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Conserved domains on  [gi|49176408|ref|YP_026252|]
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guanosine-5'-triphosphate,3'-diphosphate phosphatase [Escherichia coli str. K-12 substr. MG1655]

Protein Classification

guanosine-5'-triphosphate,3'-diphosphate diphosphatase( domain architecture ID 11485156)

guanosine-5'-triphosphate,3'-diphosphate diphosphatase (GppA) catalyzes the conversion of pppGpp to ppGpp

CATH:  3.30.420.40
EC:  3.6.1.40
PubMed:  8800467|7781919
SCOP:  3000092

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PRK11031 PRK11031
guanosine-5'-triphosphate,3'-diphosphate diphosphatase;
1-494 0e+00

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


:

Pssm-ID: 236826 [Multi-domain]  Cd Length: 496  Bit Score: 1052.25  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176408    1 MGSTSSLYAAIDLGSNSFHMLVVREVAGSIQTLTRIKRKVRLAAGLNSENALSNEAMERGWQCLRLFAERLQDIPPSQIR 80
Cdd:PRK11031   1 MLSSSSLYAAIDLGSNSFHMLVVREVAGSIQTLARIKRKVRLAAGLDSDNALSNEAMERGWQCLRLFAERLQDIPPSQIR 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176408   81 VVATATLRLAVNAGDFIAKAQEILGCPVQVISGEEEARLIYQGVAHTTGGADQRLVVDIGGASTELVTGTGAQTTSLFSL 160
Cdd:PRK11031  81 VVATATLRLAVNADEFLAKAQEILGCPVQVISGEEEARLIYQGVAHTTGGADQRLVVDIGGASTELVTGTGAQATSLFSL 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176408  161 SMGCVTWLERYFADRNLGQENFDAAEKAAREVLRPVADELRYHGWKVCVGASGTVQALQEIMMAQGMDERITLEKLQQLK 240
Cdd:PRK11031 161 SMGCVTWLERYFKDRNLTQENFDAAEKAAREVLRPVADELREHGWQVCVGASGTVQALQEIMMAQGMDERITLAKLQQLK 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176408  241 QRAIHCGRLEELEIDGLTLERALVFPSGLAILIAIFTELNIQCMTLAGGALREGLVYGMLHLAVEQDIRSRTLRNIQRRF 320
Cdd:PRK11031 241 QRAIQCGRLEELEIEGLTLERALVFPSGLAILIAIFEELNIESMTLAGGALREGLVYGMLHLPVEQDIRSRTLRNIQRRF 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176408  321 MIDIDQAQRVAKVAANFFDQVENEWHLEAISRDLLISACQLHEIGLSVDFKQAPQHAAYLVRNLDLPGFTPAQKKLLATL 400
Cdd:PRK11031 321 QIDTEQAQRVAKLADNFLQQVENEWHLEPRSRELLISACQLHEIGLSVDFKQAPQHAAYLVRNLDLPGFTPAQKKLLATL 400
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176408  401 LLNQTNPVDLSSLHQQNAVPPRVAEQLCRLLRLAIIFASRRRDDLVPEMTLQANHELLTLTLPQGWLTQHPLGKEIIAQE 480
Cdd:PRK11031 401 LLNQTNPVDLSSLHQQNALPPRVAERLCRLLRLAIIFASRRRDDLLPEVTLQANDELLTLTLPQGWLAQHPLGAEELEQE 480
                        490
                 ....*....|....
gi 49176408  481 SQWQSYVHWPLEVH 494
Cdd:PRK11031 481 SQWQSYVHWPLEVE 494
 
Name Accession Description Interval E-value
PRK11031 PRK11031
guanosine-5'-triphosphate,3'-diphosphate diphosphatase;
1-494 0e+00

