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Conserved domains on  [gi|341821440|emb|CCC72364|]
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ppx/GppA phosphatase family protein [Megasphaera elsdenii DSM 20460]

Protein Classification

acetate and sugar kinases/Hsc70/actin family protein( domain architecture ID 99298)

acetate and sugar kinases/Hsc70/actin (ASKHA) family protein catalyzes phosphoryl transfer from ATP to their respective substrates

CATH:  3.30.420.40
Gene Ontology:  GO:0000166
PubMed:  8800467|7781919
SCOP:  3000092

Graphical summary

 Zoom to residue level

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List of domain hits

Name Accession Description Interval E-value
ASKHA_NBD_AaPPX-GppA_MtPPX2-like cd24054
nucleotide-binding domain (NBD) of Aquifex aeolicus PPX/GppA, Mycobacterium tuberculosis PPX2, ...
6-292 2.44e-105

nucleotide-binding domain (NBD) of Aquifex aeolicus PPX/GppA, Mycobacterium tuberculosis PPX2, Fusobacterium nucleatum AroB, and similar proteins; The PPX/GppA family proteins play essential roles in bacterial survival and metabolism. Guanosine pentaphosphate (pppGpp) phosphohydrolase (GppA; EC 3.6.1.40) plays a key role in (p)ppGpp homeostasis. It specifically catalyzes the conversion of pppGpp to ppGpp (guanosine tetraphosphate). Sharing a similar domain structure, GppA is indistinguishable from exopolyphosphatase (PPX; EC 3.6.1.11), which mediates the metabolism of cellular inorganic polyphosphate. Especially, it is responsible for the maintenance of appropriate levels of cellular inorganic polyphosphate (PolyP). The family corresponds to a group of proteins similar to Aquifex aeolicus exopolyphosphatase/guanosine pentaphosphate phosphohydrolase (AaPPX/GppA), Mycobacterium tuberculosis exopolyphosphatase 2 (MtPPX2), Fusobacterium nucleatum bifunctional 3-dehydroquinate synthase/phosphatase (AroB) and similar proteins.


:

Pssm-ID: 466904 [Multi-domain]  Cd Length: 296  Bit Score: 309.02  E-value: 2.44e-105
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341821440   6 YAVIDIGSNSLRLMTGwQEVPGTWIFSPKELATTRLGKDIDETHHLSPAGMEASFAAMERWKG---QLTGIPVCAVATSA 82
Cdd:cd24054    1 IAAIDIGTNSVRLLIA-EVDGGGLRVLLDERRITRLGEGLDETGRLSPEAIERTLEALKEFKKiarEYGVEKIRAVATSA 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341821440  83 VREAVDGQAFLAEVRARFGWHCRAISGLEEASLSFTGATASLN-PDVTAAVIDIGGGSSEVAAGRGGDLCWSHSYPMGAV 161
Cdd:cd24054   80 LRDAKNRDEFLERVKEETGLEIEIISGEEEARLSFLGALSGLPlPDGPILVIDIGGGSTELILGKGGGILFSVSLPLGAV 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341821440 162 RFT----RGEVMSHQDVAHLERHCYQ--EWLPMKIRPDLLIGVGGTLTTLAAMDLQLAVYDAEKVEGHCISYEALCGHIE 235
Cdd:cd24054  160 RLTerflKSDPPSEEELEALREAIREllEELLLPPKPDRLVGVGGTATTLAAIDLGLEEYDPEKIHGYVLSLEELEELID 239
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 341821440 236 RLQAMTPEERRHVPGLQPKRSDIIIAGLLIAKSFLQRYQIPAITVSERDLMEGVFFR 292
Cdd:cd24054  240 RLASMSLEERRKLPGLEPGRADIILAGALILLEILEYLGADELTVSDRGLREGLLLE 296
 
Name Accession Description Interval E-value
ASKHA_NBD_AaPPX-GppA_MtPPX2-like cd24054
nucleotide-binding domain (NBD) of Aquifex aeolicus PPX/GppA, Mycobacterium tuberculosis PPX2, ...
6-292 2.44e-105

nucleotide-binding domain (NBD) of Aquifex aeolicus PPX/GppA, Mycobacterium tuberculosis PPX2, Fusobacterium nucleatum AroB, and similar proteins; The PPX/GppA family proteins play essential roles in bacterial survival and metabolism. Guanosine pentaphosphate (pppGpp) phosphohydrolase (GppA; EC 3.6.1.40) plays a key role in (p)ppGpp homeostasis. It specifically catalyzes the conversion of pppGpp to ppGpp (guanosine tetraphosphate). Sharing a similar domain structure, GppA is indistinguishable from exopolyphosphatase (PPX; EC 3.6.1.11), which mediates the metabolism of cellular inorganic polyphosphate. Especially, it is responsible for the maintenance of appropriate levels of cellular inorganic polyphosphate (PolyP). The family corresponds to a group of proteins similar to Aquifex aeolicus exopolyphosphatase/guanosine pentaphosphate phosphohydrolase (AaPPX/GppA), Mycobacterium tuberculosis exopolyphosphatase 2 (MtPPX2), Fusobacterium nucleatum bifunctional 3-dehydroquinate synthase/phosphatase (AroB) and similar proteins.


Pssm-ID: 466904 [Multi-domain]  Cd Length: 296  Bit Score: 309.02  E-value: 2.44e-105
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341821440   6 YAVIDIGSNSLRLMTGwQEVPGTWIFSPKELATTRLGKDIDETHHLSPAGMEASFAAMERWKG---QLTGIPVCAVATSA 82
Cdd:cd24054    1 IAAIDIGTNSVRLLIA-EVDGGGLRVLLDERRITRLGEGLDETGRLSPEAIERTLEALKEFKKiarEYGVEKIRAVATSA 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341821440  83 VREAVDGQAFLAEVRARFGWHCRAISGLEEASLSFTGATASLN-PDVTAAVIDIGGGSSEVAAGRGGDLCWSHSYPMGAV 161
Cdd:cd24054   80 LRDAKNRDEFLERVKEETGLEIEIISGEEEARLSFLGALSGLPlPDGPILVIDIGGGSTELILGKGGGILFSVSLPLGAV 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341821440 162 RFT----RGEVMSHQDVAHLERHCYQ--EWLPMKIRPDLLIGVGGTLTTLAAMDLQLAVYDAEKVEGHCISYEALCGHIE 235
Cdd:cd24054  160 RLTerflKSDPPSEEELEALREAIREllEELLLPPKPDRLVGVGGTATTLAAIDLGLEEYDPEKIHGYVLSLEELEELID 239
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 341821440 236 RLQAMTPEERRHVPGLQPKRSDIIIAGLLIAKSFLQRYQIPAITVSERDLMEGVFFR 292
Cdd:cd24054  240 RLASMSLEERRKLPGLEPGRADIILAGALILLEILEYLGADELTVSDRGLREGLLLE 296
GppA COG0248
Exopolyphosphatase/pppGpp-phosphohydrolase [Nucleotide transport and metabolism, Signal ...
4-303 2.69e-92

Exopolyphosphatase/pppGpp-phosphohydrolase [Nucleotide transport and metabolism, Signal transduction mechanisms];


