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Conserved domains on  [gi|1083445303|gb|OGF51184|]
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MAG: CoA-binding protein [Candidatus Firestonebacteria bacterium RIFOXYA2_FULL_40_8]

Protein Classification

CoA-binding protein( domain architecture ID 10596747)

CoA-binding protein similar to Escherichia coli YccU and Bacillus subtilis YneT

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
CoA_binding_2 pfam13380
CoA binding domain; This domain has a Rossmann fold and is found in a number of proteins ...
 13-125 9.35e-49

CoA binding domain; This domain has a Rossmann fold and is found in a number of proteins including succinyl CoA synthetases, malate and ATP-citrate ligases.


:

Pssm-ID: 433162 [Multi-domain]  Cd Length: 116  Bit Score: 151.54  E-value: 9.35e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083445303  13 KVFAVVGASSNPEKYGYTITKNLLDRGYKVYPVNPRLEELHGVKCYKSLTDLPEKPDVVDVVIPPKLTEELMKEVLKLGL 92
Cdd:pfam13380   1 KTIAVVGASPNPGRPGYKVARYLLEHGYPVIPVNPKAKEILGEPVYPSLADPPEPVDLVDVFRPPEAVPEIVEEALALGA 80

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1083445303  93 TRVWMQPGAESSAAVEFCEKNGIKVIHGACVMM 125
Cdd:pfam13380  81 KAVWLQPGIENEEAAAIARAAGIRVVGDRCLGV 113
 
Name Accession Description Interval E-value
CoA_binding_2 pfam13380
CoA binding domain; This domain has a Rossmann fold and is found in a number of proteins ...
 13-125 9.35e-49

CoA binding domain; This domain has a Rossmann fold and is found in a number of proteins including succinyl CoA synthetases, malate and ATP-citrate ligases.


Pssm-ID: 433162 [Multi-domain]  Cd Length: 116  Bit Score: 151.54  E-value: 9.35e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083445303  13 KVFAVVGASSNPEKYGYTITKNLLDRGYKVYPVNPRLEELHGVKCYKSLTDLPEKPDVVDVVIPPKLTEELMKEVLKLGL 92
Cdd:pfam13380   1 KTIAVVGASPNPGRPGYKVARYLLEHGYPVIPVNPKAKEILGEPVYPSLADPPEPVDLVDVFRPPEAVPEIVEEALALGA 80

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1083445303  93 TRVWMQPGAESSAAVEFCEKNGIKVIHGACVMM 125
Cdd:pfam13380  81 KAVWLQPGIENEEAAAIARAAGIRVVGDRCLGV 113
YccU COG1832
Predicted CoA-binding protein [General function prediction only];
1-124 3.76e-44

Predicted CoA-binding protein [General function prediction only];


Pssm-ID: 441437 [Multi-domain]  Cd Length: 138  Bit Score: 140.65  E-value: 3.76e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083445303   1 MDASLITEFMQQ-KVFAVVGASSNPEKYGYTITKNLLDRGYKVYPVNPRLEELHGVKCYKSLTDLPEKPDVVDVVIPPKL 79
Cdd:COG1832     4 PDDEEIREILKSaKTIAVVGLSPNPERPSYYVAKYLQRHGYRVIPVNPGAKEILGEKVYASLADIPEPVDIVDVFRRSEA 83

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1083445303  80 TEELMKEVLKLGLTRVWMQPGAESSAAVEFCEKNGIKVIHGACVM 124
Cdd:COG1832    84 VPEIVDEAIAIGAKVVWLQLGVVNEEAAERAEAAGLDVVMDRCPK 128
AcCoA-syn-alpha TIGR02717
acetyl coenzyme A synthetase (ADP forming), alpha domain; Although technically reversible, it ...
 13-93 4.90e-25

acetyl coenzyme A synthetase (ADP forming), alpha domain; Although technically reversible, it is believed that this group of ADP-dependent acetyl-CoA synthetases (ACS) act in the direction of acetate and ATP production in the organisms in which it has been characterized. In most species this protein exists as a fused alpha-beta domain polypeptide. In Pyrococcus and related species, however the domains exist as separate polypeptides. This model represents the alpha (N-terminal) domain. In Pyrococcus and related species there appears to have been the development of a paralogous family such that four other proteins are close relatives. In reference, one of these (along with its beta-domain partner) was characterized as ACS-II showing specificity for phenylacetyl-CoA. This model has been constructed to exclude these non-ACS-I paralogs. This may result in new, authentic ACS-I sequences falling below the trusted cutoff.