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


Pssm-ID: 236826 [Multi-domain]  Cd Length: 496  Bit Score: 1052.25  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176408    1 MGSTSSLYAAIDLGSNSFHMLVVREVAGSIQTLTRIKRKVRLAAGLNSENALSNEAMERGWQCLRLFAERLQDIPPSQIR 80
Cdd:PRK11031   1 MLSSSSLYAAIDLGSNSFHMLVVREVAGSIQTLARIKRKVRLAAGLDSDNALSNEAMERGWQCLRLFAERLQDIPPSQIR 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176408   81 VVATATLRLAVNAGDFIAKAQEILGCPVQVISGEEEARLIYQGVAHTTGGADQRLVVDIGGASTELVTGTGAQTTSLFSL 160
Cdd:PRK11031  81 VVATATLRLAVNADEFLAKAQEILGCPVQVISGEEEARLIYQGVAHTTGGADQRLVVDIGGASTELVTGTGAQATSLFSL 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176408  161 SMGCVTWLERYFADRNLGQENFDAAEKAAREVLRPVADELRYHGWKVCVGASGTVQALQEIMMAQGMDERITLEKLQQLK 240
Cdd:PRK11031 161 SMGCVTWLERYFKDRNLTQENFDAAEKAAREVLRPVADELREHGWQVCVGASGTVQALQEIMMAQGMDERITLAKLQQLK 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176408  241 QRAIHCGRLEELEIDGLTLERALVFPSGLAILIAIFTELNIQCMTLAGGALREGLVYGMLHLAVEQDIRSRTLRNIQRRF 320
Cdd:PRK11031 241 QRAIQCGRLEELEIEGLTLERALVFPSGLAILIAIFEELNIESMTLAGGALREGLVYGMLHLPVEQDIRSRTLRNIQRRF 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176408  321 MIDIDQAQRVAKVAANFFDQVENEWHLEAISRDLLISACQLHEIGLSVDFKQAPQHAAYLVRNLDLPGFTPAQKKLLATL 400
Cdd:PRK11031 321 QIDTEQAQRVAKLADNFLQQVENEWHLEPRSRELLISACQLHEIGLSVDFKQAPQHAAYLVRNLDLPGFTPAQKKLLATL 400
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176408  401 LLNQTNPVDLSSLHQQNAVPPRVAEQLCRLLRLAIIFASRRRDDLVPEMTLQANHELLTLTLPQGWLTQHPLGKEIIAQE 480
Cdd:PRK11031 401 LLNQTNPVDLSSLHQQNALPPRVAERLCRLLRLAIIFASRRRDDLLPEVTLQANDELLTLTLPQGWLAQHPLGAEELEQE 480
                        490
                 ....*....|....
gi 49176408  481 SQWQSYVHWPLEVH 494
Cdd:PRK11031 481 SQWQSYVHWPLEVE 494
ASKHA_NBD_EcGppA-like cd24117
nucleotide-binding domain (NBD) of Escherichia coli guanosine pentaphosphate phosphohydrolase ...
9-298 0e+00

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: 558.20  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176408   9 AAIDLGSNSFHMLVVREVAGSIQTLTRIKRKVRLAAGLNSENALSNEAMERGWQCLRLFAERLQDIPPSQIRVVATATLR 88
Cdd:cd24117   1 AAIDLGSNSFHMLVVREVAGSIQTLTKIKRKVRLAAGLDSENALSNEAMERGWQCLRLFAERLQDIPPDNIRVVATATLR 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176408  89 LAVNAGDFIAKAQEILGCPVQVISGEEEARLIYQGVAHTTGGADQRLVVDIGGASTELVTGTGAQTTSLFSLSMGCVTWL 168
Cdd:cd24117  81 LATNADVFIAKAQEILGHPVQVISGEEEARLIYQGVAHTSGGAGNRLVVDIGGASTELIIGTGAQTTSLFSLSMGCVTWL 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176408 169 ERYFADRNLGQENFDAAEKAAREVLRPVADELRYHGWKVCVGASGTVQALQEIMMAQGMDERITLEKLQQLKQRAIHCGR 248
Cdd:cd24117 161 ERYFADRNLSAENFEAAIKAAREVLRPVADELRYHGWQVCVGASGTVQALQEIMVAQGMDERITLEKLQQLKQQAIHCGK 240
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|
gi 49176408 249 LEELEIDGLTLERALVFPSGLAILIAIFTELNIQCMTLAGGALREGLVYG 298
Cdd:cd24117 241 LEELEIDGLTLERALVFPSGLAILIAIFEELEIKCMTLAGGALREGLVYG 290
Ppx-GppA pfam02541
Ppx/GppA phosphatase family; This family consists of the N-terminal region of ...
21-301 4.85e-122

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: 358.17  E-value: 4.85e-122
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176408    21 LVVREVAGSIQTLTRIKRKVRLAAGLNSENALSNEAMERGWQCLRLFAERLQDIPPSQIRVVATATLRLAVNAGDFIAKA 100
Cdd:pfam02541   1 VIARIVAGHLQIVAREKRKVRLAEGLNSTGRLNEEAIERTISALKEFAEILQGFGVENIRAVATSALRDAVNADEFLARV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176408   101 QEILGCPVQVISGEEEARLIYQGVAHTTGGADQRLVVDIGGASTELVTGTGAQTTSLFSLSMGCVTWLERYFADRNLGQE 180
Cdd:pfam02541  81 KKETGLPVEIISGEEEARLIYLGVVSTLGSKGRGLVIDIGGGSTELVLGENKKVRKLISLPMGCVRLTERFFHDDPLTKE 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176408   181 NFDAAEKAAREVLRPVADELRYHG-WKVCVGASGTVQALQEIMMAQG-MDERITLEKLQQLKQRAIHCGRLEELEIDGLT 258
Cdd:pfam02541 161 EVARARDAVRKELEEPKDEVRIGGgWIRALGTSGTISALAPLMALHGiMGYEITAEELEELIEKLSQITREDRLELAGVS 240
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 49176408   259 LERALVFPSGLAILIAIFTELNIQCMTLAGGALREGLVYGMLH 301
Cdd:pfam02541 241 DERADVIVAGALILSAVFEALSIEAMIISDGGLREGVLYSLLL 283
GppA COG0248
Exopolyphosphatase/pppGpp-phosphohydrolase [Nucleotide transport and metabolism, Signal ...
4-309 1.86e-119