Pssm-ID: 440018 [Multi-domain]  Cd Length: 314  Bit Score: 276.68  E-value: 2.69e-92
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341821440   4 QKYAVIDIGSNSLRLMTGWQEVPGTWIFSPKELATTRLGKDIDETHHLSPAGMEASFAAMERWKGQLTGIPV---CAVAT 80
Cdd:COG0248    3 MRLAAIDIGSNSVRLLIAEVDEGGSFRILDREKEPVRLGEGLDATGRLSEEAIERALAALKRFAELLREYGVervRAVAT 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341821440  81 SAVREAVDGQAFLAEVRARFGWHCRAISGLEEASLSFTGATASLNPDV-TAAVIDIGGGSSEVAAGRGGDLCWSHSYPMG 159
Cdd:COG0248   83 SALREAKNGDEFLDRVKEETGLPIEVISGEEEARLIYLGVLSGLPLSDgRGLVVDIGGGSTELILGDGGEILFSESLPLG 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341821440 160 AVRFTR----GEVMSHQDVAHLERHCYQE-----WLPMKIRPDLLIGVGGTLTTLAAMDLQLAVYDaEKVEGHCISYEAL 230
Cdd:COG0248  163 AVRLTErffpDDPPTAEEFAAAREYIREEleplaKELRKGGPDTLVGTGGTIRTLARLLLALGRYD-EKVHGYTLTREEL 241
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 341821440 231 CGHIERLQAMTPEERRHVPGLQPKRSDIIIAGLLIAKSFLQRYQIPAITVSERDLMEGVFFRHSFHDAAWNSR 303
Cdd:COG0248  242 EELIERLLSLTLEERAKLPGLSPDRADVILAGAAILEALMEALGIEEIVVSDRGLREGLLYDLLGRDGKKDDR 314
exo_poly_only TIGR03706
exopolyphosphatase; It appears that a single enzyme may act as both exopolyphosphatase (Ppx) ...
6-293 3.43e-67

exopolyphosphatase; It appears that a single enzyme may act as both exopolyphosphatase (Ppx) and guanosine pentaphosphate phosphohydrolase (GppA) in a number of species. Members of the seed alignment use to define this exception-level model are encoded adjacent to a polyphosphate kinase 1 gene, and the trusted cutoff is set high enough (425) that no genome has a second hit. Therefore all members may be presumed to at least share exopolyphospatase activity, and may lack GppA activity. GppA acts in the stringent response. [Central intermediary metabolism, Phosphorus compounds]


Pssm-ID: 274735 [Multi-domain]  Cd Length: 300  Bit Score: 212.02  E-value: 3.43e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341821440    6 YAVIDIGSNSLRLMTGwQEVPGtwifSPKEL----ATTRLGKDIDETHHLSPAGMEASFAAMERWKGQLTGIP---VCAV 78
Cdd:TIGR03706   2 IAAIDIGSNSVRLVIA-RGVEG----SLQVLfnekEMVRLGEGLDSTGRLSEEAIERALEALKRFAELLRGFPvdeVRAV 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341821440   79 ATSAVREAVDGQAFLAEVRARFGWHCRAISGLEEASLSFTGATASLnPDVTAAVIDIGGGSSEVAAGRGGDLCWSHSYPM 158
Cdd:TIGR03706  77 ATAALRDAKNGPEFLKEAEAILGLPIEVISGEEEARLIYLGVAHTL-PIADGLVVDIGGGSTELILGKDGEPGEGVSLPL 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341821440  159 GAVRFTR----GEVMSHQDVAHLERHCYQE-----WLPmKIRPDLLIGVGGTLTTLAAMDLQLAVYDAEKVEGHCISYEA 229
Cdd:TIGR03706 156 GCVRLTEqffpDGPISKKSLKQARKAAREElaslkWLK-KGGWRPLYGVGGTWRALARLHMAQRGYPLHGLHGYEITAEG 234
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 341821440  230 LCGHIERLQAMTPEERRHVPGLQPKRSDIIIAGLLIAKSFLQRYQIPAITVSERDLMEGVFFRH 293
Cdd:TIGR03706 235 LLELLEELIKLSREERLKLPGLSKDRADILPGGAAILEELFRALGIEQIIFSSGGLREGVLYEL 298
Ppx-GppA pfam02541
Ppx/GppA phosphatase family; This family consists of the N-terminal region of ...
34-292 1.06e-43

Ppx/GppA phosphatase family; This family consists of the N-terminal region of exopolyphosphatase (Ppx) EC:3.6.1.11 and guanosine pentaphosphate phospho-hydrolase (GppA) EC:3.6.1.40.


Pssm-ID: 396889 [Multi-domain]  Cd Length: 285  Bit Score: 150.94  E-value: 1.06e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341821440   34 KELATTRLGKDIDETHHLSPAGMEASFAAMERWKGQLTGIPV---CAVATSAVREAVDGQAFLAEVRARFGWHCRAISGL 110
Cdd:pfam02541  15 REKRKVRLAEGLNSTGRLNEEAIERTISALKEFAEILQGFGVeniRAVATSALRDAVNADEFLARVKKETGLPVEIISGE 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341821440  111 EEASLSFTGATASLNPDVTAAVIDIGGGSSEVAAGRGGDLCWSHSYPMGAVRFTrgEVMSHQDVAHLER-HCYQEWLPMK 189
Cdd:pfam02541  95 EEARLIYLGVVSTLGSKGRGLVIDIGGGSTELVLGENKKVRKLISLPMGCVRLT--ERFFHDDPLTKEEvARARDAVRKE 172
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341821440  190 IRP---DLLIGvGGTLTTLAAMDLQLAVYD---AEKVEGHCISYEALCGHIERLQAMTPEERRHVPGLQPKRSDIIIAGL 263
Cdd:pfam02541 173 LEEpkdEVRIG-GGWIRALGTSGTISALAPlmaLHGIMGYEITAEELEELIEKLSQITREDRLELAGVSDERADVIVAGA 251
                         250       260
                  ....*....|....*....|....*....
gi 341821440  264 LIAKSFLQRYQIPAITVSERDLMEGVFFR 292
Cdd:pfam02541 252 LILSAVFEALSIEAMIISDGGLREGVLYS 280
PRK11031 PRK11031
guanosine-5'-triphosphate,3'-diphosphate diphosphatase;
6-161 8.42e-15

guanosine-5'-triphosphate,3'-diphosphate diphosphatase;


Pssm-ID: 236826 [Multi-domain]  Cd Length: 496  Bit Score: 74.61  E-value: 8.42e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341821440   6 YAVIDIGSNSLRlMTGWQEVPGtwifSPKELA----TTRLGKDIDETHHLSPAGMEASFAAMERWKGQLTGIP---VCAV 78
Cdd:PRK11031   8 YAAIDLGSNSFH-MLVVREVAG----SIQTLArikrKVRLAAGLDSDNALSNEAMERGWQCLRLFAERLQDIPpsqIRVV 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341821440  79 ATSAVREAVDGQAFLAEVRARFGWHCRAISGLEEASLSFTG-ATASLNPDvTAAVIDIGGGSSEVAAGRGGDLCWSHSYP 157
Cdd:PRK11031  83 ATATLRLAVNADEFLAKAQEILGCPVQVISGEEEARLIYQGvAHTTGGAD-QRLVVDIGGASTELVTGTGAQATSLFSLS 161

                 ....
gi 341821440 158 MGAV 161
Cdd:PRK11031 162 MGCV 165
 
Name Accession Description Interval E-value
ASKHA_NBD_AaPPX-GppA_MtPPX2-like cd24054
nucleotide-binding domain (NBD) of Aquifex aeolicus PPX/GppA, Mycobacterium tuberculosis PPX2, ...
6-292 2.44e-105

nucleotide-binding domain (NBD) of Aquifex aeolicus PPX/GppA, Mycobacterium tuberculosis PPX2, Fusobacterium nucleatum AroB, and similar proteins; The PPX/GppA family proteins play essential roles in bacterial survival and metabolism. Guanosine pentaphosphate (pppGpp) phosphohydrolase (GppA; EC 3.6.1.40) plays a key role in (p)ppGpp homeostasis. It specifically catalyzes the conversion of pppGpp to ppGpp (guanosine tetraphosphate). Sharing a similar domain structure, GppA is indistinguishable from exopolyphosphatase (PPX; EC 3.6.1.11), which mediates the metabolism of cellular inorganic polyphosphate. Especially, it is responsible for the maintenance of appropriate levels of cellular inorganic polyphosphate (PolyP). The family corresponds to a group of proteins similar to Aquifex aeolicus exopolyphosphatase/guanosine pentaphosphate phosphohydrolase (AaPPX/GppA), Mycobacterium tuberculosis exopolyphosphatase 2 (MtPPX2), Fusobacterium nucleatum bifunctional 3-dehydroquinate synthase/phosphatase (AroB) and similar proteins.


