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Conserved domains on  [gi|1199203737|gb|OUR71753|]
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exopolyphosphatase [Arcobacter sp. 31_11_sub10_T18]

Protein Classification

Ppx/GppA phosphatase family protein( domain architecture ID 1904159)

Ppx/GppA phosphatase family protein similar to Pseudomonas aeruginosa exopolyphosphatase, which releases orthophosphate processively from the ends of inorganic polyphosphate (polyP) chains; belongs to the sugar kinase/HSP70/actin superfamily

Graphical summary

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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, ...
6-296 4.14e-86

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: 260.10  E-value: 4.14e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199203737   6 TIDLGSNSFRVLVYNYKKH--VVLKEYNEIVGTADDLINTGLISNEAIHRVIGAINKSSSELD-YNPRNSICVTTAAMRM 82
Cdd:cd24054     3 AIDIGTNSVRLLIAEVDGGglRVLLDERRITRLGEGLDETGRLSPEAIERTLEALKEFKKIAReYGVEKIRAVATSALRD 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199203737  83 AKNSDEVFKKVFTSTGVKLNIIDGEEEARLTLLAIKHALKRQKlqsEKFVLLDIGGGSVELTIHSNNQ-YIVKSFDFGIV 161
Cdd:cd24054    83 AKNRDEFLERVKEETGLEIEIISGEEEARLSFLGALSGLPLPD---GPILVIDIGGGSTELILGKGGGiLFSVSLPLGAV 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199203737 162 TMTQKF-QNDSILISELSKQTKKILSYLNDLNIELSNFEFIATAGTPTTIAAVKHGQNFldYNKEIVNGTVINLSDINTC 240
Cdd:cd24054   160 RLTERFlKSDPPSEEELEALREAIRELLEELLLPPKPDRLVGVGGTATTLAAIDLGLEE--YDPEKIHGYVLSLEELEEL 237
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1199203737 241 LSLLKNKSDFELNKIFG--PNSKDFIKVGILIYKSFFEILNKTESTVFDDGLKEGVAI 296
Cdd:cd24054   238 IDRLASMSLEERRKLPGlePGRADIILAGALILLEILEYLGADELTVSDRGLREGLLL 295
 
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, ...
6-296 4.14e-86

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: 260.10  E-value: 4.14e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199203737   6 TIDLGSNSFRVLVYNYKKH--VVLKEYNEIVGTADDLINTGLISNEAIHRVIGAINKSSSELD-YNPRNSICVTTAAMRM 82
Cdd:cd24054     3 AIDIGTNSVRLLIAEVDGGglRVLLDERRITRLGEGLDETGRLSPEAIERTLEALKEFKKIAReYGVEKIRAVATSALRD 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199203737  83 AKNSDEVFKKVFTSTGVKLNIIDGEEEARLTLLAIKHALKRQKlqsEKFVLLDIGGGSVELTIHSNNQ-YIVKSFDFGIV 161
Cdd:cd24054    83 AKNRDEFLERVKEETGLEIEIISGEEEARLSFLGALSGLPLPD---GPILVIDIGGGSTELILGKGGGiLFSVSLPLGAV 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199203737 162 TMTQKF-QNDSILISELSKQTKKILSYLNDLNIELSNFEFIATAGTPTTIAAVKHGQNFldYNKEIVNGTVINLSDINTC 240
Cdd:cd24054   160 RLTERFlKSDPPSEEELEALREAIRELLEELLLPPKPDRLVGVGGTATTLAAIDLGLEE--YDPEKIHGYVLSLEELEEL 237
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1199203737 241 LSLLKNKSDFELNKIFG--PNSKDFIKVGILIYKSFFEILNKTESTVFDDGLKEGVAI 296
Cdd:cd24054   238 IDRLASMSLEERRKLPGlePGRADIILAGALILLEILEYLGADELTVSDRGLREGLLL 295
GppA COG0248
Exopolyphosphatase/pppGpp-phosphohydrolase [Nucleotide transport and metabolism, Signal ...
7-304 3.93e-66

