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Conserved domains on  [gi|1177256066|gb|ARH02128|]
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CTP synthase, partial [Leuconostoc mesenteroides]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
pyrG super family cl35313
CTP synthetase; Validated
 1-136 7.56e-77

CTP synthetase; Validated


The actual alignment was detected with superfamily member PRK05380:

Pssm-ID: 235437 [Multi-domain]  Cd Length: 533  Bit Score: 236.46  E-value: 7.56e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1177256066   1 RSLGIQPDMIVLRTQRPLEENLKQKISTFTDVNENAVIESRDVETLYEIPLNLQAQGMDDVVLNKLKLDAPKAEMSDWSK 80
Cdd:PRK05380  198 RSIGIQPDILVCRSERPLPEEEKRKIALFCNVPEEAVISAPDVDSIYEVPLLLHEQGLDDIVLERLGLEAPEPDLSEWEE 277

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1177256066  81 MVELIKHPKKTVNVTLVGKYTDLPDAYISVNESLKHAGYAQDADVKINRVKSENVT 136
Cdd:PRK05380  278 LVERLKNPKGEVTIALVGKYVELPDAYKSVIEALKHAGIANDVKVNIKWIDSEDLE 333
 
Name Accession Description Interval E-value
pyrG PRK05380
CTP synthetase; Validated
 1-136 7.56e-77

CTP synthetase; Validated


Pssm-ID: 235437 [Multi-domain]  Cd Length: 533  Bit Score: 236.46  E-value: 7.56e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1177256066   1 RSLGIQPDMIVLRTQRPLEENLKQKISTFTDVNENAVIESRDVETLYEIPLNLQAQGMDDVVLNKLKLDAPKAEMSDWSK 80
Cdd:PRK05380  198 RSIGIQPDILVCRSERPLPEEEKRKIALFCNVPEEAVISAPDVDSIYEVPLLLHEQGLDDIVLERLGLEAPEPDLSEWEE 277

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1177256066  81 MVELIKHPKKTVNVTLVGKYTDLPDAYISVNESLKHAGYAQDADVKINRVKSENVT 136
Cdd:PRK05380  278 LVERLKNPKGEVTIALVGKYVELPDAYKSVIEALKHAGIANDVKVNIKWIDSEDLE 333
PyrG COG0504
CTP synthase (UTP-ammonia lyase) [Nucleotide transport and metabolism]; CTP synthase ...
 1-137 1.40e-75

CTP synthase (UTP-ammonia lyase) [Nucleotide transport and metabolism]; CTP synthase (UTP-ammonia lyase) is part of the Pathway/BioSystem: Pyrimidine biosynthesis


Pssm-ID: 440270 [Multi-domain]  Cd Length: 535  Bit Score: 233.36  E-value: 1.40e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1177256066   1 RSLGIQPDMIVLRTQRPLEENLKQKISTFTDVNENAVIESRDVETLYEIPLNLQAQGMDDVVLNKLKLDAPKAEMSDWSK 80
Cdd:COG0504   199 RSIGIQPDILVCRSERPLPEEIKRKIALFCNVPEEAVISAPDVDSIYEVPLMLHEQGLDEIVLKKLGLEAREPDLSEWEE 278

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1177256066  81 MVELIKHPKKTVNVTLVGKYTDLPDAYISVNESLKHAGYAQDADVKINRVKSENVTP 137
Cdd:COG0504   279 LVERIKNPKKEVTIALVGKYVELPDAYKSVVEALKHAGIANGVKVNIKWIDSEDLEE 335
CTP_synth_N pfam06418
CTP synthase N-terminus; This family consists of the N-terminal region of the CTP synthase ...
 1-68 2.98e-33

CTP synthase N-terminus; This family consists of the N-terminal region of the CTP synthase protein (EC:6.3.4.2). This family is found in conjunction with pfam00117 located in the C-terminal region of the protein. CTP synthase catalyzes the synthesis of CTP from UTP by amination of the pyrimidine ring at the 4-position.


