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Conserved domains on  [gi|974920650|gb|KUR01415|]
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hypothetical protein AWI32_00495 [Enterobacter bugandensis]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
CT_C_D super family cl19310
Carboxyltransferase domain, subdomain C and D; Urea carboxylase (UC) catalyzes a two-step, ...
9-211 5.45e-107

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.


The actual alignment was detected with superfamily member TIGR00370:

Pssm-ID: 473162  Cd Length: 202  Bit Score: 306.01  E-value: 5.45e-107
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974920650    9 LGETAVVLELEPPVTLATQKRIWRLAQRLPELPGVVEAIPGMNNITVVLrDPHTGALDAIERLQRWWEESEALEPESRTI 88
Cdd:TIGR00370   1 IGESAVVIRLGPPINEQVQGIVWAAAAYLEEQPGFVECIPGMNNLTVFY-DMYEVYKHLPQRLSSPWEEVKDYEVNRRII 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974920650   89 EIPVVYGGKGGPDLGVVAEHCGLTVKQVVELHSSVDYVVWFLGFQPGFPYLGGLSPRLHTPRRAEPRLSVPAGTVAIGGE 168
Cdd:TIGR00370  80 EIPVCYGGEFGPDLEEVAKINQLSPEEVIDIHSNGEYVVYMLGFQPGFPYLGGLPERLHTPRRASPRPSVPAGSVGIGGL 159
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 974920650  169 QTGVYPLTSPGGWQLIGHTSMPLFKPGQEAPILLRPGDTLRFI 211
Cdd:TIGR00370 160 QTGVYPISTPGGWQLIGKTPLALFDPQENPPTLLRAGDIVKFV 202
 
Name Accession Description Interval E-value
TIGR00370 TIGR00370
sensor histidine kinase inhibitor, KipI family; [Hypothetical proteins, Conserved]
9-211 5.45e-107

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


Pssm-ID: 129467  Cd Length: 202  Bit Score: 306.01  E-value: 5.45e-107
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974920650    9 LGETAVVLELEPPVTLATQKRIWRLAQRLPELPGVVEAIPGMNNITVVLrDPHTGALDAIERLQRWWEESEALEPESRTI 88
Cdd:TIGR00370   1 IGESAVVIRLGPPINEQVQGIVWAAAAYLEEQPGFVECIPGMNNLTVFY-DMYEVYKHLPQRLSSPWEEVKDYEVNRRII 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974920650   89 EIPVVYGGKGGPDLGVVAEHCGLTVKQVVELHSSVDYVVWFLGFQPGFPYLGGLSPRLHTPRRAEPRLSVPAGTVAIGGE 168
Cdd:TIGR00370  80 EIPVCYGGEFGPDLEEVAKINQLSPEEVIDIHSNGEYVVYMLGFQPGFPYLGGLPERLHTPRRASPRPSVPAGSVGIGGL 159
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 974920650  169 QTGVYPLTSPGGWQLIGHTSMPLFKPGQEAPILLRPGDTLRFI 211
Cdd:TIGR00370 160 QTGVYPISTPGGWQLIGKTPLALFDPQENPPTLLRAGDIVKFV 202
PxpB COG2049
5-oxoprolinase subunit B/Allophanate hydrolase subunit 1 [Amino acid transport and metabolism]; ...
1-215 1.14e-103

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


Pssm-ID: 441652  Cd Length: 229  Bit Score: 298.59  E-value: 1.14e-103
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974920650   1 MQRARCYLLGETAVVLELEPPVTLATQKRIWRLAQRLPE--LPGVVEAIPGMNNITVVLRDPHTGALDAIERLQRWWEE- 77
Cdd:COG2049    2 RMAMRILPAGDRALLVEFGDEIDLELNRRVLALAAALRAapLPGVVEVVPAYRSLLVHFDPLVIDPAALAARLRALLAEl 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974920650  78 SEALEPESRTIEIPVVYGGKGGPDLGVVAEHCGLTVKQVVELHSSVDYVVWFLGFQPGFPYLGGLSPRLHTPRRAEPRLS 157
Cdd:COG2049   82 DAAAEVPSRLVEIPVCYDGEFGPDLEEVARHNGLSVEEVIALHTAAEYRVYMLGFAPGFPYLGGLDPRLATPRRATPRTR 161
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 974920650 158 VPAGTVAIGGEQTGVYPLTSPGGWQLIGHTSMPLFKPGQEAPILLRPGDTLRFIPQKE 215
Cdd:COG2049  162 VPAGSVGIAGAQTGIYPLESPGGWQLIGRTPLPLFDPDREPPALLRPGDRVRFVPISE 219
CT_C_D pfam02682
Carboxyltransferase domain, subdomain C and D; Urea carboxylase (UC) catalyzes a two-step, ...
5-202 9.16e-95

