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Conserved domains on  [gi|516234602|ref|WP_017638565|]
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MULTISPECIES: urease accessory protein UreD [Staphylococcus]

Protein Classification

urease accessory protein UreD( domain architecture ID 10002853)

urease accessory protein UreD/UreH forms a complex together with UreF and UreG that acts as a GTP-hydrolysis-dependent molecular chaperone which is required for maturation of urease via the functional incorporation of the urease nickel metallocenter

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
UreH COG0829
Urease accessory protein UreH [Posttranslational modification, protein turnover, chaperones];
2-276 1.17e-78

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


:

Pssm-ID: 440591 [Multi-domain]  Cd Length: 286  Bit Score: 239.72  E-value: 1.17e-78
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516234602   2 SQQSWTGQLDLTVFNNGKRSVARDIFFEKALKVIRPVYLNGSTTPTFYIVNVGGGYLDGDRYSMNFNIEDNASVTLTSQG 81
Cdd:COG0829   11 GAQGWRGRLRLGFARRGGRTVLARLYHSGPLRVQRPFYPEGPGVCHVVLLHPPGGLVGGDRLRIDITVGAGAHALLTTQA 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516234602  82 ATKIYKTLKDHVEQYQTFQLKPNAYMEYVADPIIAYENAKFYQHNRFDLDETSAMFYTDILTPGYSSDDKNFSYKYMHLV 161
Cdd:COG0829   91 ATKVYRSDGGYARQDVRLTVGAGARLEWLPQETILFDGARLRQRTRVDLAPGARLLGWEIVVLGRPARGERFAFGRLRSR 170
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516234602 162 NEIYINNELVTYDNLMLNPEKNSIDSLGYMENYTHLGSAYFIHPSVNQKFIDEIYnqiKHFEKELNCRLGITQLPTHGLS 241
Cdd:COG0829  171 LEIRRDGRLLWAERLRLDGDAALLDSPAGLGGAPVFATLVAVGPDADEALLEALR---ALLAEAPGVRAGASALPDGGLV 247
                        250       260       270
                 ....*....|....*....|....*....|....*
gi 516234602 242 IRILSNRTQYIESILEKAQSYIANELYDREINFLR 276
Cdd:COG0829  248 VRLLGPDAEALRRALRAAWQALRPALLGRPPALPR 282
 
Name Accession Description Interval E-value
UreH COG0829
Urease accessory protein UreH [Posttranslational modification, protein turnover, chaperones];
2-276 1.17e-78

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


Pssm-ID: 440591 [Multi-domain]  Cd Length: 286  Bit Score: 239.72  E-value: 1.17e-78
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516234602   2 SQQSWTGQLDLTVFNNGKRSVARDIFFEKALKVIRPVYLNGSTTPTFYIVNVGGGYLDGDRYSMNFNIEDNASVTLTSQG 81
Cdd:COG0829   11 GAQGWRGRLRLGFARRGGRTVLARLYHSGPLRVQRPFYPEGPGVCHVVLLHPPGGLVGGDRLRIDITVGAGAHALLTTQA 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516234602  82 ATKIYKTLKDHVEQYQTFQLKPNAYMEYVADPIIAYENAKFYQHNRFDLDETSAMFYTDILTPGYSSDDKNFSYKYMHLV 161
Cdd:COG0829   91 ATKVYRSDGGYARQDVRLTVGAGARLEWLPQETILFDGARLRQRTRVDLAPGARLLGWEIVVLGRPARGERFAFGRLRSR 170
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516234602 162 NEIYINNELVTYDNLMLNPEKNSIDSLGYMENYTHLGSAYFIHPSVNQKFIDEIYnqiKHFEKELNCRLGITQLPTHGLS 241
Cdd:COG0829  171 LEIRRDGRLLWAERLRLDGDAALLDSPAGLGGAPVFATLVAVGPDADEALLEALR---ALLAEAPGVRAGASALPDGGLV 247
                        250       260       270
                 ....*....|....*....|....*....|....*
gi 516234602 242 IRILSNRTQYIESILEKAQSYIANELYDREINFLR 276
Cdd:COG0829  248 VRLLGPDAEALRRALRAAWQALRPALLGRPPALPR 282
UreD pfam01774
UreD urease accessory protein; UreD is a urease accessory protein. Urease pfam00449 hydrolyses ...
49-199 4.41e-50

UreD urease accessory protein; UreD is a urease accessory protein. Urease pfam00449 hydrolyses urea into ammonia and carbamic acid. UreD is involved in activation of the urease enzyme via the UreD-UreF-UreG-urease complex and is required for urease nickel metallocenter assembly. See also UreF pfam01730, UreG pfam01495.


