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Conserved domains on  [gi|1590333710|ref|WP_131655293|]
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5-oxoprolinase subunit PxpB [Pseudomonas taetrolens]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PxpB COG2049
5-oxoprolinase subunit B/Allophanate hydrolase subunit 1 [Amino acid transport and metabolism]; ...
1-226 3.22e-90

5-oxoprolinase subunit B/Allophanate hydrolase subunit 1 [Amino acid transport and metabolism];


:

Pssm-ID: 441652  Cd Length: 229  Bit Score: 265.08  E-value: 3.22e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590333710   1 MKPRIEVVAIDCLMLRLFDEIAETNMPWMLAASQRLRAGFAGHLIDLVPSYTTLMVHYDGLALSPGQARELIAQALTDLQ 80
Cdd:COG2049     3 MAMRILPAGDRALLVEFGDEIDLELNRRVLALAAALRAAPLPGVVEVVPAYRSLLVHFDPLVIDPAALAARLRALLAELD 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590333710  81 PDTQSRGQCHVLPVWYDVSVGPELTLLAERTGWSVSEVIRRHSEHHYQVFALGFAPGFAFMGLVEEALAAPRLATPRKRV 160
Cdd:COG2049    83 AAAEVPSRLVEIPVCYDGEFGPDLEEVARHNGLSVEEVIALHTAAEYRVYMLGFAPGFPYLGGLDPRLATPRRATPRTRV 162
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1590333710 161 AAGSVGIAERQTAAYPAQSPGGWNLIGRTPSALFDREREGYSLMQPGDSVQFAPVSHAEFINLGGD 226
Cdd:COG2049   163 PAGSVGIAGAQTGIYPLESPGGWQLIGRTPLPLFDPDREPPALLRPGDRVRFVPISEEEFDALRGE 228
 
Name Accession Description Interval E-value
PxpB COG2049
5-oxoprolinase subunit B/Allophanate hydrolase subunit 1 [Amino acid transport and metabolism]; ...
1-226 3.22e-90

5-oxoprolinase subunit B/Allophanate hydrolase subunit 1 [Amino acid transport and metabolism];


Pssm-ID: 441652  Cd Length: 229  Bit Score: 265.08  E-value: 3.22e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590333710   1 MKPRIEVVAIDCLMLRLFDEIAETNMPWMLAASQRLRAGFAGHLIDLVPSYTTLMVHYDGLALSPGQARELIAQALTDLQ 80
Cdd:COG2049     3 MAMRILPAGDRALLVEFGDEIDLELNRRVLALAAALRAAPLPGVVEVVPAYRSLLVHFDPLVIDPAALAARLRALLAELD 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590333710  81 PDTQSRGQCHVLPVWYDVSVGPELTLLAERTGWSVSEVIRRHSEHHYQVFALGFAPGFAFMGLVEEALAAPRLATPRKRV 160
Cdd:COG2049    83 AAAEVPSRLVEIPVCYDGEFGPDLEEVARHNGLSVEEVIALHTAAEYRVYMLGFAPGFPYLGGLDPRLATPRRATPRTRV 162
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1590333710 161 AAGSVGIAERQTAAYPAQSPGGWNLIGRTPSALFDREREGYSLMQPGDSVQFAPVSHAEFINLGGD 226
Cdd:COG2049   163 PAGSVGIAGAQTGIYPLESPGGWQLIGRTPLPLFDPDREPPALLRPGDRVRFVPISEEEFDALRGE 228
AHS1 smart00796
Allophanate hydrolase subunit 1; This domain represents subunit 1 of allophanate hydrolase ...
3-202 1.06e-79

Allophanate hydrolase subunit 1; This domain represents subunit 1 of allophanate hydrolase (AHS1).


Pssm-ID: 214820  Cd Length: 201  Bit Score: 237.42  E-value: 1.06e-79
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590333710    3 PRIEVVAIDCLMLRLFDEIAETNMPWMLAASQRLRAGFAGHLIDLVPSYTTLMVHYDGLALSPGQARELIAQALTDLQ-P 81
Cdd:smart00796   1 MRIRPAGDRALLVEFGDEIDLALNRRVLALARALRAAPLPGVVELVPGYRSLLVHFDPLVIDPAALLARLRALEALPLaE 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590333710   82 DTQSRGQCHVLPVWYDVSVGPELTLLAERTGWSVSEVIRRHSEHHYQVFALGFAPGFAFMGLVEEALAAPRLATPRKRVA 161
Cdd:smart00796  81 ALEVPGRIIEIPVCYGGEFGPDLEFVARHNGLSVDEVIRLHSAAEYRVYMLGFAPGFPYLGGLDPRLATPRRSTPRTRVP 160
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|.
gi 1590333710  162 AGSVGIAERQTAAYPAQSPGGWNLIGRTPSALFDREREGYS 202
Cdd:smart00796 161 AGSVGIAGAQTGIYPLESPGGWQLIGRTPLPLFDPDREPPA 201
CT_C_D pfam02682
Carboxyltransferase domain, subdomain C and D; Urea carboxylase (UC) catalyzes a two-step, ...
4-204 1.03e-76

Carboxyltransferase domain, subdomain C and D; Urea carboxylase (UC) catalyzes a two-step, ATP- and biotin-dependent carboxylation reaction of urea. It is composed of biotin carboxylase (BC), carboxyltransferase (CT), and biotin carboxyl carrier protein (BCCP) domains. The CT domain of UC consists of four subdomains, named A, B, C and D. This domain covers the C and D subdomains of the CT domain. This domain covers the whole length of kipI (kinase A inhibitor) from Bacillus subtilis. It can also be found in S. cerevisiae urea amidolyase Dur1,2, which is a multifunctional biotin-dependent enzyme with domains for urea carboxylase and allophanate (urea carboxylate) hydrolase activity.