Pssm-ID: 131764 [Multi-domain]  Cd Length: 447  Bit Score: 97.77  E-value: 4.90e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083445303  13 KVFAVVGASSNPEKYGYTITKNLLDRGY--KVYPVNPRLEELHGVKCYKSLTDLPEKPDVVDVVIPPKLTEELMKEVLKL 90
Cdd:TIGR02717   8 KSVAVIGASRDPGKVGYAIMKNLIEGGYkgKIYPVNPKAGEILGVKAYPSVLEIPDPVDLAVIVVPAKYVPQVVEECGEK 87


                  ...
gi 1083445303  91 GLT 93
Cdd:TIGR02717  88 GVK 90
CoA_binding smart00881
CoA binding domain; This domain has a Rossmann fold and is found in a number of proteins ...
 16-100 1.15e-17

CoA binding domain; This domain has a Rossmann fold and is found in a number of proteins including succinyl CoA synthetases, malate and ATP-citrate ligases.


Pssm-ID: 214881 [Multi-domain]  Cd Length: 100  Bit Score: 72.16  E-value: 1.15e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083445303   16 AVVGASSNPEKYGYTITKNLLDRGYK-VYPVNPRL--EELHGVKCYKSLTDLPEK--PDVVDVVIPPKLTEELMKEVLKL 90
Cdd:smart00881   9 AVVGASGNLGSFGLAVMRNLLEYGTKfVGGVYPGKvgPKVDGVPVYDSVAEAPEEtgVDVAVIFVPAEAAPDAIDEAIEA 88

                           90
                   ....*....|.
gi 1083445303   91 GLTR-VWMQPG 100
Cdd:smart00881  89 GIKGiVVITEG 99
PRK06182 PRK06182
short chain dehydrogenase; Validated
 10-75 7.91e-03

short chain dehydrogenase; Validated


Pssm-ID: 180448 [Multi-domain]  Cd Length: 273  Bit Score: 34.55  E-value: 7.91e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1083445303  10 MQQKVFAVVGASSNpekYGYTITKNLLDRGYKVYPVNPRLEEL-----HGVKCYK-SLTDLPEKPDVVDVVI 75
Cdd:PRK06182    1 MQKKVALVTGASSG---IGKATARRLAAQGYTVYGAARRVDKMedlasLGVHPLSlDVTDEASIKAAVDTII 69
PI-PLCc_GDPD_SF_unchar1 cd08583
Uncharacterized hypothetical proteins similar to the catalytic domains of ...
 55-118 9.56e-03

Uncharacterized hypothetical proteins similar to the catalytic domains of Phosphoinositide-specific phospholipaseand Glycerophosphodiester phosphodiesterases; This subfamily corresponds to a group of uncharacterized hypothetical proteins similar to the catalytic domains of Phosphoinositide-specific phospholipase C (PI-PLC), and glycerophosphodiester phosphodiesterases (GP-GDE), and also sphingomyelinases D (SMases D) and similar proteins. They hydrolyze the 3'-5' phosphodiester bonds in different substrates, utilizing a similar mechanism of general base and acid catalysis involving two conserved histidine residues.


Pssm-ID: 176525 [Multi-domain]  Cd Length: 237  Bit Score: 34.58  E-value: 9.56e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1083445303  55 VKCYKSLTDLPEK--PDVVDVVIPPKLTEELMKEV-----LKLGLTRVWMQPGAESSAAVEFCEKNGIKVI 118
Cdd:cd08583   116 KKLYEYIVKEAKEvdPDLLDRVIPQIYNEEMYEAImsiypFKSVIYTLYRQDSIRLDEIIAFCYENGIKAV 186
 
Name Accession Description Interval E-value
CoA_binding_2 pfam13380
CoA binding domain; This domain has a Rossmann fold and is found in a number of proteins ...
 13-125 9.35e-49

CoA binding domain; This domain has a Rossmann fold and is found in a number of proteins including succinyl CoA synthetases, malate and ATP-citrate ligases.


