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Conserved domains on  [gi|1828979500|gb|QIU94337|]
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DUF1599 domain-containing protein [Bacteroides faecium]

Protein Classification

DUF1599 domain-containing protein( domain architecture ID 10541880)

DUF1599 domain-containing protein may contain a nucleotide modification associated domain that is associated with the 5-hydroxymethyl uridine synthase and is predicted to play a role in modified base biosynthesis pathways

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
DUF1599 pfam07659
Nucleotide modification associated domain 1; An alpha helical domain with conserved polar ...
 22-82 3.72e-34

Nucleotide modification associated domain 1; An alpha helical domain with conserved polar residues suggestive of enzymatic function. The domain is associated with the 5-hydroxymethyl uridine synthase and is predicted to play a role in modified base biosynthesis pathways.


:

Pssm-ID: 429579  Cd Length: 61  Bit Score: 114.96  E-value: 3.72e-34
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1828979500  22 KLHDYGPAWRILRPASVTDQIFIKANRIRSIETKGVTLIDEGIRAEFIAIVNYGIIGLIQL 82
Cdd:pfam07659   1 KNHDYGEAWRIMRLSSLTDQILIKAQRIRSIEEKGEALVSEGIDAEYIDIINYSIFALIQL 61
DUF1599 pfam07659
Nucleotide modification associated domain 1; An alpha helical domain with conserved polar ...
 115-176 1.04e-30

Nucleotide modification associated domain 1; An alpha helical domain with conserved polar residues suggestive of enzymatic function. The domain is associated with the 5-hydroxymethyl uridine synthase and is predicted to play a role in modified base biosynthesis pathways.


:

Pssm-ID: 429579  Cd Length: 61  Bit Score: 106.10  E-value: 1.04e-30
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1828979500 115 KNHDYDEAWRSMRVSSYTDLILMKIYRTKQIESlSGNTLVSEGIDANYMDMINYSVFGLIKI 176
Cdd:pfam07659   1 KNHDYGEAWRIMRLSSLTDQILIKAQRIRSIEE-KGEALVSEGIDAEYIDIINYSIFALIQL 61
 
Name Accession Description Interval E-value
DUF1599 pfam07659
Nucleotide modification associated domain 1; An alpha helical domain with conserved polar ...
 22-82 3.72e-34

Nucleotide modification associated domain 1; An alpha helical domain with conserved polar residues suggestive of enzymatic function. The domain is associated with the 5-hydroxymethyl uridine synthase and is predicted to play a role in modified base biosynthesis pathways.


Pssm-ID: 429579  Cd Length: 61  Bit Score: 114.96  E-value: 3.72e-34
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1828979500  22 KLHDYGPAWRILRPASVTDQIFIKANRIRSIETKGVTLIDEGIRAEFIAIVNYGIIGLIQL 82
Cdd:pfam07659   1 KNHDYGEAWRIMRLSSLTDQILIKAQRIRSIEEKGEALVSEGIDAEYIDIINYSIFALIQL 61
DUF1599 pfam07659
Nucleotide modification associated domain 1; An alpha helical domain with conserved polar ...
 115-176 1.04e-30

Nucleotide modification associated domain 1; An alpha helical domain with conserved polar residues suggestive of enzymatic function. The domain is associated with the 5-hydroxymethyl uridine synthase and is predicted to play a role in modified base biosynthesis pathways.


Pssm-ID: 429579  Cd Length: 61  Bit Score: 106.10  E-value: 1.04e-30
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1828979500 115 KNHDYDEAWRSMRVSSYTDLILMKIYRTKQIESlSGNTLVSEGIDANYMDMINYSVFGLIKI 176
Cdd:pfam07659   1 KNHDYGEAWRIMRLSSLTDQILIKAQRIRSIEE-KGEALVSEGIDAEYIDIINYSIFALIQL 61
 
Name Accession Description Interval E-value
DUF1599 pfam07659
Nucleotide modification associated domain 1; An alpha helical domain with conserved polar ...
 22-82 3.72e-34

Nucleotide modification associated domain 1; An alpha helical domain with conserved polar residues suggestive of enzymatic function. The domain is associated with the 5-hydroxymethyl uridine synthase and is predicted to play a role in modified base biosynthesis pathways.


Pssm-ID: 429579  Cd Length: 61  Bit Score: 114.96  E-value: 3.72e-34
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1828979500  22 KLHDYGPAWRILRPASVTDQIFIKANRIRSIETKGVTLIDEGIRAEFIAIVNYGIIGLIQL 82
Cdd:pfam07659   1 KNHDYGEAWRIMRLSSLTDQILIKAQRIRSIEEKGEALVSEGIDAEYIDIINYSIFALIQL 61
DUF1599 pfam07659
Nucleotide modification associated domain 1; An alpha helical domain with conserved polar ...
 115-176 1.04e-30

Nucleotide modification associated domain 1; An alpha helical domain with conserved polar residues suggestive of enzymatic function. The domain is associated with the 5-hydroxymethyl uridine synthase and is predicted to play a role in modified base biosynthesis pathways.


Pssm-ID: 429579  Cd Length: 61  Bit Score: 106.10  E-value: 1.04e-30
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1828979500 115 KNHDYDEAWRSMRVSSYTDLILMKIYRTKQIESlSGNTLVSEGIDANYMDMINYSVFGLIKI 176
Cdd:pfam07659   1 KNHDYGEAWRIMRLSSLTDQILIKAQRIRSIEE-KGEALVSEGIDAEYIDIINYSIFALIQL 61
 
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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