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


Pssm-ID: 440018 [Multi-domain]  Cd Length: 314  Bit Score: 352.95  E-value: 1.86e-119
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176408   4 TSSLYAAIDLGSNSFHMLVVREVA-GSIQTLTRIKRKVRLAAGLNSENALSNEAMERGWQCLRLFAERLQDIPPSQIRVV 82
Cdd:COG0248   1 APMRLAAIDIGSNSVRLLIAEVDEgGSFRILDREKEPVRLGEGLDATGRLSEEAIERALAALKRFAELLREYGVERVRAV 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176408  83 ATATLRLAVNAGDFIAKAQEILGCPVQVISGEEEARLIYQGVAHTTGGADQR-LVVDIGGASTELVTGTGAQTTSLFSLS 161
Cdd:COG0248  81 ATSALREAKNGDEFLDRVKEETGLPIEVISGEEEARLIYLGVLSGLPLSDGRgLVVDIGGGSTELILGDGGEILFSESLP 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176408 162 MGCVTWLERYFADRNLGQENFDAAEKAAREVLRPVADELRYHGWKVCVGASGTVQALQEIMMAQG------MDERITLEK 235
Cdd:COG0248 161 LGAVRLTERFFPDDPPTAEEFAAAREYIREELEPLAKELRKGGPDTLVGTGGTIRTLARLLLALGrydekvHGYTLTREE 240
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 49176408 236 LQQLKQRAIHCGRLEELEIDGLTLERALVFPSGLAILIAIFTELNIQCMTLAGGALREGLVYGMLHLAVEQDIR 309
Cdd:COG0248 241 LEELIERLLSLTLEERAKLPGLSPDRADVILAGAAILEALMEALGIEEIVVSDRGLREGLLYDLLGRDGKKDDR 314
exo_poly_only TIGR03706
exopolyphosphatase; It appears that a single enzyme may act as both exopolyphosphatase (Ppx) ...
7-300 4.05e-107

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: 320.65  E-value: 4.05e-107
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176408     7 LYAAIDLGSNSFHMLVVREVAGSIQTLTRIKRKVRLAAGLNSENALSNEAMERGWQCLRLFAERLQDIPPSQIRVVATAT 86
Cdd:TIGR03706   1 PIAAIDIGSNSVRLVIARGVEGSLQVLFNEKEMVRLGEGLDSTGRLSEEAIERALEALKRFAELLRGFPVDEVRAVATAA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176408    87 LRLAVNAGDFIAKAQEILGCPVQVISGEEEARLIYQGVAHTTGGADqRLVVDIGGASTELVTGTGAQTTSLFSLSMGCVT 166
Cdd:TIGR03706  81 LRDAKNGPEFLKEAEAILGLPIEVISGEEEARLIYLGVAHTLPIAD-GLVVDIGGGSTELILGKDGEPGEGVSLPLGCVR 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176408   167 WLERYFADRNLGQENFDAAEKAAREVLRPvADELRYHGWKVCVGASGTVQALQEIMMAQ------GMDE-RITLEKLQQL 239
Cdd:TIGR03706 160 LTEQFFPDGPISKKSLKQARKAAREELAS-LKWLKKGGWRPLYGVGGTWRALARLHMAQrgyplhGLHGyEITAEGLLEL 238
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 49176408   240 KQRAIHCGRLEELEIDGLTLERALVFPSGLAILIAIFTELNIQCMTLAGGALREGLVYGML 300
Cdd:TIGR03706 239 LEELIKLSREERLKLPGLSKDRADILPGGAAILEELFRALGIEQIIFSSGGLREGVLYELL 299
 
Name Accession Description Interval E-value
PRK11031 PRK11031
guanosine-5'-triphosphate,3'-diphosphate diphosphatase;
1-494 0e+00

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


Pssm-ID: 236826 [Multi-domain]  Cd Length: 496  Bit Score: 1052.25  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176408    1 MGSTSSLYAAIDLGSNSFHMLVVREVAGSIQTLTRIKRKVRLAAGLNSENALSNEAMERGWQCLRLFAERLQDIPPSQIR 80
Cdd:PRK11031   1 MLSSSSLYAAIDLGSNSFHMLVVREVAGSIQTLARIKRKVRLAAGLDSDNALSNEAMERGWQCLRLFAERLQDIPPSQIR 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176408   81 VVATATLRLAVNAGDFIAKAQEILGCPVQVISGEEEARLIYQGVAHTTGGADQRLVVDIGGASTELVTGTGAQTTSLFSL 160
Cdd:PRK11031  81 VVATATLRLAVNADEFLAKAQEILGCPVQVISGEEEARLIYQGVAHTTGGADQRLVVDIGGASTELVTGTGAQATSLFSL 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176408  161 SMGCVTWLERYFADRNLGQENFDAAEKAAREVLRPVADELRYHGWKVCVGASGTVQALQEIMMAQGMDERITLEKLQQLK 240
Cdd:PRK11031 161 SMGCVTWLERYFKDRNLTQENFDAAEKAAREVLRPVADELREHGWQVCVGASGTVQALQEIMMAQGMDERITLAKLQQLK 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176408  241 QRAIHCGRLEELEIDGLTLERALVFPSGLAILIAIFTELNIQCMTLAGGALREGLVYGMLHLAVEQDIRSRTLRNIQRRF 320
Cdd:PRK11031 241 QRAIQCGRLEELEIEGLTLERALVFPSGLAILIAIFEELNIESMTLAGGALREGLVYGMLHLPVEQDIRSRTLRNIQRRF 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176408  321 MIDIDQAQRVAKVAANFFDQVENEWHLEAISRDLLISACQLHEIGLSVDFKQAPQHAAYLVRNLDLPGFTPAQKKLLATL 400
Cdd:PRK11031 321 QIDTEQAQRVAKLADNFLQQVENEWHLEPRSRELLISACQLHEIGLSVDFKQAPQHAAYLVRNLDLPGFTPAQKKLLATL 400
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176408  401 LLNQTNPVDLSSLHQQNAVPPRVAEQLCRLLRLAIIFASRRRDDLVPEMTLQANHELLTLTLPQGWLTQHPLGKEIIAQE 480
Cdd:PRK11031 401 LLNQTNPVDLSSLHQQNALPPRVAERLCRLLRLAIIFASRRRDDLLPEVTLQANDELLTLTLPQGWLAQHPLGAEELEQE 480
                        490
                 ....*....|....
gi 49176408  481 SQWQSYVHWPLEVH 494
Cdd:PRK11031 481 SQWQSYVHWPLEVE 494
ASKHA_NBD_EcGppA-like cd24117
nucleotide-binding domain (NBD) of Escherichia coli guanosine pentaphosphate phosphohydrolase ...
9-298 0e+00