Pssm-ID: 433162 [Multi-domain]  Cd Length: 116  Bit Score: 151.54  E-value: 9.35e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083445303  13 KVFAVVGASSNPEKYGYTITKNLLDRGYKVYPVNPRLEELHGVKCYKSLTDLPEKPDVVDVVIPPKLTEELMKEVLKLGL 92
Cdd:pfam13380   1 KTIAVVGASPNPGRPGYKVARYLLEHGYPVIPVNPKAKEILGEPVYPSLADPPEPVDLVDVFRPPEAVPEIVEEALALGA 80

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1083445303  93 TRVWMQPGAESSAAVEFCEKNGIKVIHGACVMM 125
Cdd:pfam13380  81 KAVWLQPGIENEEAAAIARAAGIRVVGDRCLGV 113
YccU COG1832
Predicted CoA-binding protein [General function prediction only];
1-124 3.76e-44

Predicted CoA-binding protein [General function prediction only];


Pssm-ID: 441437 [Multi-domain]  Cd Length: 138  Bit Score: 140.65  E-value: 3.76e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083445303   1 MDASLITEFMQQ-KVFAVVGASSNPEKYGYTITKNLLDRGYKVYPVNPRLEELHGVKCYKSLTDLPEKPDVVDVVIPPKL 79
Cdd:COG1832     4 PDDEEIREILKSaKTIAVVGLSPNPERPSYYVAKYLQRHGYRVIPVNPGAKEILGEKVYASLADIPEPVDIVDVFRRSEA 83

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1083445303  80 TEELMKEVLKLGLTRVWMQPGAESSAAVEFCEKNGIKVIHGACVM 124
Cdd:COG1832    84 VPEIVDEAIAIGAKVVWLQLGVVNEEAAERAEAAGLDVVMDRCPK 128
PatZN COG1042
Acyl-CoA synthetase (NDP forming) [Energy production and conversion];
16-91 9.16e-28

Acyl-CoA synthetase (NDP forming) [Energy production and conversion];


Pssm-ID: 440664 [Multi-domain]  Cd Length: 708  Bit Score: 106.36  E-value: 9.16e-28
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1083445303  16 AVVGASSNPEKYGYTITKNLLDRGY--KVYPVNPRLEELHGVKCYKSLTDLPEKPDVVDVVIPPKLTEELMKEVLKLG 91
Cdd:COG1042    16 AVIGASDRPGKVGGRVLRNLLEGGFkgKIYPVNPKYDEVLGLPCYPSVADLPEPPDLAVIAVPAETVPDVVEECGEKG 93
AcCoA-syn-alpha TIGR02717
acetyl coenzyme A synthetase (ADP forming), alpha domain; Although technically reversible, it ...
 13-93 4.90e-25

acetyl coenzyme A synthetase (ADP forming), alpha domain; Although technically reversible, it is believed that this group of ADP-dependent acetyl-CoA synthetases (ACS) act in the direction of acetate and ATP production in the organisms in which it has been characterized. In most species this protein exists as a fused alpha-beta domain polypeptide. In Pyrococcus and related species, however the domains exist as separate polypeptides. This model represents the alpha (N-terminal) domain. In Pyrococcus and related species there appears to have been the development of a paralogous family such that four other proteins are close relatives. In reference, one of these (along with its beta-domain partner) was characterized as ACS-II showing specificity for phenylacetyl-CoA. This model has been constructed to exclude these non-ACS-I paralogs. This may result in new, authentic ACS-I sequences falling below the trusted cutoff.


Pssm-ID: 131764 [Multi-domain]  Cd Length: 447  Bit Score: 97.77  E-value: 4.90e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083445303  13 KVFAVVGASSNPEKYGYTITKNLLDRGY--KVYPVNPRLEELHGVKCYKSLTDLPEKPDVVDVVIPPKLTEELMKEVLKL 90
Cdd:TIGR02717   8 KSVAVIGASRDPGKVGYAIMKNLIEGGYkgKIYPVNPKAGEILGVKAYPSVLEIPDPVDLAVIVVPAKYVPQVVEECGEK 87


                  ...
gi 1083445303  91 GLT 93
Cdd:TIGR02717  88 GVK 90
CoA_binding smart00881
CoA binding domain; This domain has a Rossmann fold and is found in a number of proteins ...
 16-100 1.15e-17

CoA binding domain; This domain has a Rossmann fold and is found in a number of proteins including succinyl CoA synthetases, malate and ATP-citrate ligases.


