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Conserved domains on  [gi|334305706|sp|C8Z792|]
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RecName: Full=Altered inheritance of mitochondria protein 9, mitochondrial; AltName: Full=Found in mitochondrial proteome protein 29; Flags: Precursor

Protein Classification

protein kinase family protein( domain architecture ID 229378)

protein kinase family protein may catalyze the transfer of the gamma-phosphoryl group from ATP to substrates such as serine/threonine and/or tyrosine residues on proteins, or may be a pseudokinase

CATH:  1.10.510.10
PubMed:  16244704
SCOP:  4003661

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PKc_like super family cl21453
Protein Kinases, catalytic domain; The protein kinase superfamily is mainly composed of the ...
 147-284 4.14e-09

Protein Kinases, catalytic domain; The protein kinase superfamily is mainly composed of the catalytic domains of serine/threonine-specific and tyrosine-specific protein kinases. It also includes RIO kinases, which are atypical serine protein kinases, aminoglycoside phosphotransferases, and choline kinases. These proteins catalyze the transfer of the gamma-phosphoryl group from ATP to hydroxyl groups in specific substrates such as serine, threonine, or tyrosine residues of proteins.


The actual alignment was detected with superfamily member cd05120:

Pssm-ID: 473864 [Multi-domain]  Cd Length: 158  Bit Score: 55.77  E-value: 4.14e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334305706 147 IHEGKHHRIYKVDTNLNkaFILRIPyplenENTLSYRIRSEVATMDFADLKLGIKVPKIFCYGvnslNPVRQPFVLQEFI 226
Cdd:cd05120    6 IKEGGDNKVYLLGDPRE--YVLKIG-----PPRLKKDLEKEAAMLQLLAGKLSLPVPKVYGFG----ESDGWEYLLMERI 74

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 334305706 227 EGELLMKDWDPLiedgSSNQKKydNVIKQVSDFQSKLVSLKLNAFgsiyFNNDLKDGN 284
Cdd:cd05120   75 EGETLSEVWPRL----SEEEKE--KIADQLAEILAALHRIDSSVL----THGDLHPGN 122
 
Name Accession Description Interval E-value
APH_ChoK_like cd05120
Aminoglycoside 3'-phosphotransferase and Choline Kinase family; This family is composed of APH, ...
 147-284 4.14e-09

Aminoglycoside 3'-phosphotransferase and Choline Kinase family; This family is composed of APH, ChoK, ethanolamine kinase (ETNK), macrolide 2'-phosphotransferase (MPH2'), an unusual homoserine kinase, and uncharacterized proteins with similarity to the N-terminal domain of acyl-CoA dehydrogenase 10 (ACAD10). The members of this family catalyze the transfer of the gamma-phosphoryl group from ATP (or CTP) to small molecule substrates such as aminoglycosides, macrolides, choline, ethanolamine, and homoserine. Phosphorylation of the antibiotics, aminoglycosides and macrolides, leads to their inactivation and to bacterial antibiotic resistance. Phosphorylation of choline, ethanolamine, and homoserine serves as precursors to the synthesis of important biological compounds, such as the major phospholipids, phosphatidylcholine and phosphatidylethanolamine and the amino acids, threonine, methionine, and isoleucine. The APH/ChoK family is part of a larger superfamily that includes the catalytic domains of other kinases, such as the typical serine/threonine/tyrosine protein kinases (PKs), RIO kinases, actin-fragmin kinase (AFK), and phosphoinositide 3-kinase (PI3K).


Pssm-ID: 270690 [Multi-domain]  Cd Length: 158  Bit Score: 55.77  E-value: 4.14e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334305706 147 IHEGKHHRIYKVDTNLNkaFILRIPyplenENTLSYRIRSEVATMDFADLKLGIKVPKIFCYGvnslNPVRQPFVLQEFI 226
Cdd:cd05120    6 IKEGGDNKVYLLGDPRE--YVLKIG-----PPRLKKDLEKEAAMLQLLAGKLSLPVPKVYGFG----ESDGWEYLLMERI 74

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 334305706 227 EGELLMKDWDPLiedgSSNQKKydNVIKQVSDFQSKLVSLKLNAFgsiyFNNDLKDGN 284
Cdd:cd05120   75 EGETLSEVWPRL----SEEEKE--KIADQLAEILAALHRIDSSVL----THGDLHPGN 122
 
Name Accession Description Interval E-value
APH_ChoK_like cd05120
Aminoglycoside 3'-phosphotransferase and Choline Kinase family; This family is composed of APH, ...
 147-284 4.14e-09

Aminoglycoside 3'-phosphotransferase and Choline Kinase family; This family is composed of APH, ChoK, ethanolamine kinase (ETNK), macrolide 2'-phosphotransferase (MPH2'), an unusual homoserine kinase, and uncharacterized proteins with similarity to the N-terminal domain of acyl-CoA dehydrogenase 10 (ACAD10). The members of this family catalyze the transfer of the gamma-phosphoryl group from ATP (or CTP) to small molecule substrates such as aminoglycosides, macrolides, choline, ethanolamine, and homoserine. Phosphorylation of the antibiotics, aminoglycosides and macrolides, leads to their inactivation and to bacterial antibiotic resistance. Phosphorylation of choline, ethanolamine, and homoserine serves as precursors to the synthesis of important biological compounds, such as the major phospholipids, phosphatidylcholine and phosphatidylethanolamine and the amino acids, threonine, methionine, and isoleucine. The APH/ChoK family is part of a larger superfamily that includes the catalytic domains of other kinases, such as the typical serine/threonine/tyrosine protein kinases (PKs), RIO kinases, actin-fragmin kinase (AFK), and phosphoinositide 3-kinase (PI3K).


Pssm-ID: 270690 [Multi-domain]  Cd Length: 158  Bit Score: 55.77  E-value: 4.14e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334305706 147 IHEGKHHRIYKVDTNLNkaFILRIPyplenENTLSYRIRSEVATMDFADLKLGIKVPKIFCYGvnslNPVRQPFVLQEFI 226
Cdd:cd05120    6 IKEGGDNKVYLLGDPRE--YVLKIG-----PPRLKKDLEKEAAMLQLLAGKLSLPVPKVYGFG----ESDGWEYLLMERI 74

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 334305706 227 EGELLMKDWDPLiedgSSNQKKydNVIKQVSDFQSKLVSLKLNAFgsiyFNNDLKDGN 284
Cdd:cd05120   75 EGETLSEVWPRL----SEEEKE--KIADQLAEILAALHRIDSSVL----THGDLHPGN 122
 
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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