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Conserved domains on  [gi|503291744|ref|WP_013526405|]
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urease subunit gamma [Haemophilus influenzae]

Protein Classification

urease subunit gamma( domain architecture ID 10455515)

urease subunit gamma (UreA) forms a heterotrimer with subunits alpha (UreC) and beta (UreB) to catalyze the breakdown of urea

EC:  3.5.1.5
Gene Symbol:  ureA
Gene Ontology:  GO:0009039|GO:0043419
PubMed:  21290719

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Urease_gamma pfam00547
Urease, gamma subunit; Urease is a nickel-binding enzyme that catalyzes the hydrolysis of urea ...
 1-99 3.99e-65

Urease, gamma subunit; Urease is a nickel-binding enzyme that catalyzes the hydrolysis of urea to carbon dioxide and ammonia.


:

Pssm-ID: 459850  Cd Length: 99  Bit Score: 191.09  E-value: 3.99e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503291744    1 MHLTSREQEKLMLFLAGELAAKRKARGLKLNYPETIAYIASHLQEAAREGMSVAEVMQYGATLLTVDDVMEGVAEMVHEV 80
Cdd:pfam00547   1 MHLTPREQDKLLLFVAGELARRRLARGLKLNYPEAVALIADELLEGARDGKSVAELMQLGRTVLGRDDVMPGVPEMLPEV 80

                          90
                  ....*....|....*....
gi 503291744   81 QIEATFPDGTKLVTVHNPI 99
Cdd:pfam00547  81 QVEATFPDGTKLVTVHDPI 99
 
Name Accession Description Interval E-value
Urease_gamma pfam00547
Urease, gamma subunit; Urease is a nickel-binding enzyme that catalyzes the hydrolysis of urea ...
 1-99 3.99e-65

Urease, gamma subunit; Urease is a nickel-binding enzyme that catalyzes the hydrolysis of urea to carbon dioxide and ammonia.


Pssm-ID: 459850  Cd Length: 99  Bit Score: 191.09  E-value: 3.99e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503291744    1 MHLTSREQEKLMLFLAGELAAKRKARGLKLNYPETIAYIASHLQEAAREGMSVAEVMQYGATLLTVDDVMEGVAEMVHEV 80
Cdd:pfam00547   1 MHLTPREQDKLLLFVAGELARRRLARGLKLNYPEAVALIADELLEGARDGKSVAELMQLGRTVLGRDDVMPGVPEMLPEV 80

                          90
                  ....*....|....*....
gi 503291744   81 QIEATFPDGTKLVTVHNPI 99
Cdd:pfam00547  81 QVEATFPDGTKLVTVHDPI 99
ureA PRK13241
urease subunit gamma; Provisional
 1-100 6.00e-65

urease subunit gamma; Provisional


Pssm-ID: 183913  Cd Length: 100  Bit Score: 190.86  E-value: 6.00e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503291744   1 MHLTSREQEKLMLFLAGELAAKRKARGLKLNYPETIAYIASHLQEAAREGMSVAEVMQYGATLLTVDDVMEGVAEMVHEV 80
Cdd:PRK13241   1 MHLTPREKDKLLIFTAALLAERRKARGLKLNYPEAVALISDALLEGARDGKTVAELMSYGRTVLTRDDVMEGVPEMIPDV 80

                         90       100
                 ....*....|....*....|
gi 503291744  81 QIEATFPDGTKLVTVHNPIR 100
Cdd:PRK13241  81 QVEATFPDGTKLVTVHDPIR 100
UreA COG0831
Urease gamma subunit [Amino acid transport and metabolism];
1-100 6.05e-62

Urease gamma subunit [Amino acid transport and metabolism];


Pssm-ID: 440593  Cd Length: 102  Bit Score: 183.41  E-value: 6.05e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503291744   1 MHLTSREQEKLMLFLAGELAAKRKARGLKLNYPETIAYIASHLQEAAREGMSVAEVMQYGATLLTVDDVMEGVAEMVHEV 80
Cdd:COG0831    1 MHLTPREQEKLLIFTAAELARRRRARGLKLNYPEAVALISDEVLEGARDGKSVAELMEEGRTVLTRDDVMPGVPEMIPEV 80

