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Conserved domains on  [gi|1483849152|gb|RJS80529|]
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CoA-binding protein [Candidatus Bathyarchaeota archaeon]

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 ...
 16-127 5.00e-46

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: 144.99  E-value: 5.00e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1483849152  16 FAVIGASRDPKKYGHQVYKDLRKAGYKVYPVNPNADEILGDKCYPSLESLPEKPDVVDIVVPPKITEQIVKTCKKLGIRM 95
Cdd:pfam13380   3 IAVVGASPNPGRPGYKVARYLLEHGYPVIPVNPKAKEILGEPVYPSLADPPEPVDLVDVFRPPEAVPEIVEEALALGAKA 82

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1483849152  96 IWMQPGSESEAAIRFCEENGMDVVHGVCVMVE 127
Cdd:pfam13380  83 VWLQPGIENEEAAAIARAAGIRVVGDRCLGVE 114
 
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 ...
 16-127 5.00e-46

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: 144.99  E-value: 5.00e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1483849152  16 FAVIGASRDPKKYGHQVYKDLRKAGYKVYPVNPNADEILGDKCYPSLESLPEKPDVVDIVVPPKITEQIVKTCKKLGIRM 95
Cdd:pfam13380   3 IAVVGASPNPGRPGYKVARYLLEHGYPVIPVNPKAKEILGEPVYPSLADPPEPVDLVDVFRPPEAVPEIVEEALALGAKA 82

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1483849152  96 IWMQPGSESEAAIRFCEENGMDVVHGVCVMVE 127
Cdd:pfam13380  83 VWLQPGIENEEAAAIARAAGIRVVGDRCLGVE 114
YccU COG1832
Predicted CoA-binding protein [General function prediction only];
1-127 5.37e-46

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


Pssm-ID: 441437 [Multi-domain]  Cd Length: 138  Bit Score: 145.66  E-value: 5.37e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1483849152   1 MDEKLILEFLNKKNVFAVIGASRDPKKYGHQVYKDLRKAGYKVYPVNPNADEILGDKCYPSLESLPEKPDVVDIVVPPKI 80
Cdd:COG1832     4 PDDEEIREILKSAKTIAVVGLSPNPERPSYYVAKYLQRHGYRVIPVNPGAKEILGEKVYASLADIPEPVDIVDVFRRSEA 83

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1483849152  81 TEQIVKTCKKLGIRMIWMQPGSESEAAIRFCEENGMDVVHGVCVMVE 127
Cdd:COG1832    84 VPEIVDEAIAIGAKVVWLQLGVVNEEAAERAEAAGLDVVMDRCPKIE 130
AcCoA-syn-alpha TIGR02717
acetyl coenzyme A synthetase (ADP forming), alpha domain; Although technically reversible, it ...
 7-94 9.18e-27

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: 102.77  E-value: 9.18e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1483849152   7 LEFLNKKNVFAVIGASRDPKKYGHQVYKDLRKAGY--KVYPVNPNADEILGDKCYPSLESLPEKPDVVDIVVPPKITEQI 84
Cdd:TIGR02717   1 LEHLFNPKSVAVIGASRDPGKVGYAIMKNLIEGGYkgKIYPVNPKAGEILGVKAYPSVLEIPDPVDLAVIVVPAKYVPQV 80

                          90
                  ....*....|
gi 1483849152  85 VKTCKKLGIR 94
Cdd:TIGR02717  81 VEECGEKGVK 90
CoA_binding smart00881
CoA binding domain; This domain has a Rossmann fold and is found in a number of proteins ...
 9-101 7.94e-20

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: 77.94  E-value: 7.94e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1483849152    9 FLNKKNVFAVIGASRDPKKYGHQVYKDLRKAG----YKVYP--VNPNADEIlgdKCYPSLESLPEK--PDVVDIVVPPKI 80
Cdd:smart00881   1 LLNPNTSVAVVGASGNLGSFGLAVMRNLLEYGtkfvGGVYPgkVGPKVDGV---PVYDSVAEAPEEtgVDVAVIFVPAEA 77

                           90       100
                   ....*....|....*....|..
gi 1483849152   81 TEQIVKTCKKLGIRMI-WMQPG 101
Cdd:smart00881  78 APDAIDEAIEAGIKGIvVITEG 99
 
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 ...
 16-127 5.00e-46

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: 144.99  E-value: 5.00e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1483849152  16 FAVIGASRDPKKYGHQVYKDLRKAGYKVYPVNPNADEILGDKCYPSLESLPEKPDVVDIVVPPKITEQIVKTCKKLGIRM 95
Cdd:pfam13380   3 IAVVGASPNPGRPGYKVARYLLEHGYPVIPVNPKAKEILGEPVYPSLADPPEPVDLVDVFRPPEAVPEIVEEALALGAKA 82