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


Pssm-ID: 440018 [Multi-domain]  Cd Length: 314  Bit Score: 209.66  E-value: 3.93e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199203737   7 IDLGSNSFRVLVYNYKKH---VVLKEYNEIVGTADDLINTGLISNEAIHRVIGAINKSSSEL-DYNPRNSICVTTAAMRM 82
Cdd:COG0248     8 IDIGSNSVRLLIAEVDEGgsfRILDREKEPVRLGEGLDATGRLSEEAIERALAALKRFAELLrEYGVERVRAVATSALRE 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199203737  83 AKNSDEVFKKVFTSTGVKLNIIDGEEEARLTLLAIKHALkrqKLQSEKFVLLDIGGGSVELTIHSNNQYI-VKSFDFGIV 161
Cdd:COG0248    88 AKNGDEFLDRVKEETGLPIEVISGEEEARLIYLGVLSGL---PLSDGRGLVVDIGGGSTELILGDGGEILfSESLPLGAV 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199203737 162 TMTQKFQNDSIL----ISELSKQTKKILSYLNDLNIELSNFEFIATAGTPTTIAAVKHGqnfLDYNKEIVNGTVINLSDI 237
Cdd:COG0248   165 RLTERFFPDDPPtaeeFAAAREYIREELEPLAKELRKGGPDTLVGTGGTIRTLARLLLA---LGRYDEKVHGYTLTREEL 241
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1199203737 238 NTCLSLLKNKSDFELNKIFG--PNSKDFIKVGILIYKSFFEILNKTESTVFDDGLKEGVAINFALEKDQ 304
Cdd:COG0248   242 EELIERLLSLTLEERAKLPGlsPDRADVILAGAAILEALMEALGIEEIVVSDRGLREGLLYDLLGRDGK 310
exo_poly_only TIGR03706
exopolyphosphatase; It appears that a single enzyme may act as both exopolyphosphatase (Ppx) ...
7-294 4.36e-42

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: 146.92  E-value: 4.36e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199203737   7 IDLGSNSFRVLVYNYKKH--VVLKEYNEIVGTADDLINTGLISNEAIHRVIGAInKSSSEL--DYNPRNSICVTTAAMRM 82
Cdd:TIGR03706   5 IDIGSNSVRLVIARGVEGslQVLFNEKEMVRLGEGLDSTGRLSEEAIERALEAL-KRFAELlrGFPVDEVRAVATAALRD 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199203737  83 AKNSDEVFKKVFTSTGVKLNIIDGEEEARLTLLAIKHAlkrqkLQSEKFVLLDIGGGSVELTIHSNNQYIV-KSFDFGIV 161
Cdd:TIGR03706  84 AKNGPEFLKEAEAILGLPIEVISGEEEARLIYLGVAHT-----LPIADGLVVDIGGGSTELILGKDGEPGEgVSLPLGCV 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199203737 162 TMTQKFQNDSILISELSKQTKKILSY-LNDLN--IELSNFEFIATAGTPTTIAAVkHgQNFLDYNKEIVNGTVINLSDIN 238
Cdd:TIGR03706 159 RLTEQFFPDGPISKKSLKQARKAAREeLASLKwlKKGGWRPLYGVGGTWRALARL-H-MAQRGYPLHGLHGYEITAEGLL 236
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1199203737 239 TCLSLLKNKSDFELNKIFG--PNSKDFIKVGILIYKSFFEILNKTESTVFDDGLKEGV 294
Cdd:TIGR03706 237 ELLEELIKLSREERLKLPGlsKDRADILPGGAAILEELFRALGIEQIIFSSGGLREGV 294
Ppx-GppA pfam02541
Ppx/GppA phosphatase family; This family consists of the N-terminal region of ...
43-294 3.23e-31

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: 118.20  E-value: 3.23e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199203737  43 TGLISNEAIHRVIGAInKSSSEL--DYNPRNSICVTTAAMRMAKNSDEVFKKVFTSTGVKLNIIDGEEEARLTLLAIKHA 120
Cdd:pfam02541  29 TGRLNEEAIERTISAL-KEFAEIlqGFGVENIRAVATSALRDAVNADEFLARVKKETGLPVEIISGEEEARLIYLGVVST 107
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199203737 121 LKrqklQSEKFVLLDIGGGSVELTIHSNNQY-IVKSFDFGIVTMTQKFQNDSILISE----LSKQTKKILS-YLNDLNIE 194
Cdd:pfam02541 108 LG----SKGRGLVIDIGGGSTELVLGENKKVrKLISLPMGCVRLTERFFHDDPLTKEevarARDAVRKELEePKDEVRIG 183
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199203737 195 LSNFEFIATAGTPTTIAAVKHGQNFLDYnkeivngtVINLSDINTCLSLLKNKSDFELNKIFG--PNSKDFIKVGILIYK 272
Cdd:pfam02541 184 GGWIRALGTSGTISALAPLMALHGIMGY--------EITAEELEELIEKLSQITREDRLELAGvsDERADVIVAGALILS 255
                         250       260
                  ....*....|....*....|..
gi 1199203737 273 SFFEILNKTESTVFDDGLKEGV 294
Cdd:pfam02541 256 AVFEALSIEAMIISDGGLREGV 277
PRK10854 PRK10854
exopolyphosphatase; Provisional
6-167 7.55e-15

exopolyphosphatase; Provisional


Pssm-ID: 182781 [Multi-domain]  Cd Length: 513  Bit Score: 74.77  E-value: 7.55e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199203737   6 TIDLGSNSFRVL---VYNYKKHVV--LKEYneiVGTADDLINTGLISNEAIHRVIGAINKSSSELDYNPRNSIC-VTTAA 79
Cdd:PRK10854   15 AVDLGSNSFHMViarVVDGAMQIIgrLKQR---VHLADGLDSDNMLSEEAMERGLNCLSLFAERLQGFSPANVCiVGTHT 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199203737  80 MRMAKNSDEVFKKVFTSTGVKLNIIDGEEEARLTLLAIKHAlkrQKLQSEKFVLlDIGGGSVELTIHSN-NQYIVKSFDF 158
Cdd:PRK10854   92 LRQALNATDFLKRAEKVIPYPIEIISGNEEARLIFMGVEHT---QPEKGRKLVI-DIGGGSTELVIGENfEPILVESRRM 167

