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Conserved domains on  [gi|818652471|gb|KKS99070|]
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hypothetical protein UV75_C0011G0019 [Candidatus Giovannonibacteria bacterium GW2011_GWA1_43_15]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
NT_Pol-beta-like super family cl11966
Nucleotidyltransferase (NT) domain of DNA polymerase beta and similar proteins; This ...
 38-133 1.85e-13

Nucleotidyltransferase (NT) domain of DNA polymerase beta and similar proteins; This superfamily includes the NT domains of DNA polymerase beta and other family X DNA polymerases, as well as the NT domains of Class I and Class II CCA-adding enzymes, RelA- and SpoT-like ppGpp synthetases and hydrolases, 2'5'-oligoadenylate (2-5A)synthetases, Escherichia coli adenylyltransferase (GlnE), Escherichia coli uridylyl transferase (GlnD), poly (A) polymerases, terminal uridylyl transferases, and Staphylococcus aureus kanamycin nucleotidyltransferase, and similar proteins. The Escherichia coli CCA-adding enzyme belongs to this superfamily but is not included as this enzyme lacks the N-terminal helix conserved in the remainder of the superfamily. In the majority of the Pol beta-like superfamily NTs, two carboxylates, Dx[D/E], together with a third more distal carboxylate coordinate two divalent metal cations that are essential for catalysis. These divalent metal ions are involved in a two-metal ion mechanism of nucleotide addition. Two of the three catalytic carboxylates are found in Rel-Spo enzymes, with the second carboxylate of the DXD motif missing. Evidence supports a single-cation synthetase mechanism for Rel-Spo enzymes.


The actual alignment was detected with superfamily member TIGR00691:

Pssm-ID: 472251 [Multi-domain]  Cd Length: 683  Bit Score: 67.42  E-value: 1.85e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818652471   38 PIIMHSLRVGSELMEFKQEKNIVIAGFLHDLLEDTDCKPKEIEKEFGKKVVRLVLACTSDENIKdYKERWRKLVSNIKQ- 116
Cdd:TIGR00691  19 PYIIHPLAVALILAELGMDEETVCAALLHDVIEDTPVTEEEIEEEFGEEVAELVDGVTKITKLK-KKSRQELQAENFRKm 97

                          90       100
                  ....*....|....*....|..
gi 818652471  117 ---AGHD--AIIIKLIDQIANL 133
Cdd:TIGR00691  98 ilaMAQDirVIVIKLADRLHNM 119
 
Name Accession Description Interval E-value
spoT_relA TIGR00691
(p)ppGpp synthetase, RelA/SpoT family; The functions of E. coli RelA and SpoT differ somewhat. ...
 38-133 1.85e-13

(p)ppGpp synthetase, RelA/SpoT family; The functions of E. coli RelA and SpoT differ somewhat. RelA (EC 2.7.6.5) produces pppGpp (or ppGpp) from ATP and GTP (or GDP). SpoT (EC 3.1.7.2) degrades ppGpp, but may also act as a secondary ppGpp synthetase. The two proteins are strongly similar. In many species, a single homolog to SpoT and RelA appears reponsible for both ppGpp synthesis and ppGpp degradation. (p)ppGpp is a regulatory metabolite of the stringent response, but appears also to be involved in antibiotic biosynthesis in some species. [Cellular processes, Adaptations to atypical conditions]


Pssm-ID: 213552 [Multi-domain]  Cd Length: 683  Bit Score: 67.42  E-value: 1.85e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818652471   38 PIIMHSLRVGSELMEFKQEKNIVIAGFLHDLLEDTDCKPKEIEKEFGKKVVRLVLACTSDENIKdYKERWRKLVSNIKQ- 116
Cdd:TIGR00691  19 PYIIHPLAVALILAELGMDEETVCAALLHDVIEDTPVTEEEIEEEFGEEVAELVDGVTKITKLK-KKSRQELQAENFRKm 97