Pssm-ID: 426925  Cd Length: 201  Bit Score: 230.14  E-value: 1.03e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590333710   4 RIEVVAIDCLMLRLFDEIAETNMPWMLAASQRLRAGFAGHLIDLVPSYTTLMVHYDGLALSPGQARELIAQALTDLQPDT 83
Cdd:pfam02682   1 RIRPAGDRALLVEFGDEIDLALNRRVLALAAALRAAPLPGVVEVVPGYRSLLVHYDPLVTDLAALEARLRALLAALEAAA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590333710  84 QSRGQCHVLPVWYDVSVGPELTLLAERTGWSVSEVIRRHSEHHYQVFALGFAPGFAFMGLVEEALAAPRLATPRKRVAAG 163
Cdd:pfam02682  81 APGGRLIEIPVCYDGEFGPDLAEVAAHNGLSVEEVIRLHSAAEYRVYFLGFAPGFPYLGGLDPRLAVPRRATPRTRVPAG 160
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1590333710 164 SVGIAERQTAAYPAQSPGGWNLIGRTPSALFDREREGYSLM 204
Cdd:pfam02682 161 SVGIAGRQTGIYPLESPGGWQLIGRTPLPLFDPDRDPPALL 201
TIGR00370 TIGR00370
sensor histidine kinase inhibitor, KipI family; [Hypothetical proteins, Conserved]
13-212 2.98e-39

sensor histidine kinase inhibitor, KipI family; [Hypothetical proteins, Conserved]


Pssm-ID: 129467  Cd Length: 202  Bit Score: 134.60  E-value: 2.98e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590333710  13 LMLRLFDEIAETNMPWMLAASQRLRAgfAGHLIDLVPSYTTLMVHYD--GLALSPGQARELIAQALTDLQPdtQSRgqcH 90
Cdd:TIGR00370   6 VVIRLGPPINEQVQGIVWAAAAYLEE--QPGFVECIPGMNNLTVFYDmyEVYKHLPQRLSSPWEEVKDYEV--NRR---I 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590333710  91 V-LPVWYDVSVGPELTLLAERTGWSVSEVIRRHSEHHYQVFALGFAPGFAFMGLVEEALAAPRLATPRKRVAAGSVGIAE 169
Cdd:TIGR00370  79 IeIPVCYGGEFGPDLEEVAKINQLSPEEVIDIHSNGEYVVYMLGFQPGFPYLGGLPERLHTPRRASPRPSVPAGSVGIGG 158
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1590333710 170 RQTAAYPAQSPGGWNLIGRTPSALFDREREGYSLMQPGDSVQF 212
Cdd:TIGR00370 159 LQTGVYPISTPGGWQLIGKTPLALFDPQENPPTLLRAGDIVKF 201
 
Name Accession Description Interval E-value
PxpB COG2049
5-oxoprolinase subunit B/Allophanate hydrolase subunit 1 [Amino acid transport and metabolism]; ...
1-226 3.22e-90

5-oxoprolinase subunit B/Allophanate hydrolase subunit 1 [Amino acid transport and metabolism];


Pssm-ID: 441652  Cd Length: 229  Bit Score: 265.08  E-value: 3.22e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590333710   1 MKPRIEVVAIDCLMLRLFDEIAETNMPWMLAASQRLRAGFAGHLIDLVPSYTTLMVHYDGLALSPGQARELIAQALTDLQ 80
Cdd:COG2049     3 MAMRILPAGDRALLVEFGDEIDLELNRRVLALAAALRAAPLPGVVEVVPAYRSLLVHFDPLVIDPAALAARLRALLAELD 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590333710  81 PDTQSRGQCHVLPVWYDVSVGPELTLLAERTGWSVSEVIRRHSEHHYQVFALGFAPGFAFMGLVEEALAAPRLATPRKRV 160
Cdd:COG2049    83 AAAEVPSRLVEIPVCYDGEFGPDLEEVARHNGLSVEEVIALHTAAEYRVYMLGFAPGFPYLGGLDPRLATPRRATPRTRV 162
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1590333710 161 AAGSVGIAERQTAAYPAQSPGGWNLIGRTPSALFDREREGYSLMQPGDSVQFAPVSHAEFINLGGD 226
Cdd:COG2049   163 PAGSVGIAGAQTGIYPLESPGGWQLIGRTPLPLFDPDREPPALLRPGDRVRFVPISEEEFDALRGE 228
AHS1 smart00796
Allophanate hydrolase subunit 1; This domain represents subunit 1 of allophanate hydrolase ...
3-202 1.06e-79

Allophanate hydrolase subunit 1; This domain represents subunit 1 of allophanate hydrolase (AHS1).