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: 558.20  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176408   9 AAIDLGSNSFHMLVVREVAGSIQTLTRIKRKVRLAAGLNSENALSNEAMERGWQCLRLFAERLQDIPPSQIRVVATATLR 88
Cdd:cd24117   1 AAIDLGSNSFHMLVVREVAGSIQTLTKIKRKVRLAAGLDSENALSNEAMERGWQCLRLFAERLQDIPPDNIRVVATATLR 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176408  89 LAVNAGDFIAKAQEILGCPVQVISGEEEARLIYQGVAHTTGGADQRLVVDIGGASTELVTGTGAQTTSLFSLSMGCVTWL 168
Cdd:cd24117  81 LATNADVFIAKAQEILGHPVQVISGEEEARLIYQGVAHTSGGAGNRLVVDIGGASTELIIGTGAQTTSLFSLSMGCVTWL 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176408 169 ERYFADRNLGQENFDAAEKAAREVLRPVADELRYHGWKVCVGASGTVQALQEIMMAQGMDERITLEKLQQLKQRAIHCGR 248
Cdd:cd24117 161 ERYFADRNLSAENFEAAIKAAREVLRPVADELRYHGWQVCVGASGTVQALQEIMVAQGMDERITLEKLQQLKQQAIHCGK 240
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|
gi 49176408 249 LEELEIDGLTLERALVFPSGLAILIAIFTELNIQCMTLAGGALREGLVYG 298
Cdd:cd24117 241 LEELEIDGLTLERALVFPSGLAILIAIFEELEIKCMTLAGGALREGLVYG 290
ASKHA_NBD_EcPPX-GppA-like cd24053
nucleotide-binding domain (NBD) of Escherichia coli exopolyphosphatase (EcPPX), guanosine ...
9-297 1.06e-142

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: 411.16  E-value: 1.06e-142
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176408   9 AAIDLGSNSFHMLVVREVAGSIQTLTRIKRKVRLAAGLNSENALSNEAMERGWQCLRLFAERLQDIPPSQIRVVATATLR 88
Cdd:cd24053   1 AAVDLGSNSFHLLIARVDDGRLRVVDRLKERVRLAAGLDADGRLSPEAIERALECLARFGERLAGFPPDRVRVVGTNTLR 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176408  89 LAVNAGDFIAKAQEILGCPVQVISGEEEARLIYQGVAHTTGG-ADQRLVVDIGGASTELVTGTGAQTTSLFSLSMGCVTW 167
Cdd:cd24053  81 VARNAQQFLARAESALGHPIEVISGEEEARLIYLGVAHTLPDdSGRRLVIDIGGGSTELIIGEGFEPEFLESLPLGCVSY 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176408 168 LERYFADRNLGQENFDAAEKAAREVLRPVADELRYHGWKVCVGASGTVQALQEIMMAQGMDER-ITLEKLQQLKQRAIHC 246
Cdd:cd24053 161 TKRFFPDGEITAEAFQAAVAAARQELEPIAARYKALGWDQAVGSSGTIKAIARVLEALGWGGGgITREGLEKLREELLRA 240
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|.
gi 49176408 247 GRLEELEIDGLTLERALVFPSGLAILIAIFTELNIQCMTLAGGALREGLVY 297
Cdd:cd24053 241 GSVARLDLPGLSPDRRAVFAGGLAILLALFEELGIDQLTVSDGALREGVLY 291
PRK10854 PRK10854
exopolyphosphatase; Provisional
8-493 3.00e-126