                          90       100
                  ....*....|....*....|..
gi 818652471  117 ---AGHD--AIIIKLIDQIANL 133
Cdd:TIGR00691  98 ilaMAQDirVIVIKLADRLHNM 119
SpoT COG0317
(p)ppGpp synthase/hydrolase, HD superfamily [Signal transduction mechanisms, Transcription];
9-95 5.67e-11

(p)ppGpp synthase/hydrolase, HD superfamily [Signal transduction mechanisms, Transcription];


Pssm-ID: 440086 [Multi-domain]  Cd Length: 722  Bit Score: 60.17  E-value: 5.67e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818652471   9 TYTPDAQ-KQIERAIVFmikkIEEHCYNEK-----PIIMHSLRVGSELMEFKQEKNIVIAGFLHDLLEDTDCKPKEIEKE 82
Cdd:COG0317   22 AYLPPADiALIRRAYEF----AEEAHEGQKrksgePYITHPLAVAEILAELGLDAETIAAALLHDVVEDTDVTLEEIEEE 97

                         90
                 ....*....|...
gi 818652471  83 FGKKVVRLVLACT 95
Cdd:COG0317   98 FGEEVAELVDGVT 110
HD_4 pfam13328
HD domain; HD domains are metal dependent phosphohydrolases.
 40-136 9.80e-10

HD domain; HD domains are metal dependent phosphohydrolases.


Pssm-ID: 433119 [Multi-domain]  Cd Length: 157  Bit Score: 54.58  E-value: 9.80e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818652471   40 IMHSLRVGSElmefkqeknIVIAGFLHDLLEDTDCKPKEIEKEFGKKVVRLVLACT------------SDENIKDYKERW 107
Cdd:pfam13328  30 ILAELGLDAD---------TVIAALLHDVVEDTGGSLEEIEERFGDEVARLVEGVSrldriqklaardWAERKAAQAENL 100

                          90       100       110
                  ....*....|....*....|....*....|...
gi 818652471  108 RKL----VSNIKqaghdAIIIKLIDQIANLPYY 136
Cdd:pfam13328 101 RKMllamVEDIR-----VVLVKLADRLQTLRSL 128
PRK11092 PRK11092
bifunctional GTP diphosphokinase/guanosine-3',5'-bis pyrophosphate 3'-pyrophosphohydrolase;
37-133 1.77e-06

bifunctional GTP diphosphokinase/guanosine-3',5'-bis pyrophosphate 3'-pyrophosphohydrolase;


Pssm-ID: 236843 [Multi-domain]  Cd Length: 702  Bit Score: 47.04  E-value: 1.77e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818652471  37 KPIIMHSLRVGSELMEFKQEKNIVIAGFLHDLLEDTDCKPKEIEKEFGKKVVRLVLACTSDENIK--DYK----ERWRKL 110
Cdd:PRK11092  43 EPYITHPVAVACILAEMRLDYETLMAALLHDVIEDTPATYQDMEQLFGKSVAELVEGVSKLDKLKfrDKKeaqaENFRKM 122

                         90       100
                 ....*....|....*....|....*
gi 818652471 111 VSNIKQaghD--AIIIKLIDQIANL 133
Cdd:PRK11092 123 IMAMVQ---DirVILIKLADRTHNM 144
 
Name Accession Description Interval E-value
spoT_relA TIGR00691
(p)ppGpp synthetase, RelA/SpoT family; The functions of E. coli RelA and SpoT differ somewhat. ...
 38-133 1.85e-13

(p)ppGpp synthetase, RelA/SpoT family; The functions of E. coli RelA and SpoT differ somewhat. RelA (EC 2.7.6.5) produces pppGpp (or ppGpp) from ATP and GTP (or GDP). SpoT (EC 3.1.7.2) degrades ppGpp, but may also act as a secondary ppGpp synthetase. The two proteins are strongly similar. In many species, a single homolog to SpoT and RelA appears reponsible for both ppGpp synthesis and ppGpp degradation. (p)ppGpp is a regulatory metabolite of the stringent response, but appears also to be involved in antibiotic biosynthesis in some species. [Cellular processes, Adaptations to atypical conditions]


