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Conserved domains on  [gi|1490162280|gb|RKY44243|]
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MAG: CoA-binding protein [Candidatus Omnitrophica bacterium]

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 ...
 12-126 3.32e-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: 145.76  E-value: 3.32e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490162280  12 KSFAVVGSFRNETKYAYQILKTLKNKGYEAYPVNPRLKEVEGLPCYPTIKDIPVVCDVVNIVTPPRITERIVRECKEKGV 91
Cdd:pfam13380   1 KTIAVVGASPNPGRPGYKVARYLLEHGYPVIPVNPKAKEILGEPVYPSLADPPEPVDLVDVFRPPEAVPEIVEEALALGA 80

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1490162280  92 KRVWLQPGAESQEAIKFCEDNGIKVIHSICVMMEG 126
Cdd:pfam13380  81 KAVWLQPGIENEEAAAIARAAGIRVVGDRCLGVEH 115
 
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 ...
 12-126 3.32e-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: 145.76  E-value: 3.32e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490162280  12 KSFAVVGSFRNETKYAYQILKTLKNKGYEAYPVNPRLKEVEGLPCYPTIKDIPVVCDVVNIVTPPRITERIVRECKEKGV 91
Cdd:pfam13380   1 KTIAVVGASPNPGRPGYKVARYLLEHGYPVIPVNPKAKEILGEPVYPSLADPPEPVDLVDVFRPPEAVPEIVEEALALGA 80

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1490162280  92 KRVWLQPGAESQEAIKFCEDNGIKVIHSICVMMEG 126
Cdd:pfam13380  81 KAVWLQPGIENEEAAAIARAAGIRVVGDRCLGVEH 115
YccU COG1832
Predicted CoA-binding protein [General function prediction only];
2-125 5.43e-40

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


Pssm-ID: 441437 [Multi-domain]  Cd Length: 138  Bit Score: 130.63  E-value: 5.43e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490162280   2 EELIRDFLRQ-KSFAVVGSFRNETKYAYQILKTLKNKGYEAYPVNPRLKEVEGLPCYPTIKDIPVVCDVVNIVTPPRITE 80
Cdd:COG1832     6 DEEIREILKSaKTIAVVGLSPNPERPSYYVAKYLQRHGYRVIPVNPGAKEILGEKVYASLADIPEPVDIVDVFRRSEAVP 85

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1490162280  81 RIVRECKEKGVKRVWLQPGAESQEAIKFCEDNGIKVIHSICVMME 125
Cdd:COG1832    86 EIVDEAIAIGAKVVWLQLGVVNEEAAERAEAAGLDVVMDRCPKIE 130
AcCoA-syn-alpha TIGR02717
acetyl coenzyme A synthetase (ADP forming), alpha domain; Although technically reversible, it ...
 7-117 9.32e-23

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: 91.99  E-value: 9.32e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490162280   7 DFLRQKSFAVVGSFRNETKYAYQILKTLKNKGY--EAYPVNPRLKEVEGLPCYPTIKDIPVVCDVVNIVTPPRITERIVR 84
Cdd:TIGR02717   3 HLFNPKSVAVIGASRDPGKVGYAIMKNLIEGGYkgKIYPVNPKAGEILGVKAYPSVLEIPDPVDLAVIVVPAKYVPQVVE 82

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1490162280  85 ECKEKGVKRVWL---------QPGAE-SQEAIKFCEDNGIKVI 117
Cdd:TIGR02717  83 ECGEKGVKGAVVitagfkevgEEGAElEQELVEIARKYGMRLL 125
CoA_binding smart00881
CoA binding domain; This domain has a Rossmann fold and is found in a number of proteins ...
 10-99 9.39e-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: 70.23  E-value: 9.39e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490162280   10 RQKSFAVVGSFRNETKYAYQILKTLKNKGYE-AYPVNPRL--KEVEGLPCYPTIKDIP--VVCDVVNIVTPPRITERIVR 84
Cdd:smart00881   4 PNTSVAVVGASGNLGSFGLAVMRNLLEYGTKfVGGVYPGKvgPKVDGVPVYDSVAEAPeeTGVDVAVIFVPAEAAPDAID 83

                           90
                   ....*....|....*.
gi 1490162280   85 ECKEKGVKR-VWLQPG 99
Cdd:smart00881  84 EAIEAGIKGiVVITEG 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 ...
 12-126 3.32e-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: 145.76  E-value: 3.32e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490162280  12 KSFAVVGSFRNETKYAYQILKTLKNKGYEAYPVNPRLKEVEGLPCYPTIKDIPVVCDVVNIVTPPRITERIVRECKEKGV 91
Cdd:pfam13380   1 KTIAVVGASPNPGRPGYKVARYLLEHGYPVIPVNPKAKEILGEPVYPSLADPPEPVDLVDVFRPPEAVPEIVEEALALGA 80