                  ....*....
gi 1199203737 159 GIVTMTQKF 167
Cdd:PRK10854  168 GCVSFAQLY 176
 
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, ...
6-296 4.14e-86

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: 260.10  E-value: 4.14e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199203737   6 TIDLGSNSFRVLVYNYKKH--VVLKEYNEIVGTADDLINTGLISNEAIHRVIGAINKSSSELD-YNPRNSICVTTAAMRM 82
Cdd:cd24054     3 AIDIGTNSVRLLIAEVDGGglRVLLDERRITRLGEGLDETGRLSPEAIERTLEALKEFKKIAReYGVEKIRAVATSALRD 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199203737  83 AKNSDEVFKKVFTSTGVKLNIIDGEEEARLTLLAIKHALKRQKlqsEKFVLLDIGGGSVELTIHSNNQ-YIVKSFDFGIV 161
Cdd:cd24054    83 AKNRDEFLERVKEETGLEIEIISGEEEARLSFLGALSGLPLPD---GPILVIDIGGGSTELILGKGGGiLFSVSLPLGAV 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199203737 162 TMTQKF-QNDSILISELSKQTKKILSYLNDLNIELSNFEFIATAGTPTTIAAVKHGQNFldYNKEIVNGTVINLSDINTC 240
Cdd:cd24054   160 RLTERFlKSDPPSEEELEALREAIRELLEELLLPPKPDRLVGVGGTATTLAAIDLGLEE--YDPEKIHGYVLSLEELEEL 237
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1199203737 241 LSLLKNKSDFELNKIFG--PNSKDFIKVGILIYKSFFEILNKTESTVFDDGLKEGVAI 296
Cdd:cd24054   238 IDRLASMSLEERRKLPGlePGRADIILAGALILLEILEYLGADELTVSDRGLREGLLL 295
GppA COG0248
Exopolyphosphatase/pppGpp-phosphohydrolase [Nucleotide transport and metabolism, Signal ...
7-304 3.93e-66

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


Pssm-ID: 440018 [Multi-domain]  Cd Length: 314  Bit Score: 209.66  E-value: 3.93e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199203737   7 IDLGSNSFRVLVYNYKKH---VVLKEYNEIVGTADDLINTGLISNEAIHRVIGAINKSSSEL-DYNPRNSICVTTAAMRM 82
Cdd:COG0248     8 IDIGSNSVRLLIAEVDEGgsfRILDREKEPVRLGEGLDATGRLSEEAIERALAALKRFAELLrEYGVERVRAVATSALRE 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199203737  83 AKNSDEVFKKVFTSTGVKLNIIDGEEEARLTLLAIKHALkrqKLQSEKFVLLDIGGGSVELTIHSNNQYI-VKSFDFGIV 161
Cdd:COG0248    88 AKNGDEFLDRVKEETGLPIEVISGEEEARLIYLGVLSGL---PLSDGRGLVVDIGGGSTELILGDGGEILfSESLPLGAV 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199203737 162 TMTQKFQNDSIL----ISELSKQTKKILSYLNDLNIELSNFEFIATAGTPTTIAAVKHGqnfLDYNKEIVNGTVINLSDI 237
Cdd:COG0248   165 RLTERFFPDDPPtaeeFAAAREYIREELEPLAKELRKGGPDTLVGTGGTIRTLARLLLA---LGRYDEKVHGYTLTREEL 241
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1199203737 238 NTCLSLLKNKSDFELNKIFG--PNSKDFIKVGILIYKSFFEILNKTESTVFDDGLKEGVAINFALEKDQ 304
Cdd:COG0248   242 EELIERLLSLTLEERAKLPGlsPDRADVILAGAAILEALMEALGIEEIVVSDRGLREGLLYDLLGRDGK 310
ASKHA_NBD_PPX_GppA cd24006
nucleotide-binding domain (NBD) of the exopolyphosphatase/guanosine pentaphosphate ...
7-296 2.67e-53

