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Conserved domains on  [gi|116256483|ref|NP_006068|]
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calcium uptake protein 1, mitochondrial isoform 1 [Homo sapiens]

Protein Classification

EFh_MICU1 domain-containing protein( domain architecture ID 11610842)

EFh_MICU1 domain-containing protein

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
EFh_MICU1 cd16173
EF-hand, calcium binding motif, found in calcium uptake protein 1, mitochondrial (MICU1) and ...
224-443 1.69e-84

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: 256.87  E-value: 1.69e-84
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116256483 224 NFEIAFKMFDLNGDGEVDMEEFEQVQSIIRSQTSMGMRHRDRPTTGNTLKSGLCSALTTYFFGADLKGKLTIKNFLEFQR 303
Cdd:cd16173    1 NFEIAFKMFDLNGDGEVDMEEFEQVQSIIRSQTSMGMRHRDRSTTGNTLKTGFSSALTTYFFGADLKGKLTIKNFLEFQR 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116256483 304 KLQHDVlkleferhdpvdgriterqfggmllaysgvqskkltamqrqlkkhfkegkgltfqevenfftflkniNDVDTAL 383
Cdd:cd16173   81 KLQHDV-------------------------------------------------------------------NDVDTAL 93
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 116256483 384 SFYHMAGASLDKVTMQQVARTVAKVELSDHVCDVVFALFDCDGNGELSNKEFVSIMKQRL 443
Cdd:cd16173   94 SFYHMAGASLDKVTMQQVARTVAKVELSDHVCDVVFALFDCDGNGELSNKEFVAIMKQRL 153
 
Name Accession Description Interval E-value
EFh_MICU1 cd16173
EF-hand, calcium binding motif, found in calcium uptake protein 1, mitochondrial (MICU1) and ...
224-443 1.69e-84

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: 256.87  E-value: 1.69e-84
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116256483 224 NFEIAFKMFDLNGDGEVDMEEFEQVQSIIRSQTSMGMRHRDRPTTGNTLKSGLCSALTTYFFGADLKGKLTIKNFLEFQR 303
Cdd:cd16173    1 NFEIAFKMFDLNGDGEVDMEEFEQVQSIIRSQTSMGMRHRDRSTTGNTLKTGFSSALTTYFFGADLKGKLTIKNFLEFQR 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116256483 304 KLQHDVlkleferhdpvdgriterqfggmllaysgvqskkltamqrqlkkhfkegkgltfqevenfftflkniNDVDTAL 383
Cdd:cd16173   81 KLQHDV-------------------------------------------------------------------NDVDTAL 93
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 116256483 384 SFYHMAGASLDKVTMQQVARTVAKVELSDHVCDVVFALFDCDGNGELSNKEFVSIMKQRL 443
Cdd:cd16173   94 SFYHMAGASLDKVTMQQVARTVAKVELSDHVCDVVFALFDCDGNGELSNKEFVAIMKQRL 153
EF-hand_5 pfam13202
EF hand;
225-248 3.93e-04

EF hand;


Pssm-ID: 433035 [Multi-domain]  Cd Length: 25  Bit Score: 37.68  E-value: 3.93e-04
                          10        20
                  ....*....|....*....|....
gi 116256483  225 FEIAFKMFDLNGDGEVDMEEFEQV 248
Cdd:pfam13202   1 LKDTFRQIDLNGDGKISKEELRRL 24
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
204-245 1.44e-03

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


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 39.00  E-value: 1.44e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 116256483 204 GLISFSDYIFLTTVLSTPQRNFEIAFKMFDLNGDGEVDMEEF 245
Cdd:COG5126   84 GKISADEFRRLLTALGVSEEEADELFARLDTDGDGKISFEEF 125
EFh smart00054
EF-hand, calcium binding motif; EF-hands are calcium-binding motifs that occur at least in ...
228-248 3.60e-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: 35.05  E-value: 3.60e-03
                           10        20
                   ....*....|....*....|.
gi 116256483   228 AFKMFDLNGDGEVDMEEFEQV 248
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 ...
224-443 1.69e-84