Pssm-ID: 461903  Cd Length: 265  Bit Score: 117.06  E-value: 2.98e-33
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1177256066   1 RSLGIQPDMIVLRTQRPLEENLKQKISTFTDVNENAVIESRDVETLYEIPLNLQAQGMDDVVLNKLKL 68
Cdd:pfam06418 198 RSIGIQPDIIVCRSERPLDEEVKEKIALFCNVPKEAVISAPDVSSIYEVPLLLEEQGLDDIILKRLNL 265
CTPS_N cd03113
N-terminal domain of cytidine 5'-triphosphate synthase; Cytidine 5'-triphosphate synthase ...
 1-63 2.78e-24

N-terminal domain of cytidine 5'-triphosphate synthase; Cytidine 5'-triphosphate synthase (CTPS) is a two-domain protein, which consists of an N-terminal synthetase domain and C-terminal glutaminase domain. The enzymes hydrolyze the amide bond of glutamine to ammonia and glutamate at the glutaminase domains and transfer nascent ammonia to the acceptor substrate at the synthetase domain to form an aminated product.


Pssm-ID: 349767  Cd Length: 261  Bit Score: 93.70  E-value: 2.78e-24
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1177256066   1 RSLGIQPDMIVLRTQRPLEENLKQKISTFTDVNENAVIESRDVETLYEIPLNLQAQGMDDVVL 63
Cdd:cd03113   198 RSLGIQPDIIVCRSEKPLDEETKEKIALFCNVPPEAVISVHDVSSIYEVPLLLEKQGLDDYIL 260
 
Name Accession Description Interval E-value
pyrG PRK05380
CTP synthetase; Validated
 1-136 7.56e-77

CTP synthetase; Validated


Pssm-ID: 235437 [Multi-domain]  Cd Length: 533  Bit Score: 236.46  E-value: 7.56e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1177256066   1 RSLGIQPDMIVLRTQRPLEENLKQKISTFTDVNENAVIESRDVETLYEIPLNLQAQGMDDVVLNKLKLDAPKAEMSDWSK 80
Cdd:PRK05380  198 RSIGIQPDILVCRSERPLPEEEKRKIALFCNVPEEAVISAPDVDSIYEVPLLLHEQGLDDIVLERLGLEAPEPDLSEWEE 277

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1177256066  81 MVELIKHPKKTVNVTLVGKYTDLPDAYISVNESLKHAGYAQDADVKINRVKSENVT 136
Cdd:PRK05380  278 LVERLKNPKGEVTIALVGKYVELPDAYKSVIEALKHAGIANDVKVNIKWIDSEDLE 333
PyrG COG0504
CTP synthase (UTP-ammonia lyase) [Nucleotide transport and metabolism]; CTP synthase ...
 1-137 1.40e-75

CTP synthase (UTP-ammonia lyase) [Nucleotide transport and metabolism]; CTP synthase (UTP-ammonia lyase) is part of the Pathway/BioSystem: Pyrimidine biosynthesis


Pssm-ID: 440270 [Multi-domain]  Cd Length: 535  Bit Score: 233.36  E-value: 1.40e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1177256066   1 RSLGIQPDMIVLRTQRPLEENLKQKISTFTDVNENAVIESRDVETLYEIPLNLQAQGMDDVVLNKLKLDAPKAEMSDWSK 80
Cdd:COG0504   199 RSIGIQPDILVCRSERPLPEEIKRKIALFCNVPEEAVISAPDVDSIYEVPLMLHEQGLDEIVLKKLGLEAREPDLSEWEE 278

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1177256066  81 MVELIKHPKKTVNVTLVGKYTDLPDAYISVNESLKHAGYAQDADVKINRVKSENVTP 137
Cdd:COG0504   279 LVERIKNPKKEVTIALVGKYVELPDAYKSVVEALKHAGIANGVKVNIKWIDSEDLEE 335
CTP_synth_N pfam06418
CTP synthase N-terminus; This family consists of the N-terminal region of the CTP synthase ...
 1-68 2.98e-33

CTP synthase N-terminus; This family consists of the N-terminal region of the CTP synthase protein (EC:6.3.4.2). This family is found in conjunction with pfam00117 located in the C-terminal region of the protein. CTP synthase catalyzes the synthesis of CTP from UTP by amination of the pyrimidine ring at the 4-position.