exopolyphosphatase; Provisional


Pssm-ID: 182781 [Multi-domain]  Cd Length: 513  Bit Score: 377.53  E-value: 3.00e-126
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176408    8 YAAIDLGSNSFHMLVVREVAGSIQTLTRIKRKVRLAAGLNSENALSNEAMERGWQCLRLFAERLQDIPPSQIRVVATATL 87
Cdd:PRK10854  13 FAAVDLGSNSFHMVIARVVDGAMQIIGRLKQRVHLADGLDSDNMLSEEAMERGLNCLSLFAERLQGFSPANVCIVGTHTL 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176408   88 RLAVNAGDFIAKAQEILGCPVQVISGEEEARLIYQGVAHTTGGADQRLVVDIGGASTELVTGTGAQTTSLFSLSMGCVTW 167
Cdd:PRK10854  93 RQALNATDFLKRAEKVIPYPIEIISGNEEARLIFMGVEHTQPEKGRKLVIDIGGGSTELVIGENFEPILVESRRMGCVSF 172
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176408  168 LERYFADRNLGQENFDAAEKAAREVLRPVADELRYHGWKVCVGASGTVQALQEIMMAQG-MDERITLEKLQQLKQRAIHC 246
Cdd:PRK10854 173 AQLYFPGGVISKENFQRARLAAAQKLETLAWQYRIQGWNVALGASGTIKAAHEVLVEMGeKDGLITPERLEMLVKEVLKH 252
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176408  247 GRLEELEIDGLTLERALVFPSGLAILIAIFTELNIQCMTLAGGALREGLVYGMLHLAVEQDIRSRTLRNIQRRFMIDIDQ 326
Cdd:PRK10854 253 KNFAALSLPGLSEERKTVFVPGLAILCGVFDALAIRELRLSDGALREGVLYEMEGRFRHQDIRSRTAKSLANHYNIDREQ 332
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176408  327 AQRVAKVAANFFDQveneW----------HLEAisrdLLISACQLHEIGLSVDFKQAPQHAAYLVRNLDLPGFTPAQKKL 396
Cdd:PRK10854 333 ARRVLETTMQLYEQ----WreqnpklahpQLEA----LLKWAAMLHEVGLNINHSGLHRHSAYILQNTDLPGFNQEQQLM 404
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176408  397 LATLLLNQTNPVDLSSLHQQNAVPPRVAEQLCRLLRLAIIFASRRRDDLVPE-MTLQANHELLTLTLPQGWLTQHPLGKE 475
Cdd:PRK10854 405 LATLVRYHRKAIKLDDLPRFTLFKKKQYLPLIQLLRLGVLLNNQRQATTTPPtLRLITDDSHWTLRFPHDWFSQNALVLL 484
                        490
                 ....*....|....*....
gi 49176408  476 IIAQESQ-WQSYVHWPLEV 493
Cdd:PRK10854 485 DLEKEQEyWEDVTGWRLKI 503
Ppx-GppA pfam02541
Ppx/GppA phosphatase family; This family consists of the N-terminal region of ...
21-301 4.85e-122

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: 358.17  E-value: 4.85e-122
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176408    21 LVVREVAGSIQTLTRIKRKVRLAAGLNSENALSNEAMERGWQCLRLFAERLQDIPPSQIRVVATATLRLAVNAGDFIAKA 100
Cdd:pfam02541   1 VIARIVAGHLQIVAREKRKVRLAEGLNSTGRLNEEAIERTISALKEFAEILQGFGVENIRAVATSALRDAVNADEFLARV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176408   101 QEILGCPVQVISGEEEARLIYQGVAHTTGGADQRLVVDIGGASTELVTGTGAQTTSLFSLSMGCVTWLERYFADRNLGQE 180
Cdd:pfam02541  81 KKETGLPVEIISGEEEARLIYLGVVSTLGSKGRGLVIDIGGGSTELVLGENKKVRKLISLPMGCVRLTERFFHDDPLTKE 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176408   181 NFDAAEKAAREVLRPVADELRYHG-WKVCVGASGTVQALQEIMMAQG-MDERITLEKLQQLKQRAIHCGRLEELEIDGLT 258
Cdd:pfam02541 161 EVARARDAVRKELEEPKDEVRIGGgWIRALGTSGTISALAPLMALHGiMGYEITAEELEELIEKLSQITREDRLELAGVS 240
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 49176408   259 LERALVFPSGLAILIAIFTELNIQCMTLAGGALREGLVYGMLH 301
Cdd:pfam02541 241 DERADVIVAGALILSAVFEALSIEAMIISDGGLREGVLYSLLL 283
GppA COG0248
Exopolyphosphatase/pppGpp-phosphohydrolase [Nucleotide transport and metabolism, Signal ...
4-309 1.86e-119