                         90       100
                 ....*....|....*....|
gi 503291744  81 QIEATFPDGTKLVTVHNPIR 100
Cdd:COG0831   81 QVEATFPDGTKLVTVHDPIR 100
urease_gam TIGR00193
urease, gamma subunit; In a number of species, including B.subtilis, Synechocystis, and ...
 1-100 6.82e-57

urease, gamma subunit; In a number of species, including B.subtilis, Synechocystis, and Haemophilus influenzae, urease subunits beta and gamma are encoded as separate polypeptides. In Helicobacter pylori UreA and in the fission yeast Schizosaccharomyces pombe, beta subunit-like sequence follows gamma subunit-like sequence in a single chain; the fission yeast protein contains additional C-terminal regions. Nomenclature for the various subunits of urease in Helicobacter differs from nomenclature in most other species. [Central intermediary metabolism, Nitrogen metabolism]


Pssm-ID: 272952  Cd Length: 102  Bit Score: 170.82  E-value: 6.82e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503291744    1 MHLTSREQEKLMLFLAGELAAKRKARGLKLNYPETIAYIASHLQEAAREGMSVAEVMQYGATLLTVDDVMEGVAEMVHEV 80
Cdd:TIGR00193   1 MKLTPKEQDKLMLFYAGELAKKRKARGVKLNYPEAVAYISAHIMEGARDGKKVAELMQYGRTLLTPDDVMEGVAEMLHEV 80

                          90       100
                  ....*....|....*....|
gi 503291744   81 QIEATFPDGTKLVTVHNPIR 100
Cdd:TIGR00193  81 QIEATFPDGTKLVTVHTPIR 100
Urease_gamma cd00390
Urease gamma-subunit; Urease is a nickel-dependent metalloenzyme that catalyzes the hydrolysis ...
 4-99 9.39e-57

Urease gamma-subunit; Urease is a nickel-dependent metalloenzyme that catalyzes the hydrolysis of urea to form ammonia and carbon dioxide. Nickel-dependent ureases are found in bacteria, archaea, fungi and plants. Their primary role is to allow the use of external and internally-generated urea as a nitrogen source. The enzyme consists of three subunits, alpha, beta and gamma, which can exist as separate proteins or can be fused on a single protein chain. The alpha-beta-gamma heterotrimer forms multimers, mainly trimers. The large alpha subunit is the catalytic domain containing an active site with a bi-nickel center complexed by a carbamylated lysine. The beta and gamma subunits play a role in subunit association to form the higher order trimers.


Pssm-ID: 238229  Cd Length: 96  Bit Score: 170.07  E-value: 9.39e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503291744   4 TSREQEKLMLFLAGELAAKRKARGLKLNYPETIAYIASHLQEAAREGMSVAEVMQYGATLLTVDDVMEGVAEMVHEVQIE 83
Cdd:cd00390    1 TPRELEKLLIFTAAELARKRLARGLKLNYPEAVALIADEILEGARDGKSVAELMSLGKTVLTRDDVMEGVPEMLHDVQVE 80

                         90
                 ....*....|....*.
gi 503291744  84 ATFPDGTKLVTVHNPI 99
Cdd:cd00390   81 ATFPDGTKLVTVHDPI 96
 
Name Accession Description Interval E-value
Urease_gamma pfam00547
Urease, gamma subunit; Urease is a nickel-binding enzyme that catalyzes the hydrolysis of urea ...
 1-99 3.99e-65

Urease, gamma subunit; Urease is a nickel-binding enzyme that catalyzes the hydrolysis of urea to carbon dioxide and ammonia.


Pssm-ID: 459850  Cd Length: 99  Bit Score: 191.09  E-value: 3.99e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503291744    1 MHLTSREQEKLMLFLAGELAAKRKARGLKLNYPETIAYIASHLQEAAREGMSVAEVMQYGATLLTVDDVMEGVAEMVHEV 80
Cdd:pfam00547   1 MHLTPREQDKLLLFVAGELARRRLARGLKLNYPEAVALIADELLEGARDGKSVAELMQLGRTVLGRDDVMPGVPEMLPEV 80