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: 175.80  E-value: 2.67e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199203737   7 IDLGSNSFRVLVYNYKKH---VVLKEYNEIVGTADDLINTGLISNEAIHRVIGAINKSSSELD-YNPRNSICVTTAAMRM 82
Cdd:cd24006     3 IDIGSNSIRLLIAEVDPDgsfRILERLREPVRLGEDVFTTGRISEEAIERAVEALRRFKKLADeYGVKRIRAVATSAVRE 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199203737  83 AKNSDEVFKKVFTSTGVKLNIIDGEEEARLTLLAIKHALkrqKLQSEKFVLLDIGGGSVELTIHSNNQYI-VKSFDFGIV 161
Cdd:cd24006    83 ASNGDEFLERIKRETGIDVEIISGEEEARLIYLAVRSGL---PLGDGNALIVDIGGGSTELTLGDNGEILfSESLPLGAV 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199203737 162 TMTQKFQND----SILISELSKQTKKILSYLNDLNiELSNFEFIATAGTPTTIAAVKHGQNFLDynkeivNGTVINLSDI 237
Cdd:cd24006   160 RLTERFLKDdppsELLEEYLRSFVRSVLRPLPKRR-KIKFDVAIGSGGTILALAAMALARKGKP------HGYEISREEL 232
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1199203737 238 NTCLSLLKNKSDFELNKIFG--PNSKDFIKVGILIYKSFFEILNKTESTVFDDGLKEGVAI 296
Cdd:cd24006   233 KALYDELLRLSLEERRKKYGlsPDRADVIVPAALILLELLELLGAEEIIVPDVGLRDGLLL 293
ASKHA_NBD_HpPPX-GppA-like cd24052
nucleotide-binding domain (NBD) of Helicobacter pylori exopolyphosphatase/guanosine ...
7-294 3.33e-46

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: 157.64  E-value: 3.33e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199203737   7 IDLGSNSFRVLVYNYKKHVVLKEYNE--IVGTADDLINTGLISNEAIHRVIGAINKSSSELD-YNPRNSICVTTAAMRMA 83
Cdd:cd24052     4 IDIGSNSIRLVIYEIEGGSFRLLFNEkeTVGLGEYLDEDGKLSEEGIERAIKALKRFKKICEaLGVDEIIAFATAALRNA 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199203737  84 KNSDEVFKKVFTSTGVKLNIIDGEEEARLTLLAIKHALKrqklqSEKFVLLDIGGGSVELTIHSNNQYI-VKSFDFGIVT 162
Cdd:cd24052    84 KNGEEFLERIKKETGIDIRVLSGEEEAYYGFLGVLNSLP-----LADGLVVDIGGGSTELVLFKNGKIKeSISLPLGSLR 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199203737 163 MTQKFQNDSILISELSKQTKK-ILSYLNDLNIELSNFE--FIATAGTPTTIAavKHGQNFLDYNKEIVNGTVINLSDINT 239
Cdd:cd24052   159 LYERFVSGILPTEKELKKIRKfIKKELKKLPWLKEKKGlpLYGVGGTIRALA--KLHMELKNYPLDILHGYTISAEELDE 236
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1199203737 240 CLSLLKNKSDFELNKIFGPNSK--DFIKVGILIYKSFFEILNKTESTVFDDGLKEGV 294
Cdd:cd24052   237 LLKKLKKLDKEERKKILGLSPDraDTIPPGALILKELLKYFGAKEIIVSGYGLREGY 293
ASKHA_NBD_AroB-like cd24120
nucleotide-binding domain (NBD) of Fusobacterium nucleatum bifunctional 3-dehydroquinate ...
7-296 2.36e-44

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: 152.86  E-value: 2.36e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199203737   7 IDLGSNSFRVLVYNYKKHVVLKEYNEIVGT--ADDLINTGLISNEAIHRVIGAINKSSSELD-YNPRNSICVTTAAMRMA 83
Cdd:cd24120     4 IDIGTNSCRLLIAEVEEGNVNPLFKKLETTrlGENVNKTGVLGKEAIERTVEVLKEYKRIADkYGVKKIIAFATSAVRDA 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199203737  84 KNSDEVFKKVFTSTGVKLNIIDGEEEARLTLLAIKHALKRQKlqsEKFVLLDIGGGSVELTIhSNNQYI--VKSFDFGIV 161
Cdd:cd24120    84 KNKDEFIELVKRETGIKINVISGEEEAKLSFLGATSGLDSLY---EKILVIDIGGGSTEFTL-GAPRGIkyVKSFNLGAV 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199203737 162 TMTQKF-QNDSILISELSKQTKKILSYLNDLNIELSN-FEFIATAGTPTTIAAVKHGQNflDYNKEIVNGTVINLSDINT 239
Cdd:cd24120   160 RLTESFfGNDPPDYEELENMRNYVKDKLNETEKFKSLdFKLIGVAGTITTLAAIYLGLE--VYDPEKVHGSKLTKEDIEE 237
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1199203737 240 CLSLLKNKSDFELNKIFG--PNSKDFIKVGILIYKSFFEILNKTESTVFDDGLKEGVAI 296
Cdd:cd24120   238 NLKKLISLDLEERKKIPGlePERADVIIAGTLILLEIMEILGKDFIIVSEADILEGIIL 296
exo_poly_only TIGR03706
exopolyphosphatase; It appears that a single enzyme may act as both exopolyphosphatase (Ppx) ...
7-294 4.36e-42