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: 275.20  E-value: 9.16e-95
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974920650    5 RCYLLGETAVVLELEPPVTLATQKRIWRLAQRLPE--LPGVVEAIPGMNNITVVLRDPHTGALDAIERLQRWWEE-SEAL 81
Cdd:pfam02682   1 RIRPAGDRALLVEFGDEIDLALNRRVLALAAALRAapLPGVVEVVPGYRSLLVHYDPLVTDLAALEARLRALLAAlEAAA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974920650   82 EPESRTIEIPVVYGGKGGPDLGVVAEHCGLTVKQVVELHSSVDYVVWFLGFQPGFPYLGGLSPRLHTPRRAEPRLSVPAG 161
Cdd:pfam02682  81 APGGRLIEIPVCYDGEFGPDLAEVAAHNGLSVEEVIRLHSAAEYRVYFLGFAPGFPYLGGLDPRLAVPRRATPRTRVPAG 160
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 974920650  162 TVAIGGEQTGVYPLTSPGGWQLIGHTSMPLFKPGQEAPILL 202
Cdd:pfam02682 161 SVGIAGRQTGIYPLESPGGWQLIGRTPLPLFDPDRDPPALL 201
AHS1 smart00796
Allophanate hydrolase subunit 1; This domain represents subunit 1 of allophanate hydrolase ...
5-199 3.15e-91

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


Pssm-ID: 214820  Cd Length: 201  Bit Score: 265.93  E-value: 3.15e-91
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974920650     5 RCYLLGETAVVLELEPPVTLATQKRIWRLAQRLPE--LPGVVEAIPGMNNITVVLRDPHTGALDAIERLQRWWEE--SEA 80
Cdd:smart00796   2 RIRPAGDRALLVEFGDEIDLALNRRVLALARALRAapLPGVVELVPGYRSLLVHFDPLVIDPAALLARLRALEALplAEA 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974920650    81 LEPESRTIEIPVVYGGKGGPDLGVVAEHCGLTVKQVVELHSSVDYVVWFLGFQPGFPYLGGLSPRLHTPRRAEPRLSVPA 160
Cdd:smart00796  82 LEVPGRIIEIPVCYGGEFGPDLEFVARHNGLSVDEVIRLHSAAEYRVYMLGFAPGFPYLGGLDPRLATPRRSTPRTRVPA 161
                          170       180       190
                   ....*....|....*....|....*....|....*....
gi 974920650   161 GTVAIGGEQTGVYPLTSPGGWQLIGHTSMPLFKPGQEAP 199
Cdd:smart00796 162 GSVGIAGAQTGIYPLESPGGWQLIGRTPLPLFDPDREPP 200
 
Name Accession Description Interval E-value
TIGR00370 TIGR00370
sensor histidine kinase inhibitor, KipI family; [Hypothetical proteins, Conserved]
9-211 5.45e-107

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


Pssm-ID: 129467  Cd Length: 202  Bit Score: 306.01  E-value: 5.45e-107
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974920650    9 LGETAVVLELEPPVTLATQKRIWRLAQRLPELPGVVEAIPGMNNITVVLrDPHTGALDAIERLQRWWEESEALEPESRTI 88
Cdd:TIGR00370   1 IGESAVVIRLGPPINEQVQGIVWAAAAYLEEQPGFVECIPGMNNLTVFY-DMYEVYKHLPQRLSSPWEEVKDYEVNRRII 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974920650   89 EIPVVYGGKGGPDLGVVAEHCGLTVKQVVELHSSVDYVVWFLGFQPGFPYLGGLSPRLHTPRRAEPRLSVPAGTVAIGGE 168
Cdd:TIGR00370  80 EIPVCYGGEFGPDLEEVAKINQLSPEEVIDIHSNGEYVVYMLGFQPGFPYLGGLPERLHTPRRASPRPSVPAGSVGIGGL 159
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 974920650  169 QTGVYPLTSPGGWQLIGHTSMPLFKPGQEAPILLRPGDTLRFI 211
Cdd:TIGR00370 160 QTGVYPISTPGGWQLIGKTPLALFDPQENPPTLLRAGDIVKFV 202
PxpB COG2049
5-oxoprolinase subunit B/Allophanate hydrolase subunit 1 [Amino acid transport and metabolism]; ...
1-215 1.14e-103