Pssm-ID: 466904 [Multi-domain]  Cd Length: 296  Bit Score: 309.02  E-value: 2.44e-105
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341821440   6 YAVIDIGSNSLRLMTGwQEVPGTWIFSPKELATTRLGKDIDETHHLSPAGMEASFAAMERWKG---QLTGIPVCAVATSA 82
Cdd:cd24054    1 IAAIDIGTNSVRLLIA-EVDGGGLRVLLDERRITRLGEGLDETGRLSPEAIERTLEALKEFKKiarEYGVEKIRAVATSA 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341821440  83 VREAVDGQAFLAEVRARFGWHCRAISGLEEASLSFTGATASLN-PDVTAAVIDIGGGSSEVAAGRGGDLCWSHSYPMGAV 161
Cdd:cd24054   80 LRDAKNRDEFLERVKEETGLEIEIISGEEEARLSFLGALSGLPlPDGPILVIDIGGGSTELILGKGGGILFSVSLPLGAV 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341821440 162 RFT----RGEVMSHQDVAHLERHCYQ--EWLPMKIRPDLLIGVGGTLTTLAAMDLQLAVYDAEKVEGHCISYEALCGHIE 235
Cdd:cd24054  160 RLTerflKSDPPSEEELEALREAIREllEELLLPPKPDRLVGVGGTATTLAAIDLGLEEYDPEKIHGYVLSLEELEELID 239
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 341821440 236 RLQAMTPEERRHVPGLQPKRSDIIIAGLLIAKSFLQRYQIPAITVSERDLMEGVFFR 292
Cdd:cd24054  240 RLASMSLEERRKLPGLEPGRADIILAGALILLEILEYLGADELTVSDRGLREGLLLE 296
GppA COG0248
Exopolyphosphatase/pppGpp-phosphohydrolase [Nucleotide transport and metabolism, Signal ...
4-303 2.69e-92

Exopolyphosphatase/pppGpp-phosphohydrolase [Nucleotide transport and metabolism, Signal transduction mechanisms];


Pssm-ID: 440018 [Multi-domain]  Cd Length: 314  Bit Score: 276.68  E-value: 2.69e-92
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341821440   4 QKYAVIDIGSNSLRLMTGWQEVPGTWIFSPKELATTRLGKDIDETHHLSPAGMEASFAAMERWKGQLTGIPV---CAVAT 80
Cdd:COG0248    3 MRLAAIDIGSNSVRLLIAEVDEGGSFRILDREKEPVRLGEGLDATGRLSEEAIERALAALKRFAELLREYGVervRAVAT 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341821440  81 SAVREAVDGQAFLAEVRARFGWHCRAISGLEEASLSFTGATASLNPDV-TAAVIDIGGGSSEVAAGRGGDLCWSHSYPMG 159
Cdd:COG0248   83 SALREAKNGDEFLDRVKEETGLPIEVISGEEEARLIYLGVLSGLPLSDgRGLVVDIGGGSTELILGDGGEILFSESLPLG 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341821440 160 AVRFTR----GEVMSHQDVAHLERHCYQE-----WLPMKIRPDLLIGVGGTLTTLAAMDLQLAVYDaEKVEGHCISYEAL 230
Cdd:COG0248  163 AVRLTErffpDDPPTAEEFAAAREYIREEleplaKELRKGGPDTLVGTGGTIRTLARLLLALGRYD-EKVHGYTLTREEL 241
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 341821440 231 CGHIERLQAMTPEERRHVPGLQPKRSDIIIAGLLIAKSFLQRYQIPAITVSERDLMEGVFFRHSFHDAAWNSR 303
Cdd:COG0248  242 EELIERLLSLTLEERAKLPGLSPDRADVILAGAAILEALMEALGIEEIVVSDRGLREGLLYDLLGRDGKKDDR 314
ASKHA_NBD_PPX_GppA cd24006
nucleotide-binding domain (NBD) of the exopolyphosphatase/guanosine pentaphosphate ...
7-289 3.43e-74

nucleotide-binding domain (NBD) of the exopolyphosphatase/guanosine pentaphosphate phosphohydrolase (PPX/GppA) domain family; Members of the PPX/GppA family are involved in bacterial survival and metabolism. They may play distinct biochemical roles involved in polyphosphate and (p)ppGpp metabolic pathways. Guanosine pentaphosphate (pppGpp) phosphohydrolase (GppA; EC 3.6.1.40) plays a key role in (p)ppGpp homeostasis. It specifically catalyzes the conversion of pppGpp to ppGpp (guanosine tetraphosphate). Sharing a similar domain structure, GppA is indistinguishable from exopolyphosphatase (PPX; EC 3.6.1.11), which mediates the metabolism of cellular inorganic polyphosphate. Especially, it is responsible for the maintenance of appropriate levels of cellular inorganic polyphosphate (PolyP). Some bacteria, such as Escherichia coli, possesses two homologs, EcGppA and EcPPX. Some others, such as Helicobacter pylori and Aquifex aeolicus, encode only one PPX/GppA homolog, which may play important roles in the homeostasis of both (p)ppGpp and PolyP. The PPX/GppA family belongs to the ASKHA (Acetate and Sugar Kinases/Hsc70/Actin) superfamily of phosphotransferases, all members of which share a common characteristic five-stranded beta sheet occurring in both the N- and C-terminal domains.


Pssm-ID: 466856 [Multi-domain]  Cd Length: 294  Bit Score: 229.73  E-value: 3.43e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341821440   7 AVIDIGSNSLRLMTGwqEVPGTWIFSP--KELATTRLGKDIDETHHLSPAGMEASFAAMERWKGQLTGIPV---CAVATS 81
Cdd:cd24006    1 AAIDIGSNSIRLLIA--EVDPDGSFRIleRLREPVRLGEDVFTTGRISEEAIERAVEALRRFKKLADEYGVkriRAVATS 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341821440  82 AVREAVDGQAFLAEVRARFGWHCRAISGLEEASLSFTGATASLNP-DVTAAVIDIGGGSSEVAAGRGGDLCWSHSYPMGA 160
Cdd:cd24006   79 AVREASNGDEFLERIKRETGIDVEIISGEEEARLIYLAVRSGLPLgDGNALIVDIGGGSTELTLGDNGEILFSESLPLGA 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341821440 161 VR----FTRGEVMSHQDVAHLERHCYQEWLPM----KIRPDLLIGVGGTLTTLAAMDLQlavyDAEKVEGHCISYEALCG 232
Cdd:cd24006  159 VRlterFLKDDPPSELLEEYLRSFVRSVLRPLpkrrKIKFDVAIGSGGTILALAAMALA----RKGKPHGYEISREELKA 234
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 341821440 233 HIERLQAMTPEERRHVPGLQPKRSDIIIAGLLIAKSFLQRYQIPAITVSERDLMEGV 289
Cdd:cd24006  235 LYDELLRLSLEERRKKYGLSPDRADVIVPAALILLELLELLGAEEIIVPDVGLRDGL 291
ASKHA_NBD_MtPPX2-like cd24119
nucleotide-binding domain (NBD) of Mycobacterium tuberculosis exopolyphosphatase 2 (MtPPX2) ...
7-289 1.71e-71

