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Conserved domains on  [gi|2442585597|ref|WP_272929917|]
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urease accessory protein UreF, partial [Burkholderia sp. KCJ3K979]

Protein Classification

urease accessory protein UreF( domain architecture ID 10002854)

urease accessory protein UreF is part of a accessory protein complex that facilitates maturation of urease

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
UreF COG0830
Urease accessory protein UreF [Posttranslational modification, protein turnover, chaperones];
21-98 4.78e-29

Urease accessory protein UreF [Posttranslational modification, protein turnover, chaperones];


:

Pssm-ID: 440592  Cd Length: 226  Bit Score: 103.73  E-value: 4.78e-29
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2442585597  21 TLAAYAFGWVENQTSAALKAVPLGQLAGQRIIVALRGAIDAAVRRALATPPDAVNTFAPQLGILSARHETQYSRLFRS 98
Cdd:COG0830   149 ALLAYLYSWVSNLVSAAVRLVPLGQTAGQRLLARLAPLIEAAAERALALPLDDLGSFAPLLDIASMRHETQYSRLFRS 226
 
Name Accession Description Interval E-value
UreF COG0830
Urease accessory protein UreF [Posttranslational modification, protein turnover, chaperones];
21-98 4.78e-29

Urease accessory protein UreF [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440592  Cd Length: 226  Bit Score: 103.73  E-value: 4.78e-29
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2442585597  21 TLAAYAFGWVENQTSAALKAVPLGQLAGQRIIVALRGAIDAAVRRALATPPDAVNTFAPQLGILSARHETQYSRLFRS 98
Cdd:COG0830   149 ALLAYLYSWVSNLVSAAVRLVPLGQTAGQRLLARLAPLIEAAAERALALPLDDLGSFAPLLDIASMRHETQYSRLFRS 226
UreF pfam01730
UreF; This family consists of the Urease accessory protein UreF. The urease enzyme (urea ...
21-54 1.69e-07

UreF; This family consists of the Urease accessory protein UreF. The urease enzyme (urea amidohydrolase) hydrolyses urea into ammonia and carbamic acid. UreF is proposed to modulate the activation process of urease by eliminating the binding of nickel irons to noncarbamylated protein.


Pssm-ID: 460307  Cd Length: 141  Bit Score: 46.03  E-value: 1.69e-07
                          10        20        30
                  ....*....|....*....|....*....|....
gi 2442585597  21 TLAAYAFGWVENQTSAALKAVPLGQLAGQRIIVA 54
Cdd:pfam01730 108 ALLAYLYSWASNLVSAAVRLVPLGQTAGQRLLAR 141
 
Name Accession Description Interval E-value
UreF COG0830
Urease accessory protein UreF [Posttranslational modification, protein turnover, chaperones];
21-98 4.78e-29

Urease accessory protein UreF [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440592  Cd Length: 226  Bit Score: 103.73  E-value: 4.78e-29
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2442585597  21 TLAAYAFGWVENQTSAALKAVPLGQLAGQRIIVALRGAIDAAVRRALATPPDAVNTFAPQLGILSARHETQYSRLFRS 98
Cdd:COG0830   149 ALLAYLYSWVSNLVSAAVRLVPLGQTAGQRLLARLAPLIEAAAERALALPLDDLGSFAPLLDIASMRHETQYSRLFRS 226
UreF pfam01730
UreF; This family consists of the Urease accessory protein UreF. The urease enzyme (urea ...
21-54 1.69e-07

UreF; This family consists of the Urease accessory protein UreF. The urease enzyme (urea amidohydrolase) hydrolyses urea into ammonia and carbamic acid. UreF is proposed to modulate the activation process of urease by eliminating the binding of nickel irons to noncarbamylated protein.


Pssm-ID: 460307  Cd Length: 141  Bit Score: 46.03  E-value: 1.69e-07
                          10        20        30
                  ....*....|....*....|....*....|....
gi 2442585597  21 TLAAYAFGWVENQTSAALKAVPLGQLAGQRIIVA 54
Cdd:pfam01730 108 ALLAYLYSWASNLVSAAVRLVPLGQTAGQRLLAR 141
 
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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