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Conserved domains on  [gi|262077088|gb|ACY13057|]
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conserved hypothetical protein [Haliangium ochraceum DSM 14365]

Protein Classification

DUF4032 domain-containing protein( domain architecture ID 10393110)

DUF4032 domain-containing protein; may contain a lipopolysaccharide kinase-like domain belonging to the protein kinase superfamily

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
DUF4032 pfam13224
Domain of unknown function (DUF4032); This presumed domain is functionally uncharacterized. ...
 236-398 2.81e-64

Domain of unknown function (DUF4032); This presumed domain is functionally uncharacterized. This domain family is found in bacteria, and is approximately 170 amino acids in length. The family is found in association with pfam06293.


:

Pssm-ID: 433043  Cd Length: 163  Bit Score: 202.80  E-value: 2.81e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262077088  236 QLWSELFGAEIIAPGEEHKIAARIERVHALGFDVRELDIETADDGVTRTLRLRPGRRHFHAQRLEQLTGVEVAERQARQL 315
Cdd:pfam13224   1 RLWEELTREEVFSPDERWRIEERIRRLNELGFDVGELELVTDDDGTRLRIRPKVVDAGHHRRRLLRLTGLDVEENQARRL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262077088  316 LSDLAYYRSLRHsSASANEALAALEWRAFAFEPMLERI-RAIPGVVDPVQGYCELLVHRYLCSEARGDDVGTDAAFEDWQ 394
Cdd:pfam13224  81 LNDLDAYRAALD-GQDVDEEVAAHRWLTEVFEPTVRAIpAELRGKLEPAEVFHEVLEHRWYLSERAGRDVGLDEAVQSYV 159


                  ....
gi 262077088  395 RCLV 398
Cdd:pfam13224 160 DTVL 163
PKc_like super family cl21453
Protein Kinases, catalytic domain; The protein kinase superfamily is mainly composed of the ...
 62-167 7.22e-04

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 pfam06293:

Pssm-ID: 473864  Cd Length: 206  Bit Score: 40.45  E-value: 7.22e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262077088   62 LPTRTAHREYELLRALEDEGLLVAPPVGLVEGRCGdpeAEHSAALITRYLPFTYSYRELIAQAGLA--TVRAGLPDAFAG 139
Cdd:pfam06293  52 LGRTRAFREFRLIRRLREAGLPVPKPVAAGEVKVG---GGYRADLLTERLEGAQSLADWLADWAVPsgELRRAIWEAVGR 128

                          90       100
                  ....*....|....*....|....*...
gi 262077088  140 LLVELHSAGCFWGDCSLSNVLLRRDADG 167
Cdd:pfam06293 129 LIRQMHRAGVQHGDLYAHHILLQQEGDE 156
 
Name Accession Description Interval E-value
DUF4032 pfam13224
Domain of unknown function (DUF4032); This presumed domain is functionally uncharacterized. ...
 236-398 2.81e-64

Domain of unknown function (DUF4032); This presumed domain is functionally uncharacterized. This domain family is found in bacteria, and is approximately 170 amino acids in length. The family is found in association with pfam06293.


Pssm-ID: 433043  Cd Length: 163  Bit Score: 202.80  E-value: 2.81e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262077088  236 QLWSELFGAEIIAPGEEHKIAARIERVHALGFDVRELDIETADDGVTRTLRLRPGRRHFHAQRLEQLTGVEVAERQARQL 315
Cdd:pfam13224   1 RLWEELTREEVFSPDERWRIEERIRRLNELGFDVGELELVTDDDGTRLRIRPKVVDAGHHRRRLLRLTGLDVEENQARRL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262077088  316 LSDLAYYRSLRHsSASANEALAALEWRAFAFEPMLERI-RAIPGVVDPVQGYCELLVHRYLCSEARGDDVGTDAAFEDWQ 394
Cdd:pfam13224  81 LNDLDAYRAALD-GQDVDEEVAAHRWLTEVFEPTVRAIpAELRGKLEPAEVFHEVLEHRWYLSERAGRDVGLDEAVQSYV 159