Pssm-ID: 214881 [Multi-domain]  Cd Length: 100  Bit Score: 72.16  E-value: 1.15e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083445303   16 AVVGASSNPEKYGYTITKNLLDRGYK-VYPVNPRL--EELHGVKCYKSLTDLPEK--PDVVDVVIPPKLTEELMKEVLKL 90
Cdd:smart00881   9 AVVGASGNLGSFGLAVMRNLLEYGTKfVGGVYPGKvgPKVDGVPVYDSVAEAPEEtgVDVAVIFVPAEAAPDAIDEAIEA 88

                           90
                   ....*....|.
gi 1083445303   91 GLTR-VWMQPG 100
Cdd:smart00881  89 GIKGiVVITEG 99
CoA_binding pfam02629
CoA binding domain; This domain has a Rossmann fold and is found in a number of proteins ...
 16-96 7.90e-09

CoA binding domain; This domain has a Rossmann fold and is found in a number of proteins including succinyl CoA synthetases, malate and ATP-citrate ligases.


Pssm-ID: 396961 [Multi-domain]  Cd Length: 97  Bit Score: 49.51  E-value: 7.90e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083445303  16 AVVGASSNPEKYGYTITKNLLDRGYK-VYPVNPRL--EELHGVKCYKSLTDLPEKPDvVDVVI---PPKLTEELMKEVLK 89
Cdd:pfam02629   7 IVIGAGGLGIQGLNYHFIQMLGYGIKmVFGVNPGKggTEILGIPVYNSVDELEEKTG-VDVAVitvPAPFAQEAIDELVD 85


                  ....*..
gi 1083445303  90 LGLTRVW 96
Cdd:pfam02629  86 AGIKGIV 92
PRK06182 PRK06182
short chain dehydrogenase; Validated
 10-75 7.91e-03

short chain dehydrogenase; Validated


Pssm-ID: 180448 [Multi-domain]  Cd Length: 273  Bit Score: 34.55  E-value: 7.91e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1083445303  10 MQQKVFAVVGASSNpekYGYTITKNLLDRGYKVYPVNPRLEEL-----HGVKCYK-SLTDLPEKPDVVDVVI 75
Cdd:PRK06182    1 MQKKVALVTGASSG---IGKATARRLAAQGYTVYGAARRVDKMedlasLGVHPLSlDVTDEASIKAAVDTII 69
MviM COG0673
Predicted dehydrogenase [General function prediction only];
48-117 8.96e-03

Predicted dehydrogenase [General function prediction only];


Pssm-ID: 440437 [Multi-domain]  Cd Length: 295  Bit Score: 34.51  E-value: 8.96e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1083445303  48 RLEELHGVKCYKSLTDL--PEKPDVVDVVIPPKLTEELMKEVLKLGLTrVWMQ-PGA----ESSAAVEFCEKNGIKV 117
Cdd:COG0673    43 AFAEEYGVRVYTDYEELlaDPDIDAVVIATPNHLHAELAIAALEAGKH-VLCEkPLAltleEARELVAAAEEAGVVL 118
PI-PLCc_GDPD_SF_unchar1 cd08583
Uncharacterized hypothetical proteins similar to the catalytic domains of ...
 55-118 9.56e-03

Uncharacterized hypothetical proteins similar to the catalytic domains of Phosphoinositide-specific phospholipaseand Glycerophosphodiester phosphodiesterases; This subfamily corresponds to a group of uncharacterized hypothetical proteins similar to the catalytic domains of Phosphoinositide-specific phospholipase C (PI-PLC), and glycerophosphodiester phosphodiesterases (GP-GDE), and also sphingomyelinases D (SMases D) and similar proteins. They hydrolyze the 3'-5' phosphodiester bonds in different substrates, utilizing a similar mechanism of general base and acid catalysis involving two conserved histidine residues.


Pssm-ID: 176525 [Multi-domain]  Cd Length: 237  Bit Score: 34.58  E-value: 9.56e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1083445303  55 VKCYKSLTDLPEK--PDVVDVVIPPKLTEELMKEV-----LKLGLTRVWMQPGAESSAAVEFCEKNGIKVI 118
Cdd:cd08583   116 KKLYEYIVKEAKEvdPDLLDRVIPQIYNEEMYEAImsiypFKSVIYTLYRQDSIRLDEIIAFCYENGIKAV 186
 
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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