                          90
                  ....*....|....*....
gi 503291744   81 QIEATFPDGTKLVTVHNPI 99
Cdd:pfam00547  81 QVEATFPDGTKLVTVHDPI 99
ureA PRK13241
urease subunit gamma; Provisional
 1-100 6.00e-65

urease subunit gamma; Provisional


Pssm-ID: 183913  Cd Length: 100  Bit Score: 190.86  E-value: 6.00e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503291744   1 MHLTSREQEKLMLFLAGELAAKRKARGLKLNYPETIAYIASHLQEAAREGMSVAEVMQYGATLLTVDDVMEGVAEMVHEV 80
Cdd:PRK13241   1 MHLTPREKDKLLIFTAALLAERRKARGLKLNYPEAVALISDALLEGARDGKTVAELMSYGRTVLTRDDVMEGVPEMIPDV 80

                         90       100
                 ....*....|....*....|
gi 503291744  81 QIEATFPDGTKLVTVHNPIR 100
Cdd:PRK13241  81 QVEATFPDGTKLVTVHDPIR 100
UreA COG0831
Urease gamma subunit [Amino acid transport and metabolism];
1-100 6.05e-62

Urease gamma subunit [Amino acid transport and metabolism];


Pssm-ID: 440593  Cd Length: 102  Bit Score: 183.41  E-value: 6.05e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503291744   1 MHLTSREQEKLMLFLAGELAAKRKARGLKLNYPETIAYIASHLQEAAREGMSVAEVMQYGATLLTVDDVMEGVAEMVHEV 80
Cdd:COG0831    1 MHLTPREQEKLLIFTAAELARRRRARGLKLNYPEAVALISDEVLEGARDGKSVAELMEEGRTVLTRDDVMPGVPEMIPEV 80

                         90       100
                 ....*....|....*....|
gi 503291744  81 QIEATFPDGTKLVTVHNPIR 100
Cdd:COG0831   81 QVEATFPDGTKLVTVHDPIR 100
urease_gam TIGR00193
urease, gamma subunit; In a number of species, including B.subtilis, Synechocystis, and ...
 1-100 6.82e-57

urease, gamma subunit; In a number of species, including B.subtilis, Synechocystis, and Haemophilus influenzae, urease subunits beta and gamma are encoded as separate polypeptides. In Helicobacter pylori UreA and in the fission yeast Schizosaccharomyces pombe, beta subunit-like sequence follows gamma subunit-like sequence in a single chain; the fission yeast protein contains additional C-terminal regions. Nomenclature for the various subunits of urease in Helicobacter differs from nomenclature in most other species. [Central intermediary metabolism, Nitrogen metabolism]


Pssm-ID: 272952  Cd Length: 102  Bit Score: 170.82  E-value: 6.82e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503291744    1 MHLTSREQEKLMLFLAGELAAKRKARGLKLNYPETIAYIASHLQEAAREGMSVAEVMQYGATLLTVDDVMEGVAEMVHEV 80
Cdd:TIGR00193   1 MKLTPKEQDKLMLFYAGELAKKRKARGVKLNYPEAVAYISAHIMEGARDGKKVAELMQYGRTLLTPDDVMEGVAEMLHEV 80

                          90       100
                  ....*....|....*....|
gi 503291744   81 QIEATFPDGTKLVTVHNPIR 100
Cdd:TIGR00193  81 QIEATFPDGTKLVTVHTPIR 100
PRK13192 PRK13192
bifunctional urease subunit gamma/beta; Reviewed
 1-100 6.91e-57

bifunctional urease subunit gamma/beta; Reviewed


Pssm-ID: 183886 [Multi-domain]  Cd Length: 208  Bit Score: 174.40  E-value: 6.91e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503291744   1 MHLTSREQEKLMLFLAGELAAKRKARGLKLNYPETIAYIASHLQEAAREGMSVAEVMQYGATLLTVDDVMEGVAEMVHEV 80
Cdd:PRK13192   1 MRLTPTELDRLLLFTAAELARKRRARGLKLNYPEAVALIADEVLEAARDGRSVAELIDLGRTILTTDDVLPGVADMVPEV 80