                  ....
gi 262077088  395 RCLV 398
Cdd:pfam13224 160 DTVL 163
Kdo pfam06293
Lipopolysaccharide kinase (Kdo/WaaP) family; These lipopolysaccharide kinases are related to ...
 62-167 7.22e-04

Lipopolysaccharide kinase (Kdo/WaaP) family; These lipopolysaccharide kinases are related to protein kinases pfam00069. This family includes waaP (rfaP) gene product is required for the addition of phosphate to O-4 of the first heptose residue of the lipopolysaccharide (LPS) inner core region. It has previously been shown that WaaP is necessary for resistance to hydrophobic and polycationic antimicrobials in E. coli and that it is required for virulence in invasive strains of S. enterica.


Pssm-ID: 428872  Cd Length: 206  Bit Score: 40.45  E-value: 7.22e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262077088   62 LPTRTAHREYELLRALEDEGLLVAPPVGLVEGRCGdpeAEHSAALITRYLPFTYSYRELIAQAGLA--TVRAGLPDAFAG 139
Cdd:pfam06293  52 LGRTRAFREFRLIRRLREAGLPVPKPVAAGEVKVG---GGYRADLLTERLEGAQSLADWLADWAVPsgELRRAIWEAVGR 128

                          90       100
                  ....*....|....*....|....*...
gi 262077088  140 LLVELHSAGCFWGDCSLSNVLLRRDADG 167
Cdd:pfam06293 129 LIRQMHRAGVQHGDLYAHHILLQQEGDE 156
ACAD10_11_N-like cd05154
N-terminal domain of Acyl-CoA dehydrogenase (ACAD) 10 and 11, and similar proteins; This ...
 63-146 1.19e-03

N-terminal domain of Acyl-CoA dehydrogenase (ACAD) 10 and 11, and similar proteins; This subfamily is composed of the N-terminal domains of vertebrate ACAD10 and ACAD11, and similar uncharacterized bacterial and eukaryotic proteins. ACADs are a family of flavoproteins that are involved in the beta-oxidation of fatty acyl-CoA derivatives. ACAD deficiency can cause metabolic disorders including muscle fatigue, hypoglycemia, and hepatic lipidosis. There are at least 11 distinct ACADs, some of which show distinct substrate specificities to either straight-chain or branched-chain fatty acids. ACAD10 is widely expressed in human tissues and highly expressed in liver, kidney, pancreas, and spleen. ACAD10 and ACAD11 are both significantly expressed in human brain tissues. They contain a long N-terminal domain with similarity to phosphotransferases with a Protein Kinase fold, which is absent in other ACADs. They may exhibit multiple functions in acyl-CoA oxidation pathways. ACAD11 utilizes substrates with carbon chain lengths of 20 to 26, with optimal activity towards C22CoA. ACAD10 may be associated with an increased risk in type II diabetes. The ACAD10/11-like subfamily 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: 270703 [Multi-domain]  Cd Length: 254  Bit Score: 40.29  E-value: 1.19e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262077088  63 PTRTAHREYELLRALEDEGLLVAPPVGLvegrCGDPEAEHSAALITRYLPFTYSYRELIAQAGLATVRAGLPDAFAGLLV 142
Cdd:cd05154   41 SAHDLEREYRVLRALAGTGVPVPRVLAL----CEDPSVLGAPFYVMERVDGRVLPDPLPRPDLSPEERRALARSLVDALA 116


                 ....
gi 262077088 143 ELHS 146
Cdd:cd05154  117 ALHS 120
 
Name Accession Description Interval E-value
DUF4032 pfam13224
Domain of unknown function (DUF4032); This presumed domain is functionally uncharacterized. ...
 236-398 2.81e-64

Domain of unknown function (DUF4032); This presumed domain is functionally uncharacterized. This domain family is found in bacteria, and is approximately 170 amino acids in length. The family is found in association with pfam06293.