Pssm-ID: 461903  Cd Length: 265  Bit Score: 117.06  E-value: 2.98e-33
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1177256066   1 RSLGIQPDMIVLRTQRPLEENLKQKISTFTDVNENAVIESRDVETLYEIPLNLQAQGMDDVVLNKLKL 68
Cdd:pfam06418 198 RSIGIQPDIIVCRSERPLDEEVKEKIALFCNVPKEAVISAPDVSSIYEVPLLLEEQGLDDIILKRLNL 265
PLN02327 PLN02327
CTP synthase
 1-122 9.96e-31

CTP synthase


Pssm-ID: 215186 [Multi-domain]  Cd Length: 557  Bit Score: 114.74  E-value: 9.96e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1177256066   1 RSLGIQPDMIVLRTQRPLEENLKQKISTFTDVNENAVIESRDVETLYEIPLNLQAQGMDDVVLNKLKLD--APKAEMSDW 78
Cdd:PLN02327  205 RALGLTPHILACRSTKPLEENVKEKLSQFCHVPAENILNLHDVSNIWHVPLLLRDQKAHEAILKVLNLLsvAREPDLEEW 284

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1177256066  79 SKMVELIKHPKKTVNVTLVGKYTDLPDAYISVNESLKHAGYAQD 122
Cdd:PLN02327  285 TARAESCDNLTEPVRIAMVGKYTGLSDSYLSVLKALLHASVACS 328
CTPS_N cd03113
N-terminal domain of cytidine 5'-triphosphate synthase; Cytidine 5'-triphosphate synthase ...
 1-63 2.78e-24

N-terminal domain of cytidine 5'-triphosphate synthase; Cytidine 5'-triphosphate synthase (CTPS) is a two-domain protein, which consists of an N-terminal synthetase domain and C-terminal glutaminase domain. The enzymes hydrolyze the amide bond of glutamine to ammonia and glutamate at the glutaminase domains and transfer nascent ammonia to the acceptor substrate at the synthetase domain to form an aminated product.


Pssm-ID: 349767  Cd Length: 261  Bit Score: 93.70  E-value: 2.78e-24
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1177256066   1 RSLGIQPDMIVLRTQRPLEENLKQKISTFTDVNENAVIESRDVETLYEIPLNLQAQGMDDVVL 63
Cdd:cd03113   198 RSLGIQPDIIVCRSEKPLDEETKEKIALFCNVPPEAVISVHDVSSIYEVPLLLEKQGLDDYIL 260
GATase1_CTP_Synthase cd01746
Type 1 glutamine amidotransferase (GATase1) domain found in Cytidine Triphosphate Synthetase; ...
 92-135 1.85e-15

Type 1 glutamine amidotransferase (GATase1) domain found in Cytidine Triphosphate Synthetase; Type 1 glutamine amidotransferase (GATase1) domain found in Cytidine Triphosphate Synthetase (CTP). CTP is involved in pyrimidine ribonucleotide/ribonucleoside metabolism. CTPs produce CTP from UTP and glutamine and regulate intracellular CTP levels through interactions with four ribonucleotide triphosphates. The enzyme exists as a dimer of identical chains that aggregates as a tetramer. CTP is derived form UTP in three separate steps involving two active sites. In one active site, the UTP O4 oxygen is activated by Mg-ATP-dependent phosphorylation, followed by displacement of the resulting 4-phosphate moiety by ammonia. At a separate site, ammonia is generated via rate limiting glutamine hydrolysis (glutaminase) activity. A gated channel that spans between the glutamine hydrolysis and amidoligase active sites provides a path for ammonia diffusion. CTPs belong to the triad family of amidotransferases having a conserved Cys-His-Glu catalytic triad in the glutaminase active site.


Pssm-ID: 153217 [Multi-domain]  Cd Length: 235  Bit Score: 69.89  E-value: 1.85e-15
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 1177256066  92 VNVTLVGKYTDLPDAYISVNESLKHAGYAQDADVKINRVKSENV 135
Cdd:cd01746     1 VRIALVGKYVELPDAYLSVLEALKHAGIALGVKLEIKWIDSEDL 44
 
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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