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


Pssm-ID: 440018 [Multi-domain]  Cd Length: 314  Bit Score: 352.95  E-value: 1.86e-119
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176408   4 TSSLYAAIDLGSNSFHMLVVREVA-GSIQTLTRIKRKVRLAAGLNSENALSNEAMERGWQCLRLFAERLQDIPPSQIRVV 82
Cdd:COG0248   1 APMRLAAIDIGSNSVRLLIAEVDEgGSFRILDREKEPVRLGEGLDATGRLSEEAIERALAALKRFAELLREYGVERVRAV 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176408  83 ATATLRLAVNAGDFIAKAQEILGCPVQVISGEEEARLIYQGVAHTTGGADQR-LVVDIGGASTELVTGTGAQTTSLFSLS 161
Cdd:COG0248  81 ATSALREAKNGDEFLDRVKEETGLPIEVISGEEEARLIYLGVLSGLPLSDGRgLVVDIGGGSTELILGDGGEILFSESLP 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176408 162 MGCVTWLERYFADRNLGQENFDAAEKAAREVLRPVADELRYHGWKVCVGASGTVQALQEIMMAQG------MDERITLEK 235
Cdd:COG0248 161 LGAVRLTERFFPDDPPTAEEFAAAREYIREELEPLAKELRKGGPDTLVGTGGTIRTLARLLLALGrydekvHGYTLTREE 240
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 49176408 236 LQQLKQRAIHCGRLEELEIDGLTLERALVFPSGLAILIAIFTELNIQCMTLAGGALREGLVYGMLHLAVEQDIR 309
Cdd:COG0248 241 LEELIERLLSLTLEERAKLPGLSPDRADVILAGAAILEALMEALGIEEIVVSDRGLREGLLYDLLGRDGKKDDR 314
ASKHA_NBD_EcPPX-like cd24116
nucleotide-binding domain (NBD) of Escherichia coli exopolyphosphatase (EcPPX) and similar ...
9-299 2.35e-111

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: 331.72  E-value: 2.35e-111
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176408   9 AAIDLGSNSFHMLVVREVAGSIQTLTRIKRKVRLAAGLNSENALSNEAMERGWQCLRLFAERLQDIPPSQIRVVATATLR 88
Cdd:cd24116   3 AAIDLGSNSFHMVVARVVDGALQIISRLKQRVHLADGLDEDNVLSEEAMTRGLNCLALFAERLQGFEPESVCIVGTHTLR 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176408  89 LAVNAGDFIAKAQEILGCPVQVISGEEEARLIYQGVAHTTGGADQRLVVDIGGASTELVTGTGAQTTSLFSLSMGCVTWL 168
Cdd:cd24116  83 QARNATDFLKRAEKVLPYPIEIISGNEEARLIYLGVAHTQPEKGRKLVIDIGGGSTELVIGEGFEPLLVESRQMGCVSFA 162
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176408 169 ERYFADRNLGQENFDAAEKAAREVLRPVADELRYHGWKVCVGASGTVQALQEIMMAQGM-DERITLEKLQQLKQRAIHCG 247
Cdd:cd24116 163 QRYFAGGVISKENFQRARMAAQQKLETLAWQYRKQGWQVAFGSSGTIKAAHEVLIEMGEkDGIITPERLEKLIKEVLEAD 242
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|..
gi 49176408 248 RLEELEIDGLTLERALVFPSGLAILIAIFTELNIQCMTLAGGALREGLVYGM 299
Cdd:cd24116 243 HFDSLSLPGLSEERKPVFVPGLAILCGVFDALAIRELRLSDGALREGVLYEM 294
exo_poly_only TIGR03706
exopolyphosphatase; It appears that a single enzyme may act as both exopolyphosphatase (Ppx) ...
7-300 4.05e-107

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: 320.65  E-value: 4.05e-107
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176408     7 LYAAIDLGSNSFHMLVVREVAGSIQTLTRIKRKVRLAAGLNSENALSNEAMERGWQCLRLFAERLQDIPPSQIRVVATAT 86
Cdd:TIGR03706   1 PIAAIDIGSNSVRLVIARGVEGSLQVLFNEKEMVRLGEGLDSTGRLSEEAIERALEALKRFAELLRGFPVDEVRAVATAA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176408    87 LRLAVNAGDFIAKAQEILGCPVQVISGEEEARLIYQGVAHTTGGADqRLVVDIGGASTELVTGTGAQTTSLFSLSMGCVT 166
Cdd:TIGR03706  81 LRDAKNGPEFLKEAEAILGLPIEVISGEEEARLIYLGVAHTLPIAD-GLVVDIGGGSTELILGKDGEPGEGVSLPLGCVR 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176408   167 WLERYFADRNLGQENFDAAEKAAREVLRPvADELRYHGWKVCVGASGTVQALQEIMMAQ------GMDE-RITLEKLQQL 239
Cdd:TIGR03706 160 LTEQFFPDGPISKKSLKQARKAAREELAS-LKWLKKGGWRPLYGVGGTWRALARLHMAQrgyplhGLHGyEITAEGLLEL 238
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 49176408   240 KQRAIHCGRLEELEIDGLTLERALVFPSGLAILIAIFTELNIQCMTLAGGALREGLVYGML 300
Cdd:TIGR03706 239 LEELIKLSREERLKLPGLSKDRADILPGGAAILEELFRALGIEQIIFSSGGLREGVLYELL 299
ASKHA_NBD_AaPPX-GppA_MtPPX2-like cd24054
nucleotide-binding domain (NBD) of Aquifex aeolicus PPX/GppA, Mycobacterium tuberculosis PPX2, ...
8-297 8.67e-71

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: 227.36  E-value: 8.67e-71
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176408   8 YAAIDLGSNSFHMLVVREVAGSIQTLTRIKRKVRLAAGLNSENALSNEAMERGWQCLRLFAERLQDIPPSQIRVVATATL 87
Cdd:cd24054   1 IAAIDIGTNSVRLLIAEVDGGGLRVLLDERRITRLGEGLDETGRLSPEAIERTLEALKEFKKIAREYGVEKIRAVATSAL 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176408  88 RLAVNAGDFIAKAQEILGCPVQVISGEEEARLIYQGVAHTTGGADQR-LVVDIGGASTELVTGTGAQTTSLFSLSMGCVT 166
Cdd:cd24054  81 RDAKNRDEFLERVKEETGLEIEIISGEEEARLSFLGALSGLPLPDGPiLVIDIGGGSTELILGKGGGILFSVSLPLGAVR 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176408 167 WLERYFADRNLGQENFDAAEKAAREVLRPVADELRYhgwKVCVGASGTVQALqeIMMAQGMDE---------RITLEKLQ 237
Cdd:cd24054 161 LTERFLKSDPPSEEELEALREAIRELLEELLLPPKP---DRLVGVGGTATTL--AAIDLGLEEydpekihgyVLSLEELE 235
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176408 238 QLKQRAIHCGRLEELEIDGLTLERALVFPSGLAILIAIFTELNIQCMTLAGGALREGLVY 297
Cdd:cd24054 236 ELIDRLASMSLEERRKLPGLEPGRADIILAGALILLEILEYLGADELTVSDRGLREGLLL 295
ASKHA_NBD_PPX_GppA cd24006
nucleotide-binding domain (NBD) of the exopolyphosphatase/guanosine pentaphosphate ...
9-297 4.93e-70

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: 225.11  E-value: 4.93e-70
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176408   9 AAIDLGSNSFHMLVVREVA-GSIQTLTRIKRKVRLAAGLNSENALSNEAMERGWQCLRLFAERLQDIPPSQIRVVATATL 87
Cdd:cd24006   1 AAIDIGSNSIRLLIAEVDPdGSFRILERLREPVRLGEDVFTTGRISEEAIERAVEALRRFKKLADEYGVKRIRAVATSAV 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176408  88 RLAVNAGDFIAKAQEILGCPVQVISGEEEARLIYQGVAHTTGGADQR-LVVDIGGASTELVTGTGAQTTSLFSLSMGCVT 166
Cdd:cd24006  81 REASNGDEFLERIKRETGIDVEIISGEEEARLIYLAVRSGLPLGDGNaLIVDIGGGSTELTLGDNGEILFSESLPLGAVR 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176408 167 WLERYFADRNLGQENFDAAEKAAREVLRPVADELRYhGWKVCVGASGTVQALqeIMMAQGMDE-----RITLEKLQQLKQ 241
Cdd:cd24006 161 LTERFLKDDPPSELLEEYLRSFVRSVLRPLPKRRKI-KFDVAIGSGGTILAL--AAMALARKGkphgyEISREELKALYD 237
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 49176408 242 RAIHCGRLEELEIDGLTLERALVFPSGLAILIAIFTELNIQCMTLAGGALREGLVY 297
Cdd:cd24006 238 ELLRLSLEERRKKYGLSPDRADVIVPAALILLELLELLGAEEIIVPDVGLRDGLLL 293
ASKHA_NBD_HpPPX-GppA-like cd24052
nucleotide-binding domain (NBD) of Helicobacter pylori exopolyphosphatase/guanosine ...
8-300 1.15e-56

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: 190.39  E-value: 1.15e-56
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176408   8 YAAIDLGSNSFHMLVVREVAGSIQTLTRIKRKVRLAAGLNSENALSNEAMERGWQCLRLFAERLQDIPPSQIRVVATATL 87
Cdd:cd24052   1 IAIIDIGSNSIRLVIYEIEGGSFRLLFNEKETVGLGEYLDEDGKLSEEGIERAIKALKRFKKICEALGVDEIIAFATAAL 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176408  88 RLAVNAGDFIAKAQEILGCPVQVISGEEEARLIYQGVAHTTGGADQrLVVDIGGASTELVTGTGAQTTSLFSLSMGCVTW 167
Cdd:cd24052  81 RNAKNGEEFLERIKKETGIDIRVLSGEEEAYYGFLGVLNSLPLADG-LVVDIGGGSTELVLFKNGKIKESISLPLGSLRL 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176408 168 LERYFADRNLGQENFDAAEKAAREVLRPVADELRYHGwKVCVGASGTVQALQEIMMAQG-------MDERITLEKLQQLK 240
Cdd:cd24052 160 YERFVSGILPTEKELKKIRKFIKKELKKLPWLKEKKG-LPLYGVGGTIRALAKLHMELKnypldilHGYTISAEELDELL 238
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176408 241 QRAIHCGRLEELEIDGLTLERALVFPSGLAILIAIFTELNIQCMTLAGGALREGLVYGML 300
Cdd:cd24052 239 KKLKKLDKEERKKILGLSPDRADTIPPGALILKELLKYFGAKEIIVSGYGLREGYLYEKL 298
ASKHA_NBD_MtPPX2-like cd24119
nucleotide-binding domain (NBD) of Mycobacterium tuberculosis exopolyphosphatase 2 (MtPPX2) ...
9-296 4.05e-49