nucleotide-binding domain (NBD) of Mycobacterium tuberculosis exopolyphosphatase 2 (MtPPX2) and similar proteins; The PPX/GppA family proteins play essential roles in bacterial survival and metabolism. Guanosine pentaphosphate (pppGpp) phosphohydrolase (GppA; EC 3.6.1.40) plays a key role in (p)ppGpp homeostasis. It specifically catalyzes the conversion of pppGpp to ppGpp (guanosine tetraphosphate). Sharing a similar domain structure, GppA is indistinguishable from exopolyphosphatase (PPX; EC 3.6.1.11), which mediates the metabolism of cellular inorganic polyphosphate. Especially, it is responsible for the maintenance of appropriate levels of cellular inorganic polyphosphate (PolyP). Mycobacterium tuberculosis encodes two PPX/GppA homologues, Rv0496 (MtPPX1) and Rv1026 (MtPPX2), which are analogous to the Escherichia coli PPX and GppA enzymes. MtPPX1 functions as an exopolyphosphatase, showing a distinct preference for relatively short-chain poly-P substrates. The exopolyphosphatase activities of MtPPX1 are inhibited by pppGpp. In contrast, MtPPX2 has no detectable exopolyphosphatase activities. Neither MtPPX1 nor MtPPX2 can hydrolyze pppGpp to ppGpp, which is a reaction catalyzed by E. coli PPX and GppA enzymes. Both the MtPPX1 and MtPPX2 proteins have modest ATPase and to a lesser extent ADPase activities. The family corresponds a group of proteins similar to MtPPX2.


Pssm-ID: 466969 [Multi-domain]  Cd Length: 298  Bit Score: 222.91  E-value: 1.71e-71
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341821440   7 AVIDIGSNSLRLMTGwqEVPGTWIF-SPKELATTRLGKDIDETHHLSPAGMEASFAAMERWKGQLTGIP---VCAVATSA 82
Cdd:cd24119    2 AAIDIGTNSVRLLVA--DVDEGGLReVVRRTRITRLGEGVDATGRLSPEAIERTLAALAEYAALIRELGverVRVVATSA 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341821440  83 VREAVDGQAFLAEVRARFGWHCRAISGLEEASLSFTGATASLNPDVTAAVIDIGGGSSEVAAGRGGDLCWSHSYPMGAVR 162
Cdd:cd24119   80 SRDASNRDDFLDRLESVLGVRPEVISGEEEARLSFLGATSGLPAPGPVLVVDIGGGSTELVLGRAGEVEAAISLDIGSVR 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341821440 163 FT---------RGEVMS--HQDV-AHLERhcyQEWLPMKIRPDLLIGVGGTLTTLAAMDLQLAVYDAEKVEGHCISYEAL 230
Cdd:cd24119  160 LTerflhsdppTAEELEaaRADVdAQLDE---ALDVVSLERATRLVGVAGTVTTLAALALGLPEYDPERVHGYRLSLDQV 236
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 341821440 231 CGHIERLQAMTPEERRHVPGLQPKRSDIIIAGLLIAKSFLQRYQIPAITVSERDLMEGV 289
Cdd:cd24119  237 EAVLRRLSAMTLEERAALPGLQPGRADVIVAGAVILSEVLRRLGIDEVVVSEHDILDGI 295
ASKHA_NBD_AroB-like cd24120
nucleotide-binding domain (NBD) of Fusobacterium nucleatum bifunctional 3-dehydroquinate ...
7-290 6.33e-69

nucleotide-binding domain (NBD) of Fusobacterium nucleatum bifunctional 3-dehydroquinate synthase/phosphatase (AroB) and similar proteins; The family includes a group of PPX/GppA family proteins similar to Fusobacterium nucleatum bifunctional 3-dehydroquinate synthase/phosphatase (AroB; EC 4.2.3.4/EC 3.6.1.-). AroB contains 3-dehydroquinate synthase and an unknown phosphatase. 3-dehydroquinate synthase catalyzes the second step in the shikimate pathway, which is essential to produce aromatic amino acids in bacteria, plants, and fungi, but not mammals.


Pssm-ID: 466970 [Multi-domain]  Cd Length: 297  Bit Score: 216.41  E-value: 6.33e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341821440   7 AVIDIGSNSLRLM-TGWQEVPGTWIFspKELATTRLGKDIDETHHLSPAGMEASFAAMERWKGQLTGIPV---CAVATSA 82
Cdd:cd24120    2 AAIDIGTNSCRLLiAEVEEGNVNPLF--KKLETTRLGENVNKTGVLGKEAIERTVEVLKEYKRIADKYGVkkiIAFATSA 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341821440  83 VREAVDGQAFLAEVRARFGWHCRAISGLEEASLSFTGATASL-NPDVTAAVIDIGGGSSEVAAGRGGDLCWSHSYPMGAV 161
Cdd:cd24120   80 VRDAKNKDEFIELVKRETGIKINVISGEEEAKLSFLGATSGLdSLYEKILVIDIGGGSTEFTLGAPRGIKYVKSFNLGAV 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341821440 162 RFT-RGEVMSHQDVAHLERHC------YQEWLPMKIRPDLLIGVGGTLTTLAAMDLQLAVYDAEKVEGHCISYEALCGHI 234
Cdd:cd24120  160 RLTeSFFGNDPPDYEELENMRnyvkdkLNETEKFKSLDFKLIGVAGTITTLAAIYLGLEVYDPEKVHGSKLTKEDIEENL 239
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 341821440 235 ERLQAMTPEERRHVPGLQPKRSDIIIAGLLIAKSFLQRYQIPAITVSERDLMEGVF 290
Cdd:cd24120  240 KKLISLDLEERKKIPGLEPERADVIIAGTLILLEIMEILGKDFIIVSEADILEGII 295
exo_poly_only TIGR03706
exopolyphosphatase; It appears that a single enzyme may act as both exopolyphosphatase (Ppx) ...
6-293 3.43e-67

exopolyphosphatase; It appears that a single enzyme may act as both exopolyphosphatase (Ppx) and guanosine pentaphosphate phosphohydrolase (GppA) in a number of species. Members of the seed alignment use to define this exception-level model are encoded adjacent to a polyphosphate kinase 1 gene, and the trusted cutoff is set high enough (425) that no genome has a second hit. Therefore all members may be presumed to at least share exopolyphospatase activity, and may lack GppA activity. GppA acts in the stringent response. [Central intermediary metabolism, Phosphorus compounds]