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


Pssm-ID: 441652  Cd Length: 229  Bit Score: 298.59  E-value: 1.14e-103
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974920650   1 MQRARCYLLGETAVVLELEPPVTLATQKRIWRLAQRLPE--LPGVVEAIPGMNNITVVLRDPHTGALDAIERLQRWWEE- 77
Cdd:COG2049    2 RMAMRILPAGDRALLVEFGDEIDLELNRRVLALAAALRAapLPGVVEVVPAYRSLLVHFDPLVIDPAALAARLRALLAEl 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974920650  78 SEALEPESRTIEIPVVYGGKGGPDLGVVAEHCGLTVKQVVELHSSVDYVVWFLGFQPGFPYLGGLSPRLHTPRRAEPRLS 157
Cdd:COG2049   82 DAAAEVPSRLVEIPVCYDGEFGPDLEEVARHNGLSVEEVIALHTAAEYRVYMLGFAPGFPYLGGLDPRLATPRRATPRTR 161
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 974920650 158 VPAGTVAIGGEQTGVYPLTSPGGWQLIGHTSMPLFKPGQEAPILLRPGDTLRFIPQKE 215
Cdd:COG2049  162 VPAGSVGIAGAQTGIYPLESPGGWQLIGRTPLPLFDPDREPPALLRPGDRVRFVPISE 219
CT_C_D pfam02682
Carboxyltransferase domain, subdomain C and D; Urea carboxylase (UC) catalyzes a two-step, ...
5-202 9.16e-95

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: 275.20  E-value: 9.16e-95
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974920650    5 RCYLLGETAVVLELEPPVTLATQKRIWRLAQRLPE--LPGVVEAIPGMNNITVVLRDPHTGALDAIERLQRWWEE-SEAL 81
Cdd:pfam02682   1 RIRPAGDRALLVEFGDEIDLALNRRVLALAAALRAapLPGVVEVVPGYRSLLVHYDPLVTDLAALEARLRALLAAlEAAA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974920650   82 EPESRTIEIPVVYGGKGGPDLGVVAEHCGLTVKQVVELHSSVDYVVWFLGFQPGFPYLGGLSPRLHTPRRAEPRLSVPAG 161
Cdd:pfam02682  81 APGGRLIEIPVCYDGEFGPDLAEVAAHNGLSVEEVIRLHSAAEYRVYFLGFAPGFPYLGGLDPRLAVPRRATPRTRVPAG 160
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 974920650  162 TVAIGGEQTGVYPLTSPGGWQLIGHTSMPLFKPGQEAPILL 202
Cdd:pfam02682 161 SVGIAGRQTGIYPLESPGGWQLIGRTPLPLFDPDRDPPALL 201
AHS1 smart00796
Allophanate hydrolase subunit 1; This domain represents subunit 1 of allophanate hydrolase ...
5-199 3.15e-91

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


Pssm-ID: 214820  Cd Length: 201  Bit Score: 265.93  E-value: 3.15e-91
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974920650     5 RCYLLGETAVVLELEPPVTLATQKRIWRLAQRLPE--LPGVVEAIPGMNNITVVLRDPHTGALDAIERLQRWWEE--SEA 80
Cdd:smart00796   2 RIRPAGDRALLVEFGDEIDLALNRRVLALARALRAapLPGVVELVPGYRSLLVHFDPLVIDPAALLARLRALEALplAEA 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974920650    81 LEPESRTIEIPVVYGGKGGPDLGVVAEHCGLTVKQVVELHSSVDYVVWFLGFQPGFPYLGGLSPRLHTPRRAEPRLSVPA 160
Cdd:smart00796  82 LEVPGRIIEIPVCYGGEFGPDLEFVARHNGLSVDEVIRLHSAAEYRVYMLGFAPGFPYLGGLDPRLATPRRSTPRTRVPA 161
                          170       180       190
                   ....*....|....*....|....*....|....*....
gi 974920650   161 GTVAIGGEQTGVYPLTSPGGWQLIGHTSMPLFKPGQEAP 199
Cdd:smart00796 162 GSVGIAGAQTGIYPLESPGGWQLIGRTPLPLFDPDREPP 200
 
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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