Pssm-ID: 433043  Cd Length: 163  Bit Score: 202.80  E-value: 2.81e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262077088  236 QLWSELFGAEIIAPGEEHKIAARIERVHALGFDVRELDIETADDGVTRTLRLRPGRRHFHAQRLEQLTGVEVAERQARQL 315
Cdd:pfam13224   1 RLWEELTREEVFSPDERWRIEERIRRLNELGFDVGELELVTDDDGTRLRIRPKVVDAGHHRRRLLRLTGLDVEENQARRL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262077088  316 LSDLAYYRSLRHsSASANEALAALEWRAFAFEPMLERI-RAIPGVVDPVQGYCELLVHRYLCSEARGDDVGTDAAFEDWQ 394
Cdd:pfam13224  81 LNDLDAYRAALD-GQDVDEEVAAHRWLTEVFEPTVRAIpAELRGKLEPAEVFHEVLEHRWYLSERAGRDVGLDEAVQSYV 159


                  ....
gi 262077088  395 RCLV 398
Cdd:pfam13224 160 DTVL 163
Kdo pfam06293
Lipopolysaccharide kinase (Kdo/WaaP) family; These lipopolysaccharide kinases are related to ...
 62-167 7.22e-04

Lipopolysaccharide kinase (Kdo/WaaP) family; These lipopolysaccharide kinases are related to protein kinases pfam00069. This family includes waaP (rfaP) gene product is required for the addition of phosphate to O-4 of the first heptose residue of the lipopolysaccharide (LPS) inner core region. It has previously been shown that WaaP is necessary for resistance to hydrophobic and polycationic antimicrobials in E. coli and that it is required for virulence in invasive strains of S. enterica.


Pssm-ID: 428872  Cd Length: 206  Bit Score: 40.45  E-value: 7.22e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262077088   62 LPTRTAHREYELLRALEDEGLLVAPPVGLVEGRCGdpeAEHSAALITRYLPFTYSYRELIAQAGLA--TVRAGLPDAFAG 139
Cdd:pfam06293  52 LGRTRAFREFRLIRRLREAGLPVPKPVAAGEVKVG---GGYRADLLTERLEGAQSLADWLADWAVPsgELRRAIWEAVGR 128

                          90       100
                  ....*....|....*....|....*...
gi 262077088  140 LLVELHSAGCFWGDCSLSNVLLRRDADG 167
Cdd:pfam06293 129 LIRQMHRAGVQHGDLYAHHILLQQEGDE 156
ACAD10_11_N-like cd05154
N-terminal domain of Acyl-CoA dehydrogenase (ACAD) 10 and 11, and similar proteins; This ...
 63-146 1.19e-03

N-terminal domain of Acyl-CoA dehydrogenase (ACAD) 10 and 11, and similar proteins; This subfamily is composed of the N-terminal domains of vertebrate ACAD10 and ACAD11, and similar uncharacterized bacterial and eukaryotic proteins. ACADs are a family of flavoproteins that are involved in the beta-oxidation of fatty acyl-CoA derivatives. ACAD deficiency can cause metabolic disorders including muscle fatigue, hypoglycemia, and hepatic lipidosis. There are at least 11 distinct ACADs, some of which show distinct substrate specificities to either straight-chain or branched-chain fatty acids. ACAD10 is widely expressed in human tissues and highly expressed in liver, kidney, pancreas, and spleen. ACAD10 and ACAD11 are both significantly expressed in human brain tissues. They contain a long N-terminal domain with similarity to phosphotransferases with a Protein Kinase fold, which is absent in other ACADs. They may exhibit multiple functions in acyl-CoA oxidation pathways. ACAD11 utilizes substrates with carbon chain lengths of 20 to 26, with optimal activity towards C22CoA. ACAD10 may be associated with an increased risk in type II diabetes. The ACAD10/11-like subfamily 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: 270703 [Multi-domain]  Cd Length: 254  Bit Score: 40.29  E-value: 1.19e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262077088  63 PTRTAHREYELLRALEDEGLLVAPPVGLvegrCGDPEAEHSAALITRYLPFTYSYRELIAQAGLATVRAGLPDAFAGLLV 142
Cdd:cd05154   41 SAHDLEREYRVLRALAGTGVPVPRVLAL----CEDPSVLGAPFYVMERVDGRVLPDPLPRPDLSPEERRALARSLVDALA 116


                 ....
gi 262077088 143 ELHS 146
Cdd:cd05154  117 ALHS 120
 
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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