Pssm-ID: 274735 [Multi-domain]  Cd Length: 300  Bit Score: 212.02  E-value: 3.43e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341821440    6 YAVIDIGSNSLRLMTGwQEVPGtwifSPKEL----ATTRLGKDIDETHHLSPAGMEASFAAMERWKGQLTGIP---VCAV 78
Cdd:TIGR03706   2 IAAIDIGSNSVRLVIA-RGVEG----SLQVLfnekEMVRLGEGLDSTGRLSEEAIERALEALKRFAELLRGFPvdeVRAV 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341821440   79 ATSAVREAVDGQAFLAEVRARFGWHCRAISGLEEASLSFTGATASLnPDVTAAVIDIGGGSSEVAAGRGGDLCWSHSYPM 158
Cdd:TIGR03706  77 ATAALRDAKNGPEFLKEAEAILGLPIEVISGEEEARLIYLGVAHTL-PIADGLVVDIGGGSTELILGKDGEPGEGVSLPL 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341821440  159 GAVRFTR----GEVMSHQDVAHLERHCYQE-----WLPmKIRPDLLIGVGGTLTTLAAMDLQLAVYDAEKVEGHCISYEA 229
Cdd:TIGR03706 156 GCVRLTEqffpDGPISKKSLKQARKAAREElaslkWLK-KGGWRPLYGVGGTWRALARLHMAQRGYPLHGLHGYEITAEG 234
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 341821440  230 LCGHIERLQAMTPEERRHVPGLQPKRSDIIIAGLLIAKSFLQRYQIPAITVSERDLMEGVFFRH 293
Cdd:TIGR03706 235 LLELLEELIKLSREERLKLPGLSKDRADILPGGAAILEELFRALGIEQIIFSSGGLREGVLYEL 298
ASKHA_NBD_HpPPX-GppA-like cd24052
nucleotide-binding domain (NBD) of Helicobacter pylori exopolyphosphatase/guanosine ...
6-293 1.69e-66

nucleotide-binding domain (NBD) of Helicobacter pylori exopolyphosphatase/guanosine pentaphosphate phosphohydrolase (HpPPX/GppA) and similar proteins; The PPX/GppA family proteins play essential roles in bacterial survival and metabolism. Guanosine pentaphosphate (pppGpp) phosphohydrolase (GppA; EC 3.6.1.40) plays a key role in (p)ppGpp homeostasis. It specifically catalyzes the conversion of pppGpp to ppGpp (guanosine tetraphosphate). Sharing a similar domain structure, GppA is indistinguishable from exopolyphosphatase (PPX; EC 3.6.1.11), which mediates the metabolism of cellular inorganic polyphosphate. Especially, it is responsible for the maintenance of appropriate levels of cellular inorganic polyphosphate (PolyP). The family corresponds a group of proteins similar to Helicobacter pylori PPX/GppA (HpPPX/GppA). HpPPX/GppA is phylogenetically distant from the Escherichia coli homologs. Unlike E. coli that possesses two homologs, EcGppA and EcPPX, H. pylori encodes only one PPX/GppA homolog, HpPPX/GppA. As such, HpPPX/GppA may play important roles in the homeostasis of both (p)ppGpp and PolyP.


Pssm-ID: 466902 [Multi-domain]  Cd Length: 298  Bit Score: 210.03  E-value: 1.69e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341821440   6 YAVIDIGSNSLRLMTgwQEVPGTW---IFSPKElaTTRLGKDIDETHHLSPAGMEASFAAMERWKG--QLTGI-PVCAVA 79
Cdd:cd24052    1 IAIIDIGSNSIRLVI--YEIEGGSfrlLFNEKE--TVGLGEYLDEDGKLSEEGIERAIKALKRFKKicEALGVdEIIAFA 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341821440  80 TSAVREAVDGQAFLAEVRARFGWHCRAISGLEEASLSFTGATASLNPDvTAAVIDIGGGSSEVAAGRGGDLCWSHSYPMG 159
Cdd:cd24052   77 TAALRNAKNGEEFLERIKKETGIDIRVLSGEEEAYYGFLGVLNSLPLA-DGLVVDIGGGSTELVLFKNGKIKESISLPLG 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341821440 160 AVRFT----RGEVMSHQDVAHLERHCYQE-----WLPMKiRPDLLIGVGGTLTTLAAMDLQLAVYDAEKVEGHCISYEAL 230
Cdd:cd24052  156 SLRLYerfvSGILPTEKELKKIRKFIKKElkklpWLKEK-KGLPLYGVGGTIRALAKLHMELKNYPLDILHGYTISAEEL 234
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 341821440 231 CGHIERLQAMTPEERRHVPGLQPKRSDIIIAGLLIAKSFLQRYQIPAITVSERDLMEGVFFRH 293
Cdd:cd24052  235 DELLKKLKKLDKEERKKILGLSPDRADTIPPGALILKELLKYFGAKEIIVSGYGLREGYLYEK 297
ASKHA_NBD_MtPPX1-like cd24056
nucleotide-binding domain (NBD) of Mycobacterium tuberculosis exopolyphosphatase 1 (MtPPX1) ...
7-289 5.91e-54

nucleotide-binding domain (NBD) of Mycobacterium tuberculosis exopolyphosphatase 1 (MtPPX1) and similar proteins; The PPX/GppA family proteins play essential roles in bacterial survival and metabolism. Guanosine pentaphosphate (pppGpp) phosphohydrolase (GppA; EC 3.6.1.40) plays a key role in (p)ppGpp homeostasis. It specifically catalyzes the conversion of pppGpp to ppGpp (guanosine tetraphosphate). Sharing a similar domain structure, GppA is indistinguishable from exopolyphosphatase (PPX; EC 3.6.1.11), which mediates the metabolism of cellular inorganic polyphosphate. Especially, it is responsible for the maintenance of appropriate levels of cellular inorganic polyphosphate (PolyP). Mycobacterium tuberculosis encodes two PPX/GppA homologues, Rv0496 (MtPPX1) and Rv1026 (MtPPX2), which are analogous to the Escherichia coli PPX and GppA enzymes. MtPPX1 functions as an exopolyphosphatase, showing a distinct preference for relatively short-chain poly-P substrates. The exopolyphosphatase activities of MtPPX1 are inhibited by pppGpp. In contrast, MtPPX2 has no detectable exopolyphosphatase activities. Neither MtPPX1 nor MtPPX2 can hydrolyze pppGpp to ppGpp, which is a reaction catalyzed by E. coli PPX and GppA enzymes. Both the MtPPX1 and MtPPX2 proteins have modest ATPase and to a lesser extent ADPase activities. The family corresponds a group of proteins similar to MtPPX1.


Pssm-ID: 466906 [Multi-domain]  Cd Length: 302  Bit Score: 177.80  E-value: 5.91e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341821440   7 AVIDIGSNSLRLMTGwqEVPGTWIFSP--KELATTRLGKDIDETHHLSPAGMEASFAAMERWKGQLTGI---PVCAVATS 81
Cdd:cd24056    3 AALDVGSNTFHLLVA--DVEGDGRLEPvaDEKVMLRLGEDVARTGEIGPEAIDRAAEAVRRFVELARRLgaeELLAVATS 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341821440  82 AVREAVDGQAFLAEVRARFGWHCRAISGLEEASLSFTGATASLN-PDVTAAVIDIGGGSSEVAAGRGGDLCWSHSYPMGA 160
Cdd:cd24056   81 ALREAENGPEVLDRVEAETGVPVRVLSGEEEARLTFLGARAALGwSSGPLLVLDLGGGSLELAVGVDGRPEWAASLPLGS 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341821440 161 ----VRFTRGEVMSHQDVAHLERHC---YQEWLP--MKIRPDLLIGVGGTLTTLAAMDLQLAvYDAEKVEGHCISYEALC 231
Cdd:cd24056  161 grltARFLSSDPPSPEEVRALRAAVraeLAPALDrvRAGEPRRAVATGGTARALARLAGAAR-SPVGPLNQRSLTREDLR 239
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 341821440 232 GHIERLQAMTPEERRHVPGLQPKRSDIIIAGLLIAKSFLQRYQIPAITVSERDLMEGV 289
Cdd:cd24056  240 ELRRRLASLSAAERAELPGIDPRRADLLPAGALVLEALLDALGLEELVVSEWGLREGV 297
ASKHA_NBD_AaPPX-GppA-like cd24118
nucleotide-binding domain (NBD) of Aquifex aeolicus exopolyphosphatase/guanosine ...
7-292 4.57e-53

