NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1200519375|gb|OUW32554|]
View 

hypothetical protein CBD31_01895, partial [Flavobacteriaceae bacterium TMED171]

Protein Classification

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
AANH_superfamily super family cl00292
Adenine nucleotide alpha hydrolase (AANH) superfamily; The adenine nucleotide alpha hydrolase ...
 29-60 2.21e-06

Adenine nucleotide alpha hydrolase (AANH) superfamily; The adenine nucleotide alpha hydrolase (AANH) superfamily includes N-type ATP PPases, ATP sulfurylases, universal stress response proteins (USPs), and electron transfer flavoproteins (ETFs). The domain forms an alpha/beta/alpha fold which binds to adenosine nucleotide.


The actual alignment was detected with superfamily member cd01991:

Pssm-ID: 469708 [Multi-domain]  Cd Length: 224  Bit Score: 42.26  E-value: 2.21e-06
                          10        20        30
                  ....*....|....*....|....*....|..
gi 1200519375  29 VGLMVSGGLDSAILLYALHKANPYAEIKTYCV 60
Cdd:cd01991     5 VGVLLSGGLDSSLIAALAARLLPETPIDLFTV 36
 
Name Accession Description Interval E-value
Asn_synthase_B_C cd01991
C-terminal domain of asparagine synthase B; The C-terminal domain of asparagine synthase (or ...
 29-60 2.21e-06

C-terminal domain of asparagine synthase B; The C-terminal domain of asparagine synthase (or synthetase) B is always associated with an N-terminal amidotransferase domain. Family members that contain this domain catalyze the conversion of aspartate to asparagine. Asparagine synthase B catalyzes the synthesis of asparagine from aspartate, Mg(2+)ATP, and glutamine. The three-dimensional architecture of the N-terminal domain of asparagine synthetase B is similar to that observed for glutamine phosphoribosylpyrophosphate amidotransferase while the molecular motif of the C-domain is reminiscent to that observed for GMP synthetase.


Pssm-ID: 467495 [Multi-domain]  Cd Length: 224  Bit Score: 42.26  E-value: 2.21e-06
                          10        20        30
                  ....*....|....*....|....*....|..
gi 1200519375  29 VGLMVSGGLDSAILLYALHKANPYAEIKTYCV 60
Cdd:cd01991     5 VGVLLSGGLDSSLIAALAARLLPETPIDLFTV 36
TilS COG0037
tRNA(Ile)-lysidine synthase TilS/MesJ [Translation, ribosomal structure and biogenesis]; tRNA ...
 29-60 6.03e-03

tRNA(Ile)-lysidine synthase TilS/MesJ [Translation, ribosomal structure and biogenesis]; tRNA(Ile)-lysidine synthase TilS/MesJ is part of the Pathway/BioSystem: tRNA modification


Pssm-ID: 439807 [Multi-domain]  Cd Length: 235  Bit Score: 32.88  E-value: 6.03e-03
                          10        20        30
                  ....*....|....*....|....*....|..
gi 1200519375  29 VGLMVSGGLDSAILLYALHKANPYAEIKTYCV 60
Cdd:COG0037    18 ILVAVSGGKDSLALLHLLAKLRRRLGFELVAV 49
Asn_synthase pfam00733
Asparagine synthase; This family is always found associated with pfam00310. Members of this ...
 29-60 7.37e-03

Asparagine synthase; This family is always found associated with pfam00310. Members of this family catalyze the conversion of aspartate to asparagine.


Pssm-ID: 395594 [Multi-domain]  Cd Length: 279  Bit Score: 32.59  E-value: 7.37e-03
                          10        20        30
                  ....*....|....*....|....*....|..
gi 1200519375  29 VGLMVSGGLDSAILLYALHKANPYaEIKTYCV 60
Cdd:pfam00733  20 VGAFLSGGLDSSSIAALAARQSPS-PLHTFSI 50
 
Name Accession Description Interval E-value
Asn_synthase_B_C cd01991
C-terminal domain of asparagine synthase B; The C-terminal domain of asparagine synthase (or ...
 29-60 2.21e-06

C-terminal domain of asparagine synthase B; The C-terminal domain of asparagine synthase (or synthetase) B is always associated with an N-terminal amidotransferase domain. Family members that contain this domain catalyze the conversion of aspartate to asparagine. Asparagine synthase B catalyzes the synthesis of asparagine from aspartate, Mg(2+)ATP, and glutamine. The three-dimensional architecture of the N-terminal domain of asparagine synthetase B is similar to that observed for glutamine phosphoribosylpyrophosphate amidotransferase while the molecular motif of the C-domain is reminiscent to that observed for GMP synthetase.


Pssm-ID: 467495 [Multi-domain]  Cd Length: 224  Bit Score: 42.26  E-value: 2.21e-06
                          10        20        30
                  ....*....|....*....|....*....|..
gi 1200519375  29 VGLMVSGGLDSAILLYALHKANPYAEIKTYCV 60
Cdd:cd01991     5 VGVLLSGGLDSSLIAALAARLLPETPIDLFTV 36
TilS COG0037
tRNA(Ile)-lysidine synthase TilS/MesJ [Translation, ribosomal structure and biogenesis]; tRNA ...
 29-60 6.03e-03

tRNA(Ile)-lysidine synthase TilS/MesJ [Translation, ribosomal structure and biogenesis]; tRNA(Ile)-lysidine synthase TilS/MesJ is part of the Pathway/BioSystem: tRNA modification


Pssm-ID: 439807 [Multi-domain]  Cd Length: 235  Bit Score: 32.88  E-value: 6.03e-03
                          10        20        30
                  ....*....|....*....|....*....|..
gi 1200519375  29 VGLMVSGGLDSAILLYALHKANPYAEIKTYCV 60
Cdd:COG0037    18 ILVAVSGGKDSLALLHLLAKLRRRLGFELVAV 49
Asn_synthase pfam00733
Asparagine synthase; This family is always found associated with pfam00310. Members of this ...
 29-60 7.37e-03

Asparagine synthase; This family is always found associated with pfam00310. Members of this family catalyze the conversion of aspartate to asparagine.


Pssm-ID: 395594 [Multi-domain]  Cd Length: 279  Bit Score: 32.59  E-value: 7.37e-03
                          10        20        30
                  ....*....|....*....|....*....|..
gi 1200519375  29 VGLMVSGGLDSAILLYALHKANPYaEIKTYCV 60
Cdd:pfam00733  20 VGAFLSGGLDSSSIAALAARQSPS-PLHTFSI 50
ATP_bind_3 pfam01171
PP-loop family; This family of proteins belongs to the PP-loop superfamily.
 33-56 9.60e-03

PP-loop family; This family of proteins belongs to the PP-loop superfamily.


Pssm-ID: 426097 [Multi-domain]  Cd Length: 178  Bit Score: 32.21  E-value: 9.60e-03
                          10        20
                  ....*....|....*....|....
gi 1200519375  33 VSGGLDSAILLYALHKANPYAEIK 56
Cdd:pfam01171   3 VSGGPDSMALLYLLAKLKIKLGIE 26
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH