLFDKDGDGKIDFEEFKDL 25
EFh cd00051
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal ...
 207-248 3.91e-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: 35.99  E-value: 3.91e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 545870525 207 GLISFSDYIFLTTVLSTPQRNFEI--AFKMFDLNGDGEVDMEEF 248
Cdd:cd00051   15 GTISADELKAALKSLGEGLSEEEIdeMIREVDKDGDGKIDFEEF 58
EF-hand_1 pfam00036
EF hand; The EF-hands can be divided into two classes: signalling proteins and buffering ...
 228-251 6.64e-03

EF hand; The EF-hands can be divided into two classes: signalling proteins and buffering/transport proteins. The first group is the largest and includes the most well-known members of the family such as calmodulin, troponin C and S100B. These proteins typically undergo a calcium-dependent conformational change which opens a target binding site. The latter group is represented by calbindin D9k and do not undergo calcium dependent conformational changes.


Pssm-ID: 425435 [Multi-domain]  Cd Length: 29  Bit Score: 34.30  E-value: 6.64e-03
                          10        20
                  ....*....|....*....|....
gi 545870525  228 FEIAFKMFDLNGDGEVDMEEFEQV 251
Cdd:pfam00036   2 LKEIFRLFDKDGDGKIDFEEFKEL 25
EF-hand_1 pfam00036
EF hand; The EF-hands can be divided into two classes: signalling proteins and buffering ...
 444-469 8.40e-03

EF hand; The EF-hands can be divided into two classes: signalling proteins and buffering/transport proteins. The first group is the largest and includes the most well-known members of the family such as calmodulin, troponin C and S100B. These proteins typically undergo a calcium-dependent conformational change which opens a target binding site. The latter group is represented by calbindin D9k and do not undergo calcium dependent conformational changes.


Pssm-ID: 425435 [Multi-domain]  Cd Length: 29  Bit Score: 33.91  E-value: 8.40e-03
                          10        20
                  ....*....|....*....|....*.
gi 545870525  444 CDVVFALFDCDGNGELSNKEFVSIMK 469
Cdd:pfam00036   2 LKEIFRLFDKDGDGKIDFEEFKELLK 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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