nucleotide-binding domain (NBD) of Aquifex aeolicus exopolyphosphatase/guanosine pentaphosphate phosphohydrolase (AaPPX/GppA) and similar proteins; The PPX/GppA family proteins play essential roles in bacterial survival and metabolism. Guanosine pentaphosphate (pppGpp) phosphohydrolase (GppA; EC 3.6.1.40) plays a key role in (p)ppGpp homeostasis. It specifically catalyzes the conversion of pppGpp to ppGpp (guanosine tetraphosphate). Sharing a similar domain structure, GppA is indistinguishable from exopolyphosphatase (PPX; EC 3.6.1.11), which mediates the metabolism of cellular inorganic polyphosphate. Especially, it is responsible for the maintenance of appropriate levels of cellular inorganic polyphosphate (PolyP). The family corresponds to a group of proteins similar to Aquifex aeolicus PPX/GppA (AaPPX/GppA). AaPPX/GppA is phylogenetically distant from the Escherichia coli homologs. Unlike E. coli that possesses two homologs, EcGppA and EcPPX, A. aeolicus encodes only one PPX/GppA homolog, AaPPX/GppA. As such, AaPPX/GppA may play important roles in the homeostasis of both (p)ppGpp and PolyP.


Pssm-ID: 466968 [Multi-domain]  Cd Length: 293  Bit Score: 175.34  E-value: 4.57e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341821440   7 AVIDIGSNSLRLMTGWQEvPGTWIFSPKELATTRLGKDIDETHHLSPAGMEASFAAMERWKGQLTGIPV---CAVATSAV 83
Cdd:cd24118    2 ASIDIGSYSTRLTIADIE-DGKLKILLEEGRITALGTGLKETGRLSEDRIEETLKVLKEYKKLIDEFGVeriKAVGTEAI 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341821440  84 REAVDGQAFLAEVRARFGWHCRAISGLEEASLSFTGATASLNPDVTAAVIDIGGGSSEVAAGRGGDLCWSHSYPMGAV-- 161
Cdd:cd24118   81 RRAKNREEFLERVKEEVGLDLEVISPEEEGEYAFLAVAYSLKPKGEVCVVDQGGGSTEFVYGKGEKIEFLKSLPFGIVnl 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341821440 162 --RFTRGEVMSHQDVAHLERHCYQEWLPMKIRPDLLIGVGGTLTTLAAMDLQLAVYDAEKVEGHCISYEALCGHIERLQA 239
Cdd:cd24118  161 teEFFKSDPPTEEELESLFNFLEKEISKIKKPVDTVVGLGGTITTLAALEYNIYPYDPQKVHGKKLTYGRIKKWFDTLSS 240
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|...
gi 341821440 240 MTPEERRHVPGLQPKRSDIIIAGLLIAKSFLQRYQIPAITVSERDLMEGVFFR 292
Cdd:cd24118  241 MPSEERKKIFQIEDRRAEVIIAGIAIFLKTMELFEKRSITVSDWGLLEGLLVE 293
ASKHA_NBD_ChPPX-like cd24055
nucleotide-binding domain (NBD) of Cytophaga hutchinsonii exopolyphosphatase (ChPPX) and ...
7-292 1.21e-48

nucleotide-binding domain (NBD) of Cytophaga hutchinsonii exopolyphosphatase (ChPPX) and similar proteins; The PPX/GppA family proteins play essential roles in bacterial survival and metabolism. Guanosine pentaphosphate (pppGpp) phosphohydrolase (GppA; EC 3.6.1.40) plays a key role in (p)ppGpp homeostasis. It specifically catalyzes the conversion of pppGpp to ppGpp (guanosine tetraphosphate). Sharing a similar domain structure, GppA is indistinguishable from exopolyphosphatase (PPX; EC 3.6.1.11), which mediates the metabolism of cellular inorganic polyphosphate. Especially, it is responsible for the maintenance of appropriate levels of cellular inorganic polyphosphate (PolyP). The family corresponds a group of proteins similar to uncharacterized Cytophaga hutchinsonii exopolyphosphatase (ChPPX).


Pssm-ID: 466905 [Multi-domain]  Cd Length: 300  Bit Score: 164.27  E-value: 1.21e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341821440   7 AVIDIGSNSLRLMTGwQEVPGTWIFSPKELATTRLGKDIDETHHLSPAGMEASFAAMERWKGQLTGIPV---CAVATSAV 83
Cdd:cd24055    2 AVIDLGTNTFNLLIA-EVDDGSFEILYREKVPVKLGKGGINIGIITDDAFERALDALKSFKQIAKQYGVdeiVAVGTSAL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341821440  84 REAVDGQAFLAEVRARFGWHCRAISGLEEASLSFTGATASLNP-DVTAAVIDIGGGSSEVAAGRGGDLCWSHSYPMGAVR 162
Cdd:cd24055   81 RSAENGQEFIEKIKEELGIDIEIISGEREAELIYKGVRQAVPLtDEPALIMDIGGGSVEFILANNEQILWKKSFPIGVAR 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341821440 163 ----FTRGEVMSHQDVAHLERHCYQEWLPMK-----IRPDLLIGVGGTLTTLAAM-DLQLAVYDAEKVEGHCISYEALCG 232
Cdd:cd24055  161 llekFHPNDPISPEDIERLEAFLDEELADLFealdqYKPTVLIGSSGSFDTLAEMiEANKGRTPPAGQSSYEISLEEFEA 240
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 341821440 233 HIERLQAMTPEERRHVPGLQPKRSDII-IAGLLIaKSFLQRYQIPAITVSERDLMEGVFFR 292
Cdd:cd24055  241 LYQRLLTSTLEERLAIPGMIPMRADMIvVAAILI-QHVLEKFGIPEIVVSPYALKEGLLFE 300
Ppx-GppA pfam02541
Ppx/GppA phosphatase family; This family consists of the N-terminal region of ...
34-292 1.06e-43

Ppx/GppA phosphatase family; This family consists of the N-terminal region of exopolyphosphatase (Ppx) EC:3.6.1.11 and guanosine pentaphosphate phospho-hydrolase (GppA) EC:3.6.1.40.