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: 146.92  E-value: 4.36e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199203737   7 IDLGSNSFRVLVYNYKKH--VVLKEYNEIVGTADDLINTGLISNEAIHRVIGAInKSSSEL--DYNPRNSICVTTAAMRM 82
Cdd:TIGR03706   5 IDIGSNSVRLVIARGVEGslQVLFNEKEMVRLGEGLDSTGRLSEEAIERALEAL-KRFAELlrGFPVDEVRAVATAALRD 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199203737  83 AKNSDEVFKKVFTSTGVKLNIIDGEEEARLTLLAIKHAlkrqkLQSEKFVLLDIGGGSVELTIHSNNQYIV-KSFDFGIV 161
Cdd:TIGR03706  84 AKNGPEFLKEAEAILGLPIEVISGEEEARLIYLGVAHT-----LPIADGLVVDIGGGSTELILGKDGEPGEgVSLPLGCV 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199203737 162 TMTQKFQNDSILISELSKQTKKILSY-LNDLN--IELSNFEFIATAGTPTTIAAVkHgQNFLDYNKEIVNGTVINLSDIN 238
Cdd:TIGR03706 159 RLTEQFFPDGPISKKSLKQARKAAREeLASLKwlKKGGWRPLYGVGGTWRALARL-H-MAQRGYPLHGLHGYEITAEGLL 236
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1199203737 239 TCLSLLKNKSDFELNKIFG--PNSKDFIKVGILIYKSFFEILNKTESTVFDDGLKEGV 294
Cdd:TIGR03706 237 ELLEELIKLSREERLKLPGlsKDRADILPGGAAILEELFRALGIEQIIFSSGGLREGV 294
ASKHA_NBD_AaPPX-GppA-like cd24118
nucleotide-binding domain (NBD) of Aquifex aeolicus exopolyphosphatase/guanosine ...
4-296 2.18e-35

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: 129.50  E-value: 2.18e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199203737   4 VTTIDLGSNSFRVLVYNYK--KHVVLKEYNEIVGTADDLINTGLISNEAIHRVIGAINKSSSELD-YNPRNSICVTTAAM 80
Cdd:cd24118     1 IASIDIGSYSTRLTIADIEdgKLKILLEEGRITALGTGLKETGRLSEDRIEETLKVLKEYKKLIDeFGVERIKAVGTEAI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199203737  81 RMAKNSDEVFKKVFTSTGVKLNIIDGEEEARLTLLAIKHALKRQKlqseKFVLLDIGGGSVELtIHSNNQYI--VKSFDF 158
Cdd:cd24118    81 RRAKNREEFLERVKEEVGLDLEVISPEEEGEYAFLAVAYSLKPKG----EVCVVDQGGGSTEF-VYGKGEKIefLKSLPF 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199203737 159 GIVTMTQKF-QNDSILISELskqtKKILSYLND--LNIELSNFEFIATAGTPTTIAAVKHgqNFLDYNKEIVNGTVINLS 235
Cdd:cd24118   156 GIVNLTEEFfKSDPPTEEEL----ESLFNFLEKeiSKIKKPVDTVVGLGGTITTLAALEY--NIYPYDPQKVHGKKLTYG 229
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1199203737 236 DINTCLSLLKNKSDFELNKIFG--PNSKDFIKVGILIYKSFFEILNKTESTVFDDGLKEGVAI 296
Cdd:cd24118   230 RIKKWFDTLSSMPSEERKKIFQieDRRAEVIIAGIAIFLKTMELFEKRSITVSDWGLLEGLLV 292
Ppx-GppA pfam02541
Ppx/GppA phosphatase family; This family consists of the N-terminal region of ...
43-294 3.23e-31

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: 118.20  E-value: 3.23e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199203737  43 TGLISNEAIHRVIGAInKSSSEL--DYNPRNSICVTTAAMRMAKNSDEVFKKVFTSTGVKLNIIDGEEEARLTLLAIKHA 120
Cdd:pfam02541  29 TGRLNEEAIERTISAL-KEFAEIlqGFGVENIRAVATSALRDAVNADEFLARVKKETGLPVEIISGEEEARLIYLGVVST 107
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199203737 121 LKrqklQSEKFVLLDIGGGSVELTIHSNNQY-IVKSFDFGIVTMTQKFQNDSILISE----LSKQTKKILS-YLNDLNIE 194
Cdd:pfam02541 108 LG----SKGRGLVIDIGGGSTELVLGENKKVrKLISLPMGCVRLTERFFHDDPLTKEevarARDAVRKELEePKDEVRIG 183
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199203737 195 LSNFEFIATAGTPTTIAAVKHGQNFLDYnkeivngtVINLSDINTCLSLLKNKSDFELNKIFG--PNSKDFIKVGILIYK 272
Cdd:pfam02541 184 GGWIRALGTSGTISALAPLMALHGIMGY--------EITAEELEELIEKLSQITREDRLELAGvsDERADVIVAGALILS 255
                         250       260
                  ....*....|....*....|..
gi 1199203737 273 SFFEILNKTESTVFDDGLKEGV 294
Cdd:pfam02541 256 AVFEALSIEAMIISDGGLREGV 277
ASKHA_NBD_MtPPX1-like cd24056
nucleotide-binding domain (NBD) of Mycobacterium tuberculosis exopolyphosphatase 1 (MtPPX1) ...
7-299 5.94e-31

