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Conserved domains on  [gi|1576483137|gb|RZN39267|]
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CoA-binding protein [Methanophagales archaeon ANME-1-THS]

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 ...
 16-126 6.76e-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: 144.60  E-value: 6.76e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1576483137  16 FAVVGVSSNPEKYGHLVYKDLKEAGYTVYPINPHIDEVLGDHCYHSLSELPERPDVVDTVVPPHVTEEIVEECKELGIAR 95
Cdd:pfam13380   3 IAVVGASPNPGRPGYKVARYLLEHGYPVIPVNPKAKEILGEPVYPSLADPPEPVDLVDVFRPPEAVPEIVEEALALGAKA 82

                          90       100       110
                  ....*....|....*....|....*....|.
gi 1576483137  96 VWMQPGSESEKAIEFCRQNNIKVVHDLCVMV 126
Cdd:pfam13380  83 VWLQPGIENEEAAAIARAAGIRVVGDRCLGV 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 ...
 16-126 6.76e-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: 144.60  E-value: 6.76e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1576483137  16 FAVVGVSSNPEKYGHLVYKDLKEAGYTVYPINPHIDEVLGDHCYHSLSELPERPDVVDTVVPPHVTEEIVEECKELGIAR 95
Cdd:pfam13380   3 IAVVGASPNPGRPGYKVARYLLEHGYPVIPVNPKAKEILGEPVYPSLADPPEPVDLVDVFRPPEAVPEIVEEALALGAKA 82

                          90       100       110
                  ....*....|....*....|....*....|.
gi 1576483137  96 VWMQPGSESEKAIEFCRQNNIKVVHDLCVMV 126
Cdd:pfam13380  83 VWLQPGIENEEAAAIARAAGIRVVGDRCLGV 113
YccU COG1832
Predicted CoA-binding protein [General function prediction only];
1-126 7.25e-44

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


Pssm-ID: 441437 [Multi-domain]  Cd Length: 138  Bit Score: 140.26  E-value: 7.25e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1576483137   1 MNTDLIKEFLRKENVFAVVGVSSNPEKYGHLVYKDLKEAGYTVYPINPHIDEVLGDHCYHSLSELPERPDVVDTVVPPHV 80
Cdd:COG1832     4 PDDEEIREILKSAKTIAVVGLSPNPERPSYYVAKYLQRHGYRVIPVNPGAKEILGEKVYASLADIPEPVDIVDVFRRSEA 83

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1576483137  81 TEEIVEECKELGIARVWMQPGSESEKAIEFCRQNNIKVVHDLCVMV 126
Cdd:COG1832    84 VPEIVDEAIAIGAKVVWLQLGVVNEEAAERAEAAGLDVVMDRCPKI 129
CoA_binding smart00881
CoA binding domain; This domain has a Rossmann fold and is found in a number of proteins ...
 9-101 4.30e-18

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: 73.31  E-value: 4.30e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1576483137    9 FLRKENVFAVVGVSSNPEKYGHLVYKDLKEAG----YTVYP--INPHIDEVlgdHCYHSLSELPER--PDVVDTVVPPHV 80
Cdd:smart00881   1 LLNPNTSVAVVGASGNLGSFGLAVMRNLLEYGtkfvGGVYPgkVGPKVDGV---PVYDSVAEAPEEtgVDVAVIFVPAEA 77

                           90       100
                   ....*....|....*....|..
gi 1576483137   81 TEEIVEECKELGI-ARVWMQPG 101
Cdd:smart00881  78 APDAIDEAIEAGIkGIVVITEG 99
Tiki cd14789
Tiki homology domain antagonizes Wnt function via cleavage of amino-terminal residues; Tiki is ...
 6-43 2.41e-03

Tiki homology domain antagonizes Wnt function via cleavage of amino-terminal residues; Tiki is a membrane-associated metalloprotease that inhibits Wnt via the cleavage of its amino terminus, diminishing Wnt's binding to receptors. Wnt is essential in animal development and homeostasis. In xenopus, tiki is critical in head development. In human cells, TIKI inhibits Wnt-signaling, which is important in embryogenesis, homeostasis, and regeneration. Deregulation of WNT contributes to birth defects, cancer and various diseases. TIKI homology domains are part of the TraB family and are related to the Erythromycin esterase, GumN plant pathogens, RtxA toxins, and Campylobacter Jejuni heme-binding, Chan-like proteins. TraB/PrgY are identified in gut bacterium Enterococcus faecalis, but its function has not been well characterized. Plasmid-borne, TraB has been implicated in the regulation of pheromone sensitivity and specificity. Based on homology to TIKI activity, it has been proposed that TraB acts as a metalloprotease in the inactivation of mating pheromone. The TIKI/TraB family has 2 conserved GxxH motifs and conserved glutamate and arginine residues that may be catalytic.