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1490162280  92 KRVWLQPGAESQEAIKFCEDNGIKVIHSICVMMEG 126
Cdd:pfam13380  81 KAVWLQPGIENEEAAAIARAAGIRVVGDRCLGVEH 115
YccU COG1832
Predicted CoA-binding protein [General function prediction only];
2-125 5.43e-40

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


Pssm-ID: 441437 [Multi-domain]  Cd Length: 138  Bit Score: 130.63  E-value: 5.43e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490162280   2 EELIRDFLRQ-KSFAVVGSFRNETKYAYQILKTLKNKGYEAYPVNPRLKEVEGLPCYPTIKDIPVVCDVVNIVTPPRITE 80
Cdd:COG1832     6 DEEIREILKSaKTIAVVGLSPNPERPSYYVAKYLQRHGYRVIPVNPGAKEILGEKVYASLADIPEPVDIVDVFRRSEAVP 85

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1490162280  81 RIVRECKEKGVKRVWLQPGAESQEAIKFCEDNGIKVIHSICVMME 125
Cdd:COG1832    86 EIVDEAIAIGAKVVWLQLGVVNEEAAERAEAAGLDVVMDRCPKIE 130
PatZN COG1042
Acyl-CoA synthetase (NDP forming) [Energy production and conversion];
8-117 6.78e-25

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


Pssm-ID: 440664 [Multi-domain]  Cd Length: 708  Bit Score: 98.66  E-value: 6.78e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490162280   8 FLRQKSFAVVGSFRNETKYAYQILKTLKNKGYEA--YPVNPRLKEVEGLPCYPTIKDIPVVCDVVNIVTPPRITERIVRE 85
Cdd:COG1042     9 LFRPRSVAVIGASDRPGKVGGRVLRNLLEGGFKGkiYPVNPKYDEVLGLPCYPSVADLPEPPDLAVIAVPAETVPDVVEE 88

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1490162280  86 CKEKGVKRV---------WLQPGAESQEAIK-FCEDNGIKVI 117
Cdd:COG1042    89 CGEKGVKAAvvisagfaeTGEEGAALEQELLeIARRYGMRLL 130
AcCoA-syn-alpha TIGR02717
acetyl coenzyme A synthetase (ADP forming), alpha domain; Although technically reversible, it ...
 7-117 9.32e-23

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: 91.99  E-value: 9.32e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490162280   7 DFLRQKSFAVVGSFRNETKYAYQILKTLKNKGY--EAYPVNPRLKEVEGLPCYPTIKDIPVVCDVVNIVTPPRITERIVR 84
Cdd:TIGR02717   3 HLFNPKSVAVIGASRDPGKVGYAIMKNLIEGGYkgKIYPVNPKAGEILGVKAYPSVLEIPDPVDLAVIVVPAKYVPQVVE 82

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1490162280  85 ECKEKGVKRVWL---------QPGAE-SQEAIKFCEDNGIKVI 117
Cdd:TIGR02717  83 ECGEKGVKGAVVitagfkevgEEGAElEQELVEIARKYGMRLL 125
CoA_binding smart00881
CoA binding domain; This domain has a Rossmann fold and is found in a number of proteins ...
 10-99 9.39e-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: 70.23  E-value: 9.39e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490162280   10 RQKSFAVVGSFRNETKYAYQILKTLKNKGYE-AYPVNPRL--KEVEGLPCYPTIKDIP--VVCDVVNIVTPPRITERIVR 84
Cdd:smart00881   4 PNTSVAVVGASGNLGSFGLAVMRNLLEYGTKfVGGVYPGKvgPKVDGVPVYDSVAEAPeeTGVDVAVIFVPAEAAPDAID 83

                           90
                   ....*....|....*.
gi 1490162280   85 ECKEKGVKR-VWLQPG 99
Cdd:smart00881  84 EAIEAGIKGiVVITEG 99
CoA_binding pfam02629
CoA binding domain; This domain has a Rossmann fold and is found in a number of proteins ...
 41-95 9.15e-08

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: 46.82  E-value: 9.15e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1490162280  41 AYPVNPRL--KEVEGLPCYPTIKDIP--VVCDVVNIVTPPRITERIVRECKEKGVKRVW 95
Cdd:pfam02629  34 VFGVNPGKggTEILGIPVYNSVDELEekTGVDVAVITVPAPFAQEAIDELVDAGIKGIV 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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