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Conserved domains on  [gi|1278161696|gb|PIX32262|]
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hypothetical protein COZ60_00055 [Candidatus Bathyarchaeota archaeon CG_4_8_14_3_um_filter_42_8]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PatZN super family cl34077
Acyl-CoA synthetase (NDP forming) [Energy production and conversion];
6-63 2.85e-22

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


The actual alignment was detected with superfamily member COG1042:

Pssm-ID: 440664 [Multi-domain]  Cd Length: 708  Bit Score: 88.64  E-value: 2.85e-22
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1278161696   6 YLDKIFNPQSVAIVGASDEEGTVGYALMKNFTEHGFEGKIYPVNIRKTEIFRLKSLPN 63
Cdd:COG1042     5 SLDALFRPRSVAVIGASDRPGKVGGRVLRNLLEGGFKGKIYPVNPKYDEVLGLPCYPS 62
 
Name Accession Description Interval E-value
PatZN COG1042
Acyl-CoA synthetase (NDP forming) [Energy production and conversion];
6-63 2.85e-22

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


Pssm-ID: 440664 [Multi-domain]  Cd Length: 708  Bit Score: 88.64  E-value: 2.85e-22
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1278161696   6 YLDKIFNPQSVAIVGASDEEGTVGYALMKNFTEHGFEGKIYPVNIRKTEIFRLKSLPN 63
Cdd:COG1042     5 SLDALFRPRSVAVIGASDRPGKVGGRVLRNLLEGGFKGKIYPVNPKYDEVLGLPCYPS 62
AcCoA-syn-alpha TIGR02717
acetyl coenzyme A synthetase (ADP forming), alpha domain; Although technically reversible, it ...
7-63 1.60e-19

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: 80.82  E-value: 1.60e-19
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1278161696   7 LDKIFNPQSVAIVGASDEEGTVGYALMKNFTEHGFEGKIYPVNIRKTEIFRLKSLPN 63
Cdd:TIGR02717   1 LEHLFNPKSVAVIGASRDPGKVGYAIMKNLIEGGYKGKIYPVNPKAGEILGVKAYPS 57
CoA_binding smart00881
CoA binding domain; This domain has a Rossmann fold and is found in a number of proteins ...
11-50 1.03e-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: 214881 [Multi-domain]  Cd Length: 100  Bit Score: 47.89  E-value: 1.03e-08
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|...
gi 1278161696   11 FNPQ-SVAIVGASDEEGTVGYALMKNFTEHG--FEGKIYPVNI 50
Cdd:smart00881   2 LNPNtSVAVVGASGNLGSFGLAVMRNLLEYGtkFVGGVYPGKV 44
CoA_binding_2 pfam13380
CoA binding domain; This domain has a Rossmann fold and is found in a number of proteins ...
15-56 2.04e-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: 433162 [Multi-domain]  Cd Length: 116  Bit Score: 47.15  E-value: 2.04e-08
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 1278161696  15 SVAIVGASDEEGTVGYALMKNFTEHGFEgkIYPVNIRKTEIF 56
Cdd:pfam13380   2 TIAVVGASPNPGRPGYKVARYLLEHGYP--VIPVNPKAKEIL 41
 
Name Accession Description Interval E-value
PatZN COG1042
Acyl-CoA synthetase (NDP forming) [Energy production and conversion];
6-63 2.85e-22

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


Pssm-ID: 440664 [Multi-domain]  Cd Length: 708  Bit Score: 88.64  E-value: 2.85e-22
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1278161696   6 YLDKIFNPQSVAIVGASDEEGTVGYALMKNFTEHGFEGKIYPVNIRKTEIFRLKSLPN 63
Cdd:COG1042     5 SLDALFRPRSVAVIGASDRPGKVGGRVLRNLLEGGFKGKIYPVNPKYDEVLGLPCYPS 62
AcCoA-syn-alpha TIGR02717
acetyl coenzyme A synthetase (ADP forming), alpha domain; Although technically reversible, it ...
7-63 1.60e-19

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: 80.82  E-value: 1.60e-19
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1278161696   7 LDKIFNPQSVAIVGASDEEGTVGYALMKNFTEHGFEGKIYPVNIRKTEIFRLKSLPN 63
Cdd:TIGR02717   1 LEHLFNPKSVAVIGASRDPGKVGYAIMKNLIEGGYKGKIYPVNPKAGEILGVKAYPS 57
CoA_binding smart00881
CoA binding domain; This domain has a Rossmann fold and is found in a number of proteins ...
11-50 1.03e-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: 214881 [Multi-domain]  Cd Length: 100  Bit Score: 47.89  E-value: 1.03e-08
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|...
gi 1278161696   11 FNPQ-SVAIVGASDEEGTVGYALMKNFTEHG--FEGKIYPVNI 50
Cdd:smart00881   2 LNPNtSVAVVGASGNLGSFGLAVMRNLLEYGtkFVGGVYPGKV 44
CoA_binding_2 pfam13380
CoA binding domain; This domain has a Rossmann fold and is found in a number of proteins ...
15-56 2.04e-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: 433162 [Multi-domain]  Cd Length: 116  Bit Score: 47.15  E-value: 2.04e-08
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 1278161696  15 SVAIVGASDEEGTVGYALMKNFTEHGFEgkIYPVNIRKTEIF 56
Cdd:pfam13380   2 TIAVVGASPNPGRPGYKVARYLLEHGYP--VIPVNPKAKEIL 41
YccU COG1832
Predicted CoA-binding protein [General function prediction only];
12-62 2.82e-05

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


Pssm-ID: 441437 [Multi-domain]  Cd Length: 138  Bit Score: 39.34  E-value: 2.82e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1278161696  12 NPQSVAIVGASDEEGTVGYALMKNFTEHGFegKIYPVNIRKTEIF------RLKSLP 62
Cdd:COG1832    15 SAKTIAVVGLSPNPERPSYYVAKYLQRHGY--RVIPVNPGAKEILgekvyaSLADIP 69
 
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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