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: 117.71  E-value: 5.94e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199203737   7 IDLGSNSFRVLVYNYKKH---VVLKEYNEIVGTADDLINTGLISNEAIHRVIGAI--------NKSSSELdynprnsICV 75
Cdd:cd24056     5 LDVGSNTFHLLVADVEGDgrlEPVADEKVMLRLGEDVARTGEIGPEAIDRAAEAVrrfvelarRLGAEEL-------LAV 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199203737  76 TTAAMRMAKNSDEVFKKVFTSTGVKLNIIDGEEEARLTLLAIKHALkrqKLQSEKFVLLDIGGGSVELTIHSNNQ-YIVK 154
Cdd:cd24056    78 ATSALREAENGPEVLDRVEAETGVPVRVLSGEEEARLTFLGARAAL---GWSSGPLLVLDLGGGSLELAVGVDGRpEWAA 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199203737 155 SFDFGIVTMTQKF-QNDSILISELSKQTKKILSYLNDLNIELSNFE---FIATAGTPTTIAAVKHGQNFLDynkEIVNGT 230
Cdd:cd24056   155 SLPLGSGRLTARFlSSDPPSPEEVRALRAAVRAELAPALDRVRAGEprrAVATGGTARALARLAGAARSPV---GPLNQR 231
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1199203737 231 VINLSDINTCLSLLKNKSDFELNKIFG--PNSKDFIKVGILIYKSFFEILNKTESTVFDDGLKEGVAINFA 299
Cdd:cd24056   232 SLTREDLRELRRRLASLSAAERAELPGidPRRADLLPAGALVLEALLDALGLEELVVSEWGLREGVILDEL 302
ASKHA_NBD_ChPPX-like cd24055
nucleotide-binding domain (NBD) of Cytophaga hutchinsonii exopolyphosphatase (ChPPX) and ...
7-218 3.26e-29

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: 113.04  E-value: 3.26e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199203737   7 IDLGSNSFRVLV--YNYKKHVVLKEYNEIVGTADDLINTGLISNEAIHRVIGAINKSSSELD-YNPRNSICVTTAAMRMA 83
Cdd:cd24055     4 IDLGTNTFNLLIaeVDDGSFEILYREKVPVKLGKGGINIGIITDDAFERALDALKSFKQIAKqYGVDEIVAVGTSALRSA 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199203737  84 KNSDEVFKKVFTSTGVKLNIIDGEEEARLTLLAIKHALkrqKLQSEKFVLLDIGGGSVELTIHSNNQ-YIVKSFDFGIVT 162
Cdd:cd24055    84 ENGQEFIEKIKEELGIDIEIISGEREAELIYKGVRQAV---PLTDEPALIMDIGGGSVEFILANNEQiLWKKSFPIGVAR 160
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199203737 163 MTQKF-QNDSILISELSKQTKKILSYLNDLNIELSNFE---FIATAGTPTTIAAVKHGQN 218
Cdd:cd24055   161 LLEKFhPNDPISPEDIERLEAFLDEELADLFEALDQYKptvLIGSSGSFDTLAEMIEANK 220
ASKHA_NBD_MtPPX2-like cd24119
nucleotide-binding domain (NBD) of Mycobacterium tuberculosis exopolyphosphatase 2 (MtPPX2) ...
4-237 4.13e-26

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: 104.65  E-value: 4.13e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199203737   4 VTTIDLGSNSFRVLVYNYKKHVV--LKEYNEIVGTADDLINTGLISNEAIHRVIGAINKSSSELD-YNPRNSICVTTAAM 80
Cdd:cd24119     1 VAAIDIGTNSVRLLVADVDEGGLreVVRRTRITRLGEGVDATGRLSPEAIERTLAALAEYAALIReLGVERVRVVATSAS 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199203737  81 RMAKNSDEVFKKVFTSTGVKLNIIDGEEEARLTLLAIKHALKRQklqsEKFVLLDIGGGSVELTIHSNNQYI-VKSFDFG 159
Cdd:cd24119    81 RDASNRDDFLDRLESVLGVRPEVISGEEEARLSFLGATSGLPAP----GPVLVVDIGGGSTELVLGRAGEVEaAISLDIG 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199203737 160 IVTMTQKF-QNDSILISELSKQTKKILSYLNDLNIELSNFE---FIATAGTPTTIAAVkhGQNFLDYNKEIVNGTVINLS 235
Cdd:cd24119   157 SVRLTERFlHSDPPTAEELEAARADVDAQLDEALDVVSLERatrLVGVAGTVTTLAAL--ALGLPEYDPERVHGYRLSLD 234