Pssm-ID: 350614  Cd Length: 259  Bit Score: 36.12  E-value: 2.41e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 1576483137   6 IKEFLRKE-NVFAVVGVssnpekyGHLVYKD-----LKEAGYTV 43
Cdd:cd14789   223 IEALLKKGgTVFVAVGA-------GHLVGEDgllalLRKKGYTV 259
 
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 ...
 16-126 6.76e-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: 144.60  E-value: 6.76e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1576483137  16 FAVVGVSSNPEKYGHLVYKDLKEAGYTVYPINPHIDEVLGDHCYHSLSELPERPDVVDTVVPPHVTEEIVEECKELGIAR 95
Cdd:pfam13380   3 IAVVGASPNPGRPGYKVARYLLEHGYPVIPVNPKAKEILGEPVYPSLADPPEPVDLVDVFRPPEAVPEIVEEALALGAKA 82

                          90       100       110
                  ....*....|....*....|....*....|.
gi 1576483137  96 VWMQPGSESEKAIEFCRQNNIKVVHDLCVMV 126
Cdd:pfam13380  83 VWLQPGIENEEAAAIARAAGIRVVGDRCLGV 113
YccU COG1832
Predicted CoA-binding protein [General function prediction only];
1-126 7.25e-44

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


Pssm-ID: 441437 [Multi-domain]  Cd Length: 138  Bit Score: 140.26  E-value: 7.25e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1576483137   1 MNTDLIKEFLRKENVFAVVGVSSNPEKYGHLVYKDLKEAGYTVYPINPHIDEVLGDHCYHSLSELPERPDVVDTVVPPHV 80
Cdd:COG1832     4 PDDEEIREILKSAKTIAVVGLSPNPERPSYYVAKYLQRHGYRVIPVNPGAKEILGEKVYASLADIPEPVDIVDVFRRSEA 83

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1576483137  81 TEEIVEECKELGIARVWMQPGSESEKAIEFCRQNNIKVVHDLCVMV 126
Cdd:COG1832    84 VPEIVDEAIAIGAKVVWLQLGVVNEEAAERAEAAGLDVVMDRCPKI 129
PatZN COG1042
Acyl-CoA synthetase (NDP forming) [Energy production and conversion];
1-119 7.22e-25

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


Pssm-ID: 440664 [Multi-domain]  Cd Length: 708  Bit Score: 98.27  E-value: 7.22e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1576483137   1 MNTDLIKEFLRKENVfAVVGVSSNPEKYGHLVYKDLKEAGY--TVYPINPHIDEVLGDHCYHSLSELPERPDVVDTVVPP 78
Cdd:COG1042     1 MSTRSLDALFRPRSV-AVIGASDRPGKVGGRVLRNLLEGGFkgKIYPVNPKYDEVLGLPCYPSVADLPEPPDLAVIAVPA 79

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1576483137  79 HVTEEIVEECKELGIARV---------WMQPGSESEKAI-EFCRQNNIKVV 119
Cdd:COG1042    80 ETVPDVVEECGEKGVKAAvvisagfaeTGEEGAALEQELlEIARRYGMRLL 130
CoA_binding smart00881
CoA binding domain; This domain has a Rossmann fold and is found in a number of proteins ...
 9-101 4.30e-18

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: 73.31  E-value: 4.30e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1576483137    9 FLRKENVFAVVGVSSNPEKYGHLVYKDLKEAG----YTVYP--INPHIDEVlgdHCYHSLSELPER--PDVVDTVVPPHV 80
Cdd:smart00881   1 LLNPNTSVAVVGASGNLGSFGLAVMRNLLEYGtkfvGGVYPgkVGPKVDGV---PVYDSVAEAPEEtgVDVAVIFVPAEA 77

                           90       100
                   ....*....|....*....|..
gi 1576483137   81 TEEIVEECKELGI-ARVWMQPG 101
Cdd:smart00881  78 APDAIDEAIEAGIkGIVVITEG 99
Tiki cd14789
Tiki homology domain antagonizes Wnt function via cleavage of amino-terminal residues; Tiki is ...
 6-43 2.41e-03

Tiki homology domain antagonizes Wnt function via cleavage of amino-terminal residues; Tiki is a membrane-associated metalloprotease that inhibits Wnt via the cleavage of its amino terminus, diminishing Wnt's binding to receptors. Wnt is essential in animal development and homeostasis. In xenopus, tiki is critical in head development. In human cells, TIKI inhibits Wnt-signaling, which is important in embryogenesis, homeostasis, and regeneration. Deregulation of WNT contributes to birth defects, cancer and various diseases. TIKI homology domains are part of the TraB family and are related to the Erythromycin esterase, GumN plant pathogens, RtxA toxins, and Campylobacter Jejuni heme-binding, Chan-like proteins. TraB/PrgY are identified in gut bacterium Enterococcus faecalis, but its function has not been well characterized. Plasmid-borne, TraB has been implicated in the regulation of pheromone sensitivity and specificity. Based on homology to TIKI activity, it has been proposed that TraB acts as a metalloprotease in the inactivation of mating pheromone. The TIKI/TraB family has 2 conserved GxxH motifs and conserved glutamate and arginine residues that may be catalytic.


Pssm-ID: 350614  Cd Length: 259  Bit Score: 36.12  E-value: 2.41e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 1576483137   6 IKEFLRKE-NVFAVVGVssnpekyGHLVYKD-----LKEAGYTV 43
Cdd:cd14789   223 IEALLKKGgTVFVAVGA-------GHLVGEDgllalLRKKGYTV 259
 
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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