Pssm-ID: 213552 [Multi-domain]  Cd Length: 683  Bit Score: 67.42  E-value: 1.85e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818652471   38 PIIMHSLRVGSELMEFKQEKNIVIAGFLHDLLEDTDCKPKEIEKEFGKKVVRLVLACTSDENIKdYKERWRKLVSNIKQ- 116
Cdd:TIGR00691  19 PYIIHPLAVALILAELGMDEETVCAALLHDVIEDTPVTEEEIEEEFGEEVAELVDGVTKITKLK-KKSRQELQAENFRKm 97

                          90       100
                  ....*....|....*....|..
gi 818652471  117 ---AGHD--AIIIKLIDQIANL 133
Cdd:TIGR00691  98 ilaMAQDirVIVIKLADRLHNM 119
SpoT COG0317
(p)ppGpp synthase/hydrolase, HD superfamily [Signal transduction mechanisms, Transcription];
9-95 5.67e-11

(p)ppGpp synthase/hydrolase, HD superfamily [Signal transduction mechanisms, Transcription];


Pssm-ID: 440086 [Multi-domain]  Cd Length: 722  Bit Score: 60.17  E-value: 5.67e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818652471   9 TYTPDAQ-KQIERAIVFmikkIEEHCYNEK-----PIIMHSLRVGSELMEFKQEKNIVIAGFLHDLLEDTDCKPKEIEKE 82
Cdd:COG0317   22 AYLPPADiALIRRAYEF----AEEAHEGQKrksgePYITHPLAVAEILAELGLDAETIAAALLHDVVEDTDVTLEEIEEE 97

                         90
                 ....*....|...
gi 818652471  83 FGKKVVRLVLACT 95
Cdd:COG0317   98 FGEEVAELVDGVT 110
HD_4 pfam13328
HD domain; HD domains are metal dependent phosphohydrolases.
 40-136 9.80e-10

HD domain; HD domains are metal dependent phosphohydrolases.


Pssm-ID: 433119 [Multi-domain]  Cd Length: 157  Bit Score: 54.58  E-value: 9.80e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818652471   40 IMHSLRVGSElmefkqeknIVIAGFLHDLLEDTDCKPKEIEKEFGKKVVRLVLACT------------SDENIKDYKERW 107
Cdd:pfam13328  30 ILAELGLDAD---------TVIAALLHDVVEDTGGSLEEIEERFGDEVARLVEGVSrldriqklaardWAERKAAQAENL 100

                          90       100       110
                  ....*....|....*....|....*....|...
gi 818652471  108 RKL----VSNIKqaghdAIIIKLIDQIANLPYY 136
Cdd:pfam13328 101 RKMllamVEDIR-----VVLVKLADRLQTLRSL 128
PRK11092 PRK11092
bifunctional GTP diphosphokinase/guanosine-3',5'-bis pyrophosphate 3'-pyrophosphohydrolase;
37-133 1.77e-06

bifunctional GTP diphosphokinase/guanosine-3',5'-bis pyrophosphate 3'-pyrophosphohydrolase;


Pssm-ID: 236843 [Multi-domain]  Cd Length: 702  Bit Score: 47.04  E-value: 1.77e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818652471  37 KPIIMHSLRVGSELMEFKQEKNIVIAGFLHDLLEDTDCKPKEIEKEFGKKVVRLVLACTSDENIK--DYK----ERWRKL 110
Cdd:PRK11092  43 EPYITHPVAVACILAEMRLDYETLMAALLHDVIEDTPATYQDMEQLFGKSVAELVEGVSKLDKLKfrDKKeaqaENFRKM 122

                         90       100
                 ....*....|....*....|....*
gi 818652471 111 VSNIKQaghD--AIIIKLIDQIANL 133
Cdd:PRK11092 123 IMAMVQ---DirVILIKLADRTHNM 144
 
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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