Pssm-ID: 460320  Cd Length: 164  Bit Score: 162.61  E-value: 4.41e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516234602   49 YIVNVGGGYLDGDRYSMNFNIEDNASVTLTSQGATKIYKTLKDHVEQYQTFQLKPNAYMEYVADPIIAYENAKFYQHNRF 128
Cdd:pfam01774   2 YLLHPGGGLVGGDRLDLDITVGPGARLLLTTQAATKIYRSPGGPARQTVRLTVGAGATLEWLPDPTIPFAGARYRQTTRV 81
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 516234602  129 DLDETSAMFYTDILTPGYSSDDKNFSYKYMHLVNEIYINNELVTYDNLMLNPeknSIDSLGYMENYTHLGS 199
Cdd:pfam01774  82 ELAPGASLLLWEIVTLGRPARGERFDFGRYRSRLEVRRDGRLLLRDRLRLEP---GDAGAGRLGGYTVFGT 149
 
Name Accession Description Interval E-value
UreH COG0829
Urease accessory protein UreH [Posttranslational modification, protein turnover, chaperones];
2-276 1.17e-78

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


Pssm-ID: 440591 [Multi-domain]  Cd Length: 286  Bit Score: 239.72  E-value: 1.17e-78
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516234602   2 SQQSWTGQLDLTVFNNGKRSVARDIFFEKALKVIRPVYLNGSTTPTFYIVNVGGGYLDGDRYSMNFNIEDNASVTLTSQG 81
Cdd:COG0829   11 GAQGWRGRLRLGFARRGGRTVLARLYHSGPLRVQRPFYPEGPGVCHVVLLHPPGGLVGGDRLRIDITVGAGAHALLTTQA 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516234602  82 ATKIYKTLKDHVEQYQTFQLKPNAYMEYVADPIIAYENAKFYQHNRFDLDETSAMFYTDILTPGYSSDDKNFSYKYMHLV 161
Cdd:COG0829   91 ATKVYRSDGGYARQDVRLTVGAGARLEWLPQETILFDGARLRQRTRVDLAPGARLLGWEIVVLGRPARGERFAFGRLRSR 170
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516234602 162 NEIYINNELVTYDNLMLNPEKNSIDSLGYMENYTHLGSAYFIHPSVNQKFIDEIYnqiKHFEKELNCRLGITQLPTHGLS 241
Cdd:COG0829  171 LEIRRDGRLLWAERLRLDGDAALLDSPAGLGGAPVFATLVAVGPDADEALLEALR---ALLAEAPGVRAGASALPDGGLV 247
                        250       260       270
                 ....*....|....*....|....*....|....*
gi 516234602 242 IRILSNRTQYIESILEKAQSYIANELYDREINFLR 276
Cdd:COG0829  248 VRLLGPDAEALRRALRAAWQALRPALLGRPPALPR 282
UreD pfam01774
UreD urease accessory protein; UreD is a urease accessory protein. Urease pfam00449 hydrolyses ...
49-199 4.41e-50

UreD urease accessory protein; UreD is a urease accessory protein. Urease pfam00449 hydrolyses urea into ammonia and carbamic acid. UreD is involved in activation of the urease enzyme via the UreD-UreF-UreG-urease complex and is required for urease nickel metallocenter assembly. See also UreF pfam01730, UreG pfam01495.


Pssm-ID: 460320  Cd Length: 164  Bit Score: 162.61  E-value: 4.41e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516234602   49 YIVNVGGGYLDGDRYSMNFNIEDNASVTLTSQGATKIYKTLKDHVEQYQTFQLKPNAYMEYVADPIIAYENAKFYQHNRF 128
Cdd:pfam01774   2 YLLHPGGGLVGGDRLDLDITVGPGARLLLTTQAATKIYRSPGGPARQTVRLTVGAGATLEWLPDPTIPFAGARYRQTTRV 81
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 516234602  129 DLDETSAMFYTDILTPGYSSDDKNFSYKYMHLVNEIYINNELVTYDNLMLNPeknSIDSLGYMENYTHLGS 199
Cdd:pfam01774  82 ELAPGASLLLWEIVTLGRPARGERFDFGRYRSRLEVRRDGRLLLRDRLRLEP---GDAGAGRLGGYTVFGT 149
 
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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