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: 256.87  E-value: 1.69e-84
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116256483 224 NFEIAFKMFDLNGDGEVDMEEFEQVQSIIRSQTSMGMRHRDRPTTGNTLKSGLCSALTTYFFGADLKGKLTIKNFLEFQR 303
Cdd:cd16173    1 NFEIAFKMFDLNGDGEVDMEEFEQVQSIIRSQTSMGMRHRDRSTTGNTLKTGFSSALTTYFFGADLKGKLTIKNFLEFQR 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116256483 304 KLQHDVlkleferhdpvdgriterqfggmllaysgvqskkltamqrqlkkhfkegkgltfqevenfftflkniNDVDTAL 383
Cdd:cd16173   81 KLQHDV-------------------------------------------------------------------NDVDTAL 93
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 116256483 384 SFYHMAGASLDKVTMQQVARTVAKVELSDHVCDVVFALFDCDGNGELSNKEFVSIMKQRL 443
Cdd:cd16173   94 SFYHMAGASLDKVTMQQVARTVAKVELSDHVCDVVFALFDCDGNGELSNKEFVAIMKQRL 153
EFh_MICU cd15900
EF-hand, calcium binding motif, found in mitochondrial calcium uptake proteins MICU1, MICU2, ...
224-443 2.30e-66

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: 210.16  E-value: 2.30e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116256483 224 NFEIAFKMFDLNGDGEVDMEEFEQVQSIIRSQTSMGMRHRDRpTTGNTLKSGLCSALTTYFFGADLKGKLTIKNFLEFQR 303
Cdd:cd15900    1 HFEIAFKMFDLDGDGELDKEEFNKVQSIIRSQTSVGQRHRDH-TNGESTKLGMNSTLARYFFGKDGKQKLSIEKFLEFQE 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116256483 304 KLQHDvlkleferhdpvdgriterqfggmllaysgvqskkltamqrqlkkhfkegkgltfqevenfftflknINDVDTAL 383
Cdd:cd15900   80 NLQEE-------------------------------------------------------------------IDDVDTAL 92
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 116256483 384 SFYHMAGASLDKVTMQQVARTVAKVELSDHVCDVVFALFDCDGNGELSNKEFVSIMKQRL 443
Cdd:cd15900   93 TFYHLAGASIDRKTFKRAAKVVAGVELSDHVVDVVFTIFDEDGDGILSHKEFISVMKDRL 152
EFh_MICU3 cd16175
EF-hand, calcium binding motif, found in calcium uptake protein 3, mitochondrial (MICU3) and ...
349-443 6.24e-12

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: 62.53  E-value: 6.24e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116256483 349 RQLKKHFKEGKGLTFQEVENFFTFLKN----INDVDTALSFYHMAGASLDKVTMQQVARTVAKVELSDHVCDVVFALFDC 424
Cdd:cd16175   30 RTLLVHFFGKKGKAELNFEDFYRFMDNlqteVEDFTIAMRMYTFADRSISQDEFARAVKVCTGLKLSPHLVNTVFKIFDV 109
                         90
                 ....*....|....*....
gi 116256483 425 DGNGELSNKEFVSIMKQRL 443
Cdd:cd16175  110 DGDGQLSYKEFIGIMKDRL 128
EFh_MICU2 cd16174
EF-hand, calcium binding motif, found in calcium uptake protein 2, mitochondrial (MICU2) and ...
225-443 3.48e-10

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: 58.34  E-value: 3.48e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116256483 225 FEIAFKMFDLNGDGEVDMEEFEQVQSIIRSQTSMGMRHRDRPTTGNTLKS-GLCSALTTYFFGADLKGKLTIKNFLEFQR 303
Cdd:cd16174    2 FHIAFKMLDTDGNEQVEKREFFKLQKIIGKKDDLMTQGGTETYQEASDNSdEVNTTLQVHFFGKDGNEKLQYKEFCRFME 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116256483 304 KLQhdvlkleferhdpvdgriterqfggmllaysgvqskkltamqrqlkkhfkegkgltfQEVENFftflknindvDTAL 383
Cdd:cd16174   82 NLQ---------------------------------------------------------TEVEDF----------AIAM 94
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 116256483 384 SFYHMAGASLDKVTMQQVARTVAKVELSDHVCDVVFALFDCDGNGELSNKEFVSIMKQRL 443
Cdd:cd16174   95 KMFSEANRPIKLAEFKRAVKVATGQELSDNVLDTVFKIFDLDGDDCLSHGEFLGVLKNRV 154
EF-hand_5 pfam13202
EF hand;
225-248 3.93e-04