Pssm-ID: 396889 [Multi-domain]  Cd Length: 285  Bit Score: 150.94  E-value: 1.06e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341821440   34 KELATTRLGKDIDETHHLSPAGMEASFAAMERWKGQLTGIPV---CAVATSAVREAVDGQAFLAEVRARFGWHCRAISGL 110
Cdd:pfam02541  15 REKRKVRLAEGLNSTGRLNEEAIERTISALKEFAEILQGFGVeniRAVATSALRDAVNADEFLARVKKETGLPVEIISGE 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341821440  111 EEASLSFTGATASLNPDVTAAVIDIGGGSSEVAAGRGGDLCWSHSYPMGAVRFTrgEVMSHQDVAHLER-HCYQEWLPMK 189
Cdd:pfam02541  95 EEARLIYLGVVSTLGSKGRGLVIDIGGGSTELVLGENKKVRKLISLPMGCVRLT--ERFFHDDPLTKEEvARARDAVRKE 172
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341821440  190 IRP---DLLIGvGGTLTTLAAMDLQLAVYD---AEKVEGHCISYEALCGHIERLQAMTPEERRHVPGLQPKRSDIIIAGL 263
Cdd:pfam02541 173 LEEpkdEVRIG-GGWIRALGTSGTISALAPlmaLHGIMGYEITAEELEELIEKLSQITREDRLELAGVSDERADVIVAGA 251
                         250       260
                  ....*....|....*....|....*....
gi 341821440  264 LIAKSFLQRYQIPAITVSERDLMEGVFFR 292
Cdd:pfam02541 252 LILSAVFEALSIEAMIISDGGLREGVLYS 280
ASKHA_NBD_EcPPX-GppA-like cd24053
nucleotide-binding domain (NBD) of Escherichia coli exopolyphosphatase (EcPPX), guanosine ...
7-291 6.95e-43

nucleotide-binding domain (NBD) of Escherichia coli exopolyphosphatase (EcPPX), guanosine pentaphosphate phosphohydrolase (EcGppA) and similar proteins; The PPX/GppA family proteins play essential roles in bacterial survival and metabolism. Guanosine pentaphosphate (pppGpp) phosphohydrolase (GppA; EC 3.6.1.40) plays a key role in (p)ppGpp homeostasis. It specifically catalyzes the conversion of pppGpp to ppGpp (guanosine tetraphosphate). Sharing a similar domain structure, GppA is indistinguishable from exopolyphosphatase (PPX; EC 3.6.1.11), which mediates the metabolism of cellular inorganic polyphosphate. Especially, it is responsible for the maintenance of appropriate levels of cellular inorganic polyphosphate (PolyP). The family corresponds a group of proteins similar to Escherichia coli exopolyphosphatase (EcPPX) and guanosine pentaphosphate phosphohydrolase (EcGppA). Unlike other PPX/GppA family members containing one PPX/GppA homolog, E. coli possesses two homologs, EcGppA and EcPPX.


Pssm-ID: 466903 [Multi-domain]  Cd Length: 292  Bit Score: 148.84  E-value: 6.95e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341821440   7 AVIDIGSNSLRLMTGwQEVPG--TWIFSPKElaTTRLGKDIDETHHLSPAGMEASFAAMERWKGQLTGIP---VCAVATS 81
Cdd:cd24053    1 AAVDLGSNSFHLLIA-RVDDGrlRVVDRLKE--RVRLAAGLDADGRLSPEAIERALECLARFGERLAGFPpdrVRVVGTN 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341821440  82 AVREAVDGQAFLAEVRARFGWHCRAISGLEEASLSFTGATASLNPDVTAA-VIDIGGGSSEVAAGRGGDLCWSHSYPMGA 160
Cdd:cd24053   78 TLRVARNAQQFLARAESALGHPIEVISGEEEARLIYLGVAHTLPDDSGRRlVIDIGGGSTELIIGEGFEPEFLESLPLGC 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341821440 161 VRFTR-----GEVmSHQDVAHLERHCYQEWLPmkIRPDLL-------IGVGGTLTTLAamdlQLAVYDAEkvEGHCISYE 228
Cdd:cd24053  158 VSYTKrffpdGEI-TAEAFQAAVAAARQELEP--IAARYKalgwdqaVGSSGTIKAIA----RVLEALGW--GGGGITRE 228
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 341821440 229 AL---------CGHIERLQAmtpeerrhvPGLQPKRSDIIIAGLLIAKSFLQRYQIPAITVSERDLMEGVFF 291
Cdd:cd24053  229 GLeklreellrAGSVARLDL---------PGLSPDRRAVFAGGLAILLALFEELGIDQLTVSDGALREGVLY 291
ASKHA_NBD_EcGppA-like cd24117
nucleotide-binding domain (NBD) of Escherichia coli guanosine pentaphosphate phosphohydrolase ...
7-291 4.46e-18

nucleotide-binding domain (NBD) of Escherichia coli guanosine pentaphosphate phosphohydrolase (EcGppA) and similar proteins; EcGppA (EC 3.6.1.40), also called guanosine-5'-triphosphate,3'-diphosphate pyrophosphatase, or pppGpp-5'-phosphohydrolase, catalyzes the conversion of guanosine pentaphosphate (pppGpp) to guanosine tetraphosphate (ppGpp). pppGpp is a cytoplasmic signaling molecule which together with ppGpp controls the 'stringent response', an adaptive process that allows bacteria to respond to amino acid starvation, resulting in the coordinated regulation of numerous cellular activities. EcGppA also has exopolyphosphatase activity, catalyzing the release of orthophosphate by processive hydrolysis of the phosphoanyhydride bonds of polyphosphate chains. Unlike other PPX/GppA family members containing one PPX/GppA homolog, E. coli possesses two homologs, EcGppA and EcPPX, which are indistinguishable in their domain arrangement.


Pssm-ID: 466967 [Multi-domain]  Cd Length: 290  Bit Score: 82.48  E-value: 4.46e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341821440   7 AVIDIGSNSLRLMTGwQEVPGTWIFSPKELATTRLGKDIDETHHLSPAGMEASFAAMERWKGQLTGIP---VCAVATSAV 83
Cdd:cd24117    1 AAIDLGSNSFHMLVV-REVAGSIQTLTKIKRKVRLAAGLDSENALSNEAMERGWQCLRLFAERLQDIPpdnIRVVATATL 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341821440  84 REAVDGQAFLAEVRARFGWHCRAISGLEEASLSFTG-ATASLNPDvTAAVIDIGGGSSEVAAGRGGDLCWSHSYPMGAV- 161
Cdd:cd24117   80 RLATNADVFIAKAQEILGHPVQVISGEEEARLIYQGvAHTSGGAG-NRLVVDIGGASTELIIGTGAQTTSLFSLSMGCVt 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341821440 162 ---RFTRGEVMSHQDVAH------------LERHCYQEWlpmkirpDLLIGVGGTLTTLA------AMDLQLAVYDAEKV 220
Cdd:cd24117  159 wleRYFADRNLSAENFEAaikaarevlrpvADELRYHGW-------QVCVGASGTVQALQeimvaqGMDERITLEKLQQL 231
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 341821440 221 EGHCIsyeaLCGHIERLQamtpeerrhVPGLQPKRSDIIIAGLLIAKSFLQRYQIPAITVSERDLMEGVFF 291
Cdd:cd24117  232 KQQAI----HCGKLEELE---------IDGLTLERALVFPSGLAILIAIFEELEIKCMTLAGGALREGLVY 289
ASKHA_NBD_EcPPX-like cd24116
nucleotide-binding domain (NBD) of Escherichia coli exopolyphosphatase (EcPPX) and similar ...
5-291 1.34e-17

nucleotide-binding domain (NBD) of Escherichia coli exopolyphosphatase (EcPPX) and similar proteins; EcPPX (EC 3.6.1.11), also called exopolyPase, or metaphosphatase, mediates the metabolism of cellular inorganic polyphosphate (polyP). It catalyzes degradation of polyP and releases orthophosphate processively from the ends of the polyP chain. It has a strong preference for long-chain polyphosphates and has only weak affinity for smaller size polyP of about 15 residues. Unlike other PPX/GppA family members containing one PPX/GppA homolog, E. coli possesses two homologs, EcGppA and EcPPX, which are indistinguishable in their domain arrangement.