Pssm-ID: 214820  Cd Length: 201  Bit Score: 237.42  E-value: 1.06e-79
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590333710    3 PRIEVVAIDCLMLRLFDEIAETNMPWMLAASQRLRAGFAGHLIDLVPSYTTLMVHYDGLALSPGQARELIAQALTDLQ-P 81
Cdd:smart00796   1 MRIRPAGDRALLVEFGDEIDLALNRRVLALARALRAAPLPGVVELVPGYRSLLVHFDPLVIDPAALLARLRALEALPLaE 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590333710   82 DTQSRGQCHVLPVWYDVSVGPELTLLAERTGWSVSEVIRRHSEHHYQVFALGFAPGFAFMGLVEEALAAPRLATPRKRVA 161
Cdd:smart00796  81 ALEVPGRIIEIPVCYGGEFGPDLEFVARHNGLSVDEVIRLHSAAEYRVYMLGFAPGFPYLGGLDPRLATPRRSTPRTRVP 160
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|.
gi 1590333710  162 AGSVGIAERQTAAYPAQSPGGWNLIGRTPSALFDREREGYS 202
Cdd:smart00796 161 AGSVGIAGAQTGIYPLESPGGWQLIGRTPLPLFDPDREPPA 201
CT_C_D pfam02682
Carboxyltransferase domain, subdomain C and D; Urea carboxylase (UC) catalyzes a two-step, ...
4-204 1.03e-76

Carboxyltransferase domain, subdomain C and D; Urea carboxylase (UC) catalyzes a two-step, ATP- and biotin-dependent carboxylation reaction of urea. It is composed of biotin carboxylase (BC), carboxyltransferase (CT), and biotin carboxyl carrier protein (BCCP) domains. The CT domain of UC consists of four subdomains, named A, B, C and D. This domain covers the C and D subdomains of the CT domain. This domain covers the whole length of kipI (kinase A inhibitor) from Bacillus subtilis. It can also be found in S. cerevisiae urea amidolyase Dur1,2, which is a multifunctional biotin-dependent enzyme with domains for urea carboxylase and allophanate (urea carboxylate) hydrolase activity.


Pssm-ID: 426925  Cd Length: 201  Bit Score: 230.14  E-value: 1.03e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590333710   4 RIEVVAIDCLMLRLFDEIAETNMPWMLAASQRLRAGFAGHLIDLVPSYTTLMVHYDGLALSPGQARELIAQALTDLQPDT 83
Cdd:pfam02682   1 RIRPAGDRALLVEFGDEIDLALNRRVLALAAALRAAPLPGVVEVVPGYRSLLVHYDPLVTDLAALEARLRALLAALEAAA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590333710  84 QSRGQCHVLPVWYDVSVGPELTLLAERTGWSVSEVIRRHSEHHYQVFALGFAPGFAFMGLVEEALAAPRLATPRKRVAAG 163
Cdd:pfam02682  81 APGGRLIEIPVCYDGEFGPDLAEVAAHNGLSVEEVIRLHSAAEYRVYFLGFAPGFPYLGGLDPRLAVPRRATPRTRVPAG 160
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1590333710 164 SVGIAERQTAAYPAQSPGGWNLIGRTPSALFDREREGYSLM 204
Cdd:pfam02682 161 SVGIAGRQTGIYPLESPGGWQLIGRTPLPLFDPDRDPPALL 201
TIGR00370 TIGR00370
sensor histidine kinase inhibitor, KipI family; [Hypothetical proteins, Conserved]
13-212 2.98e-39

sensor histidine kinase inhibitor, KipI family; [Hypothetical proteins, Conserved]


Pssm-ID: 129467  Cd Length: 202  Bit Score: 134.60  E-value: 2.98e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590333710  13 LMLRLFDEIAETNMPWMLAASQRLRAgfAGHLIDLVPSYTTLMVHYD--GLALSPGQARELIAQALTDLQPdtQSRgqcH 90
Cdd:TIGR00370   6 VVIRLGPPINEQVQGIVWAAAAYLEE--QPGFVECIPGMNNLTVFYDmyEVYKHLPQRLSSPWEEVKDYEV--NRR---I 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590333710  91 V-LPVWYDVSVGPELTLLAERTGWSVSEVIRRHSEHHYQVFALGFAPGFAFMGLVEEALAAPRLATPRKRVAAGSVGIAE 169
Cdd:TIGR00370  79 IeIPVCYGGEFGPDLEEVAKINQLSPEEVIDIHSNGEYVVYMLGFQPGFPYLGGLPERLHTPRRASPRPSVPAGSVGIGG 158
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1590333710 170 RQTAAYPAQSPGGWNLIGRTPSALFDREREGYSLMQPGDSVQF 212
Cdd:TIGR00370 159 LQTGVYPISTPGGWQLIGKTPLALFDPQENPPTLLRAGDIVKF 201
 
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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