EF hand;


Pssm-ID: 433035 [Multi-domain]  Cd Length: 25  Bit Score: 37.68  E-value: 3.93e-04
                          10        20
                  ....*....|....*....|....
gi 116256483  225 FEIAFKMFDLNGDGEVDMEEFEQV 248
Cdd:pfam13202   1 LKDTFRQIDLNGDGKISKEELRRL 24
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
204-245 1.44e-03

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


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 39.00  E-value: 1.44e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 116256483 204 GLISFSDYIFLTTVLSTPQRNFEIAFKMFDLNGDGEVDMEEF 245
Cdd:COG5126   84 GKISADEFRRLLTALGVSEEEADELFARLDTDGDGKISFEEF 125
EFh smart00054
EF-hand, calcium binding motif; EF-hands are calcium-binding motifs that occur at least in ...
228-248 3.60e-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: 35.05  E-value: 3.60e-03
                           10        20
                   ....*....|....*....|.
gi 116256483   228 AFKMFDLNGDGEVDMEEFEQV 248
Cdd:smart00054   5 AFRLFDKDGDGKIDFEEFKDL 25
EFh_PEF_ALG-2_like cd16185
EF-hand, calcium binding motif, found in homologs of mammalian apoptosis-linked gene 2 protein ...
214-265 4.59e-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: 37.96  E-value: 4.59e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 116256483 214 LTTVLSTPQRNFEIA-----FKMFDLNGDGEVDMEEFEQVQSIIrSQTSMGMRHRDR 265
Cdd:cd16185   22 LQKALAGGGLLFSLAtaeklIRMFDRDGNGTIDFEEFAALHQFL-SNMQNGFEQRDT 77
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
219-336 5.44e-03

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


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 37.08  E-value: 5.44e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116256483 219 STPQRNFEIAFKMFDLNGDGEVDMEEFEQvqsiirsqtsMGMRHRDRpttgntlksgLCSAlttyfFGADLKGKLTIKNF 298
Cdd:COG5126    1 DLQRRKLDRRFDLLDADGDGVLERDDFEA----------LFRRLWAT----------LFSE-----ADTDGDGRISREEF 55
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 116256483 299 LEFQRKL----QHDVLKLEFERHDP-VDGRITERQFGGMLLAY 336
Cdd:COG5126   56 VAGMESLfeatVEPFARAAFDLLDTdGDGKISADEFRRLLTAL 98
EFh cd00051
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal ...
204-245 5.62e-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: 35.22  E-value: 5.62e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 116256483 204 GLISFSDYIFLTTVLSTPQRNFEI--AFKMFDLNGDGEVDMEEF 245
Cdd:cd00051   15 GTISADELKAALKSLGEGLSEEEIdeMIREVDKDGDGKIDFEEF 58
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
321-441 8.20e-03

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


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 36.69  E-value: 8.20e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116256483 321 DGRITERQFGGMLLAYsgvqskkltaMQRQLKKHFKEGKG-LTFQEVENFFTFLKNINDVDTALSFYHMAGASLD-KVTM 398
Cdd:COG5126   19 DGVLERDDFEALFRRL----------WATLFSEADTDGDGrISREEFVAGMESLFEATVEPFARAAFDLLDTDGDgKISA 88
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 116256483 399 QQVARTVAKVELSDHVCDVVFALFDCDGNGELSNKEFVSIMKQ 441
Cdd:COG5126   89 DEFRRLLTALGVSEEEADELFARLDTDGDGKISFEEFVAAVRD 131
EF-hand_1 pfam00036
EF hand; The EF-hands can be divided into two classes: signalling proteins and buffering ...
225-248 9.47e-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: 33.53  E-value: 9.47e-03
                          10        20
                  ....*....|....*....|....
gi 116256483  225 FEIAFKMFDLNGDGEVDMEEFEQV 248
Cdd:pfam00036   2 LKEIFRLFDKDGDGKIDFEEFKEL 25
 
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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