Pssm-ID: 466966 [Multi-domain]  Cd Length: 299  Bit Score: 81.34  E-value: 1.34e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341821440   5 KYAVIDIGSNSLRLMTGwQEVPGTWIFSPKELATTRLGKDIDETHHLSPAGMEASFAAMERWKGQLTGIP---VCAVATS 81
Cdd:cd24116    1 EIAAIDLGSNSFHMVVA-RVVDGALQIISRLKQRVHLADGLDEDNVLSEEAMTRGLNCLALFAERLQGFEpesVCIVGTH 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341821440  82 AVREAVDGQAFLAEVRARFGWHCRAISGLEEASLSFTGATASLNPDVTAAVIDIGGGSSEVAAGRGGDLCWSHSYPMGAV 161
Cdd:cd24116   80 TLRQARNATDFLKRAEKVLPYPIEIISGNEEARLIYLGVAHTQPEKGRKLVIDIGGGSTELVIGEGFEPLLVESRQMGCV 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341821440 162 RFTR----GEVMSHQDVAHLERHCYQ--EWLPMKIRP---DLLIGVGGTLTTLAAMDLQLAVYDAekveghCISYEALCG 232
Cdd:cd24116  160 SFAQryfaGGVISKENFQRARMAAQQklETLAWQYRKqgwQVAFGSSGTIKAAHEVLIEMGEKDG------IITPERLEK 233
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 341821440 233 HIERLQAMTPEERRHVPGLQPKRSDIIIAGLLIAKSFLQRYQIPAITVSERDLMEGVFF 291
Cdd:cd24116  234 LIKEVLEADHFDSLSLPGLSEERKPVFVPGLAILCGVFDALAIRELRLSDGALREGVLY 292
PRK11031 PRK11031
guanosine-5'-triphosphate,3'-diphosphate diphosphatase;
6-161 8.42e-15

guanosine-5'-triphosphate,3'-diphosphate diphosphatase;


Pssm-ID: 236826 [Multi-domain]  Cd Length: 496  Bit Score: 74.61  E-value: 8.42e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341821440   6 YAVIDIGSNSLRlMTGWQEVPGtwifSPKELA----TTRLGKDIDETHHLSPAGMEASFAAMERWKGQLTGIP---VCAV 78
Cdd:PRK11031   8 YAAIDLGSNSFH-MLVVREVAG----SIQTLArikrKVRLAAGLDSDNALSNEAMERGWQCLRLFAERLQDIPpsqIRVV 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341821440  79 ATSAVREAVDGQAFLAEVRARFGWHCRAISGLEEASLSFTG-ATASLNPDvTAAVIDIGGGSSEVAAGRGGDLCWSHSYP 157
Cdd:PRK11031  83 ATATLRLAVNADEFLAKAQEILGCPVQVISGEEEARLIYQGvAHTTGGAD-QRLVVDIGGASTELVTGTGAQATSLFSLS 161

                 ....
gi 341821440 158 MGAV 161
Cdd:PRK11031 162 MGCV 165
PRK10854 PRK10854
exopolyphosphatase; Provisional
4-293 2.83e-14

exopolyphosphatase; Provisional


Pssm-ID: 182781 [Multi-domain]  Cd Length: 513  Bit Score: 72.84  E-value: 2.83e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341821440   4 QKYAVIDIGSNSL-----RLMTGWQEVPGtwifspKELATTRLGKDIDETHHLSPAGMEASFAAMERWKGQLTGIP---V 75
Cdd:PRK10854  11 QEFAAVDLGSNSFhmviaRVVDGAMQIIG------RLKQRVHLADGLDSDNMLSEEAMERGLNCLSLFAERLQGFSpanV 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341821440  76 CAVATSAVREAVDGQAFLAEVRARFGWHCRAISGLEEASLSFTGATASLNPDVTAAVIDIGGGSSEVAAGRGGDLCWSHS 155
Cdd:PRK10854  85 CIVGTHTLRQALNATDFLKRAEKVIPYPIEIISGNEEARLIFMGVEHTQPEKGRKLVIDIGGGSTELVIGENFEPILVES 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341821440 156 YPMGAVRFTR----GEVMSHQDV--AHLERHCYQEWLPMKIRP---DLLIGVGGTLTtlAAMDLQLAVYDAEKVeghcIS 226
Cdd:PRK10854 165 RRMGCVSFAQlyfpGGVISKENFqrARLAAAQKLETLAWQYRIqgwNVALGASGTIK--AAHEVLVEMGEKDGL----IT 238
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341821440 227 yealcghIERLQAMTPEERRH-------VPGLQPKRSDIIIAGLLIAKSFLQRYQIPAITVSERDLMEGVF------FRH 293
Cdd:PRK10854 239 -------PERLEMLVKEVLKHknfaalsLPGLSEERKTVFVPGLAILCGVFDALAIRELRLSDGALREGVLyemegrFRH 311
FtsA pfam14450
Cell division protein FtsA; FtsA is essential for bacterial cell division, and co-localizes to ...
131-166 7.70e-04

Cell division protein FtsA; FtsA is essential for bacterial cell division, and co-localizes to the septal ring with FtsZ. It has been suggested that the interaction of FtsA-FtsZ has arisen through coevolution in different bacterial strains. The FtsA protein contains two structurally related actin-like ATPase domains which are also structurally related to the ATPase domains of HSP70 (see PF00012). FtsA has a SHS2 domain PF02491 inserted in to the RnaseH fold PF02491.


Pssm-ID: 464177 [Multi-domain]  Cd Length: 167  Bit Score: 39.62  E-value: 7.70e-04
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 341821440  131 AVIDIGGGSSEVAAGRGGDLCWSHSYPMGAVRFTRG 166
Cdd:pfam14450   1 ALIDIGGGTTDIAVFEDGALRHTRVIPVGGNGITKD 36
FtsA COG0849
Cell division ATPase FtsA [Cell cycle control, cell division, chromosome partitioning];
108-159 4.40e-03

Cell division ATPase FtsA [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 440610 [Multi-domain]  Cd Length: 402  Bit Score: 38.19  E-value: 4.40e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 341821440 108 SGLEEASLSFTG---ATASLNPD---VTAAVIDIGGGSSEVAAGRGGDLCWSHSYPMG 159
Cdd:COG0849  174 AGLEVEDLVLSPlasAEAVLTEDekeLGVALVDIGGGTTDIAVFKDGALRHTAVIPVG 231
ASKHA_NBD_FtsA cd24048
nucleotide-binding domain (NBD) of cell division protein FtsA and similar proteins; FtsA is an ...
108-165 6.65e-03

nucleotide-binding domain (NBD) of cell division protein FtsA and similar proteins; FtsA is an essential cell division protein that assists in the assembly of the Z ring. It may serve as the principal membrane anchor for the Z ring. It is also required for the recruitment to the septal ring of the downstream cell division proteins FtsK, FtsQ, FtsL, FtsI and FtsN. FtsA binds ATP. FtsA interacts with FtsZ. This interaction plays an essential role in cell division.


Pssm-ID: 466898 [Multi-domain]  Cd Length: 372  Bit Score: 37.90  E-value: 6.65e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 341821440 108 SGLEEASLSFTG---ATASLNPD---VTAAVIDIGGGSSEVAAGRGGDLCWSHSYPMGAVRFTR 165
Cdd:cd24048  172 AGLEVDDIVLSPlasAEAVLTEDekeLGVALIDIGGGTTDIAVFKNGSLRYTAVIPVGGNHITN 235
 
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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