                         90       100
                 ....*....|....*....|
gi 503291744  81 QIEATFPDGTKLVTVHNPIR 100
Cdd:PRK13192  81 QVEATFPDGTKLVTVHDPIR 100
Urease_gamma cd00390
Urease gamma-subunit; Urease is a nickel-dependent metalloenzyme that catalyzes the hydrolysis ...
 4-99 9.39e-57

Urease gamma-subunit; Urease is a nickel-dependent metalloenzyme that catalyzes the hydrolysis of urea to form ammonia and carbon dioxide. Nickel-dependent ureases are found in bacteria, archaea, fungi and plants. Their primary role is to allow the use of external and internally-generated urea as a nitrogen source. The enzyme consists of three subunits, alpha, beta and gamma, which can exist as separate proteins or can be fused on a single protein chain. The alpha-beta-gamma heterotrimer forms multimers, mainly trimers. The large alpha subunit is the catalytic domain containing an active site with a bi-nickel center complexed by a carbamylated lysine. The beta and gamma subunits play a role in subunit association to form the higher order trimers.


Pssm-ID: 238229  Cd Length: 96  Bit Score: 170.07  E-value: 9.39e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503291744   4 TSREQEKLMLFLAGELAAKRKARGLKLNYPETIAYIASHLQEAAREGMSVAEVMQYGATLLTVDDVMEGVAEMVHEVQIE 83
Cdd:cd00390    1 TPRELEKLLIFTAAELARKRLARGLKLNYPEAVALIADEILEGARDGKSVAELMSLGKTVLTRDDVMEGVPEMLHDVQVE 80

                         90
                 ....*....|....*.
gi 503291744  84 ATFPDGTKLVTVHNPI 99
Cdd:cd00390   81 ATFPDGTKLVTVHDPI 96
PRK13986 PRK13986
urease subunit beta;
1-99 1.51e-50

urease subunit beta;


Pssm-ID: 184439 [Multi-domain]  Cd Length: 225  Bit Score: 158.84  E-value: 1.51e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503291744   1 MHLTSREQEKLMLFLAGELAAKRKARGLKLNYPETIAYIASHLQEAAREG-MSVAEVMQYGATLLTVDDVMEGVAEMVHE 79
Cdd:PRK13986   1 MKLTPKELDKLMLHYAGELAKKRKEKGIKLNYVEAVALISAHIMEEARAGkKTVAELMQEGRTLLKPDDVMDGVASMIHE 80

                         90       100
                 ....*....|....*....|
gi 503291744  80 VQIEATFPDGTKLVTVHNPI 99
Cdd:PRK13986  81 VGIEAMFPDGTKLVTVHTPI 100
PLN02303 PLN02303
urease
 1-99 5.63e-37

urease


Pssm-ID: 215172 [Multi-domain]  Cd Length: 837  Bit Score: 131.41  E-value: 5.63e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503291744   1 MHLTSREQEKLMLFLAGELAAKRKARGLKLNYPETIAYIASHLQEAAREG-MSVAEVMQYGATLLTVDDVMEGVAEMVHE 79
Cdd:PLN02303   1 MKLSPREIDKLLLHQAGFLAQKRLARGLRLNYTEAVALIATQILEFIRDGdKSVAELMDLGKQLLGRRQVLPAVPHLLHT 80

                         90       100
                 ....*....|....*....|
gi 503291744  80 VQIEATFPDGTKLVTVHNPI 99
Cdd:PLN02303  81 VQVEGTFPDGTKLVTVHDPI 100
ureA PRK13242
urease subunit gamma; Provisional
 1-99 4.78e-28

urease subunit gamma; Provisional


Pssm-ID: 139420  Cd Length: 100  Bit Score: 97.84  E-value: 4.78e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503291744   1 MHLTSREQEKLMLFLAGELAAKRKARGLKLNYPETIAYIASHLQEAAREGMSVAEVMQYGATLLTVDDVMEGVAEMVHEV 80
Cdd:PRK13242   1 MHLTPREFDKLVIHMLSDVALKRKNKGLKLNHPEAVAVLSAYVLDGAREGKTVEEVMDGARSVLKADDVMDGVPDLLPLI 80

                         90
                 ....*....|....*....
gi 503291744  81 QIEATFPDGTKLVTVHNPI 99
Cdd:PRK13242  81 QVEAVFSDGSRLVSLHNPI 99
 
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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