                  ..
gi 1199203737 236 DI 237
Cdd:cd24119   235 QV 236
ASKHA_NBD_EcPPX-GppA-like cd24053
nucleotide-binding domain (NBD) of Escherichia coli exopolyphosphatase (EcPPX), guanosine ...
7-294 1.29e-23

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: 97.61  E-value: 1.29e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199203737   7 IDLGSNSFRVLV--YNYKKHVVLKEYNEIVGTADDLINTGLISNEAIHRVIGAINKSSSELDYNPRNSICVT-TAAMRMA 83
Cdd:cd24053     3 VDLGSNSFHLLIarVDDGRLRVVDRLKERVRLAAGLDADGRLSPEAIERALECLARFGERLAGFPPDRVRVVgTNTLRVA 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199203737  84 KNSDEVFKKVFTSTGVKLNIIDGEEEARLTLLAIKHALkrqKLQSEKFVLLDIGGGSVELTIHSNNQYI-VKSFDFGIVT 162
Cdd:cd24053    83 RNAQQFLARAESALGHPIEVISGEEEARLIYLGVAHTL---PDDSGRRLVIDIGGGSTELIIGEGFEPEfLESLPLGCVS 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199203737 163 MTQKFQNDSIL--------ISELSKQTKKILSYLNDLNIElsnfEFIATAGTPTTIAAVKHGQNFldynkeivNGTVINL 234
Cdd:cd24053   160 YTKRFFPDGEItaeafqaaVAAARQELEPIAARYKALGWD----QAVGSSGTIKAIARVLEALGW--------GGGGITR 227
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1199203737 235 SDintcLSLLKNK--SDFELNKI----FGPNSKDFIKVGILIYKSFFEILNKTESTVFDDGLKEGV 294
Cdd:cd24053   228 EG----LEKLREEllRAGSVARLdlpgLSPDRRAVFAGGLAILLALFEELGIDQLTVSDGALREGV 289
ASKHA_NBD_EcPPX-like cd24116
nucleotide-binding domain (NBD) of Escherichia coli exopolyphosphatase (EcPPX) and similar ...
4-294 7.15e-16

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: 76.33  E-value: 7.15e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199203737   4 VTTIDLGSNSFRVLVynykKHVV------LKEYNEIVGTADDLINTGLISNEAIHRVIGAINKSSSELD-YNPRNSICVT 76
Cdd:cd24116     2 IAAIDLGSNSFHMVV----ARVVdgalqiISRLKQRVHLADGLDEDNVLSEEAMTRGLNCLALFAERLQgFEPESVCIVG 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199203737  77 TAAMRMAKNSDEVFKKVFTSTGVKLNIIDGEEEARLTLLAIKHAlkrQKLQSEKFVlLDIGGGSVELTIHSN-NQYIVKS 155
Cdd:cd24116    78 THTLRQARNATDFLKRAEKVLPYPIEIISGNEEARLIYLGVAHT---QPEKGRKLV-IDIGGGSTELVIGEGfEPLLVES 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199203737 156 FDFGIVTMTQKFQNDSILISELSKQTkkILSYLNDLniELSNFEF--------IATAGTPTTIAAVKHGQNFLDynkeiv 227
Cdd:cd24116   154 RQMGCVSFAQRYFAGGVISKENFQRA--RMAAQQKL--ETLAWQYrkqgwqvaFGSSGTIKAAHEVLIEMGEKD------ 223
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199203737 228 ngTVINLSDINTCLS-LLKNKSDFELNkIFGPNS--KDFIKVGILIYKSFFEILNKTESTVFDDGLKEGV 294
Cdd:cd24116   224 --GIITPERLEKLIKeVLEADHFDSLS-LPGLSEerKPVFVPGLAILCGVFDALAIRELRLSDGALREGV 290
ASKHA_NBD_EcGppA-like cd24117
nucleotide-binding domain (NBD) of Escherichia coli guanosine pentaphosphate phosphohydrolase ...
7-173 9.18e-16

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: 75.93  E-value: 9.18e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199203737   7 IDLGSNSFRVLVYnykKHV-----VLKEYNEIVGTADDLINTGLISNEAIHRVIGAINKSSSELDYNPRNSI-CVTTAAM 80
Cdd:cd24117     3 IDLGSNSFHMLVV---REVagsiqTLTKIKRKVRLAAGLDSENALSNEAMERGWQCLRLFAERLQDIPPDNIrVVATATL 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199203737  81 RMAKNSDEVFKKVFTSTGVKLNIIDGEEEARLTLLAIKHALKRQKLQsekfVLLDIGGGSVELTIHSNNQYI-VKSFDFG 159
Cdd:cd24117    80 RLATNADVFIAKAQEILGHPVQVISGEEEARLIYQGVAHTSGGAGNR----LVVDIGGASTELIIGTGAQTTsLFSLSMG 155
                         170
                  ....*....|....
gi 1199203737 160 IVTMTQKFQNDSIL 173
Cdd:cd24117   156 CVTWLERYFADRNL 169
PRK10854 PRK10854
exopolyphosphatase; Provisional
6-167 7.55e-15