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1483849152  96 IWMQPGSESEAAIRFCEENGMDVVHGVCVMVE 127
Cdd:pfam13380  83 VWLQPGIENEEAAAIARAAGIRVVGDRCLGVE 114
YccU COG1832
Predicted CoA-binding protein [General function prediction only];
1-127 5.37e-46

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


Pssm-ID: 441437 [Multi-domain]  Cd Length: 138  Bit Score: 145.66  E-value: 5.37e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1483849152   1 MDEKLILEFLNKKNVFAVIGASRDPKKYGHQVYKDLRKAGYKVYPVNPNADEILGDKCYPSLESLPEKPDVVDIVVPPKI 80
Cdd:COG1832     4 PDDEEIREILKSAKTIAVVGLSPNPERPSYYVAKYLQRHGYRVIPVNPGAKEILGEKVYASLADIPEPVDIVDVFRRSEA 83

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1483849152  81 TEQIVKTCKKLGIRMIWMQPGSESEAAIRFCEENGMDVVHGVCVMVE 127
Cdd:COG1832    84 VPEIVDEAIAIGAKVVWLQLGVVNEEAAERAEAAGLDVVMDRCPKIE 130
PatZN COG1042
Acyl-CoA synthetase (NDP forming) [Energy production and conversion];
9-94 8.35e-30

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


Pssm-ID: 440664 [Multi-domain]  Cd Length: 708  Bit Score: 112.53  E-value: 8.35e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1483849152   9 FLNKKNVfAVIGASRDPKKYGHQVYKDLRKAGY--KVYPVNPNADEILGDKCYPSLESLPEKPDVVDIVVPPKITEQIVK 86
Cdd:COG1042     9 LFRPRSV-AVIGASDRPGKVGGRVLRNLLEGGFkgKIYPVNPKYDEVLGLPCYPSVADLPEPPDLAVIAVPAETVPDVVE 87


                  ....*...
gi 1483849152  87 TCKKLGIR 94
Cdd:COG1042    88 ECGEKGVK 95
AcCoA-syn-alpha TIGR02717
acetyl coenzyme A synthetase (ADP forming), alpha domain; Although technically reversible, it ...
 7-94 9.18e-27

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: 102.77  E-value: 9.18e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1483849152   7 LEFLNKKNVFAVIGASRDPKKYGHQVYKDLRKAGY--KVYPVNPNADEILGDKCYPSLESLPEKPDVVDIVVPPKITEQI 84
Cdd:TIGR02717   1 LEHLFNPKSVAVIGASRDPGKVGYAIMKNLIEGGYkgKIYPVNPKAGEILGVKAYPSVLEIPDPVDLAVIVVPAKYVPQV 80

                          90
                  ....*....|
gi 1483849152  85 VKTCKKLGIR 94
Cdd:TIGR02717  81 VEECGEKGVK 90
CoA_binding smart00881
CoA binding domain; This domain has a Rossmann fold and is found in a number of proteins ...
 9-101 7.94e-20

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: 77.94  E-value: 7.94e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1483849152    9 FLNKKNVFAVIGASRDPKKYGHQVYKDLRKAG----YKVYP--VNPNADEIlgdKCYPSLESLPEK--PDVVDIVVPPKI 80
Cdd:smart00881   1 LLNPNTSVAVVGASGNLGSFGLAVMRNLLEYGtkfvGGVYPgkVGPKVDGV---PVYDSVAEAPEEtgVDVAVIFVPAEA 77

                           90       100
                   ....*....|....*....|..
gi 1483849152   81 TEQIVKTCKKLGIRMI-WMQPG 101
Cdd:smart00881  78 APDAIDEAIEAGIKGIvVITEG 99
CoA_binding pfam02629
CoA binding domain; This domain has a Rossmann fold and is found in a number of proteins ...
 11-97 1.14e-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: 51.82  E-value: 1.14e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1483849152  11 NKKNVFAVIGASRDPKKYGHQVYKDLRKAGYK-VYPVNPN--ADEILGDKCYPSLESLPEK--PDVVDIVVPPKITEQIV 85
Cdd:pfam02629   1 DKDTKVIVIGAGGLGIQGLNYHFIQMLGYGIKmVFGVNPGkgGTEILGIPVYNSVDELEEKtgVDVAVITVPAPFAQEAI 80

                          90
                  ....*....|..
gi 1483849152  86 KTCKKLGIRMIW 97
Cdd:pfam02629  81 DELVDAGIKGIV 92
 
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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