exopolyphosphatase; Provisional


Pssm-ID: 182781 [Multi-domain]  Cd Length: 513  Bit Score: 74.77  E-value: 7.55e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199203737   6 TIDLGSNSFRVL---VYNYKKHVV--LKEYneiVGTADDLINTGLISNEAIHRVIGAINKSSSELDYNPRNSIC-VTTAA 79
Cdd:PRK10854   15 AVDLGSNSFHMViarVVDGAMQIIgrLKQR---VHLADGLDSDNMLSEEAMERGLNCLSLFAERLQGFSPANVCiVGTHT 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199203737  80 MRMAKNSDEVFKKVFTSTGVKLNIIDGEEEARLTLLAIKHAlkrQKLQSEKFVLlDIGGGSVELTIHSN-NQYIVKSFDF 158
Cdd:PRK10854   92 LRQALNATDFLKRAEKVIPYPIEIISGNEEARLIFMGVEHT---QPEKGRKLVI-DIGGGSTELVIGENfEPILVESRRM 167

                  ....*....
gi 1199203737 159 GIVTMTQKF 167
Cdd:PRK10854  168 GCVSFAQLY 176
PRK11031 PRK11031
guanosine-5'-triphosphate,3'-diphosphate diphosphatase;
7-170 8.96e-14

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


Pssm-ID: 236826 [Multi-domain]  Cd Length: 496  Bit Score: 71.53  E-value: 8.96e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199203737   7 IDLGSNSFRVLVYnykKHV-----VLKEYNEIVGTADDLINTGLISNEAIHRVIGAINKSSSELDYNPRNSIC-VTTAAM 80
Cdd:PRK11031   11 IDLGSNSFHMLVV---REVagsiqTLARIKRKVRLAAGLDSDNALSNEAMERGWQCLRLFAERLQDIPPSQIRvVATATL 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199203737  81 RMAKNSDEVFKKVFTSTGVKLNIIDGEEEARLtllaIKHALKRQKLQSEKFVLLDIGGGSVELTIHSNNQY-IVKSFDFG 159
Cdd:PRK11031   88 RLAVNADEFLAKAQEILGCPVQVISGEEEARL----IYQGVAHTTGGADQRLVVDIGGASTELVTGTGAQAtSLFSLSMG 163
                         170
                  ....*....|.
gi 1199203737 160 IVTMTQKFQND 170
Cdd:PRK11031  164 CVTWLERYFKD 174
ASKHA_NBD_GDA1_CD39_NTPase cd24003
nucleotide-binding domain (NBD) of the GDA1/CD39 NTPase family; The GDA1/CD39 NTPase family ...
7-166 2.89e-04

nucleotide-binding domain (NBD) of the GDA1/CD39 NTPase family; The GDA1/CD39 NTPase family contains a group of apyrases (also known as adenylpyrophophatase, or ATP-diphosphohydrolases; EC 3.6.1.5), which are enzymes that catalyze the hydrolysis of phosphoanhydride bonds of nucleoside tri- and diphosphates (NTPs and NDPs) in the presence of divalent cations. In vertebrate systems, especially in mammals, apyrases are more widely referred to as nucleoside triphosphate diphosphohydrolases (NTPDases). There are eight homologs of NTPDases (NTPDases 1-8) in mammals, two apyrase enzymes from yeast, GDA1 and YND1, and a total of seven homologs of apyrase, namely AtAPY1-7, found in Arabidopsis. The GDA1/CD39 NTPase family belongs to the ASKHA (Acetate and Sugar Kinases/Hsc70/Actin) superfamily, all members of which share a common characteristic five-stranded beta sheet occurring in both the N- and C-terminal domains.


Pssm-ID: 466853  Cd Length: 332  Bit Score: 41.99  E-value: 2.89e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199203737   7 IDLGSNSFRVLVYNYKKHVvLKEYNEIVGTADDLINTGLISN-------EAIHRVIGA-INKSSSELDYNPRNSICVT-- 76
Cdd:cd24003     5 IDAGSSGTRLHVYKWKARS-DDLPSIIELVSSGKEKSGKISSssyaddpDEAKKYLQPlLEFAKAVVPEDRRSSTPVYll 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199203737  77 -TAAMRMAKNSD-----EVFKKVFTSTGVKLN-----IIDGEEEARLTLLAIKHALKRQKLQSEK--FVLLDIGGGSVEL 143
Cdd:cd24003    84 aTAGMRLLPEEQqeailDAVRTILRNSGFGFDdgwvrVISGEEEGLYGWLSVNYLLGNLGSEPAKktVGVLDLGGASTQI 163
                         170       180
                  ....*....|....*....|...
gi 1199203737 144 TIHSNNQYIVKSFDFGIVTMTQK 166
Cdd:cd24003   164 AFEPPEDDLSSLSNVYPLRLGGK 186
 
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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