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: 170.52  E-value: 4.05e-49
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176408   9 AAIDLGSNSFHMLVVREVAGSIQTLTRIKRKVRLAAGLNSENALSNEAMERGWQCLRLFAERLQDIPPSQIRVVATATLR 88
Cdd:cd24119   2 AAIDIGTNSVRLLVADVDEGGLREVVRRTRITRLGEGVDATGRLSPEAIERTLAALAEYAALIRELGVERVRVVATSASR 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176408  89 LAVNAGDFIAKAQEILGCPVQVISGEEEARLIYQGVAHTTGGADQRLVVDIGGASTELVTGTGAQTTSLFSLSMGCVTWL 168
Cdd:cd24119  82 DASNRDDFLDRLESVLGVRPEVISGEEEARLSFLGATSGLPAPGPVLVVDIGGGSTELVLGRAGEVEAAISLDIGSVRLT 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176408 169 ERYFADRNLGQENFDAAEKAAREVLRPVADELRYHGWKVCVGASGTVQALqeIMMAQGMDE---------RITLEKLQQL 239
Cdd:cd24119 162 ERFLHSDPPTAEELEAARADVDAQLDEALDVVSLERATRLVGVAGTVTTL--AALALGLPEydpervhgyRLSLDQVEAV 239
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 49176408 240 KQRAIHCGRLEELEIDGLTLERALVFPSGLAILIAIFTELNIQCMTLAGGALREGLV 296
Cdd:cd24119 240 LRRLSAMTLEERAALPGLQPGRADVIVAGAVILSEVLRRLGIDEVVVSEHDILDGIA 296
ASKHA_NBD_MtPPX1-like cd24056
nucleotide-binding domain (NBD) of Mycobacterium tuberculosis exopolyphosphatase 1 (MtPPX1) ...
9-296 1.08e-46

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: 164.32  E-value: 1.08e-46
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176408   9 AAIDLGSNSFHMLVVR-EVAGSIQTLTRIKRKVRLAAGLNSENALSNEAMERGWQCLRLFAERLQDIPPSQIRVVATATL 87
Cdd:cd24056   3 AALDVGSNTFHLLVADvEGDGRLEPVADEKVMLRLGEDVARTGEIGPEAIDRAAEAVRRFVELARRLGAEELLAVATSAL 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176408  88 RLAVNAGDFIAKAQEILGCPVQVISGEEEARLIYQGVAHTTG-GADQRLVVDIGGASTELVTGTGAQTTSLFSLSMGcVT 166
Cdd:cd24056  83 REAENGPEVLDRVEAETGVPVRVLSGEEEARLTFLGARAALGwSSGPLLVLDLGGGSLELAVGVDGRPEWAASLPLG-SG 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176408 167 WL-ERYFADRNLGQENFDAAEKAAREVLRPVADELRYHGWKVCVGASGTVQALQEIMMAQGMDE------RITLEKLQQL 239
Cdd:cd24056 162 RLtARFLSSDPPSPEEVRALRAAVRAELAPALDRVRAGEPRRAVATGGTARALARLAGAARSPVgplnqrSLTREDLREL 241
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 49176408 240 KQRAIHCGRLEELEIDGLTLERALVFPSGLAILIAIFTELNIQCMTLAGGALREGLV 296
Cdd:cd24056 242 RRRLASLSAAERAELPGIDPRRADLLPAGALVLEALLDALGLEELVVSEWGLREGVI 298
ASKHA_NBD_ChPPX-like cd24055
nucleotide-binding domain (NBD) of Cytophaga hutchinsonii exopolyphosphatase (ChPPX) and ...
9-297 1.21e-46

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: 163.89  E-value: 1.21e-46
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176408   9 AAIDLGSNSFHMLVVREVAGSIQTLTRIKRKVRLAAGLNSENALSNEAMERGWQCLRLFAERLQDIPPSQIRVVATATLR 88
Cdd:cd24055   2 AVIDLGTNTFNLLIAEVDDGSFEILYREKVPVKLGKGGINIGIITDDAFERALDALKSFKQIAKQYGVDEIVAVGTSALR 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176408  89 LAVNAGDFIAKAQEILGCPVQVISGEEEARLIYQGVAHT-TGGADQRLVVDIGGASTELVTGTGAQTTSLFSLSMGcVTW 167
Cdd:cd24055  82 SAENGQEFIEKIKEELGIDIEIISGEREAELIYKGVRQAvPLTDEPALIMDIGGGSVEFILANNEQILWKKSFPIG-VAR 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176408 168 LERYFADRN-LGQENFDAAEKAAREVLRPVADELRYHGWKVCVGASGTVQALQEIMMAQGMDE--------RITLEKLQQ 238
Cdd:cd24055 161 LLEKFHPNDpISPEDIERLEAFLDEELADLFEALDQYKPTVLIGSSGSFDTLAEMIEANKGRTppagqssyEISLEEFEA 240
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 49176408 239 LKQRAIHCGRLEELEIDGLTLERALVFPSGLAILIAIFTELNIQCMTLAGGALREGLVY 297
Cdd:cd24055 241 LYQRLLTSTLEERLAIPGMIPMRADMIVVAAILIQHVLEKFGIPEIVVSPYALKEGLLF 299
ASKHA_NBD_AroB-like cd24120
nucleotide-binding domain (NBD) of Fusobacterium nucleatum bifunctional 3-dehydroquinate ...
9-297 1.26e-37

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: 139.76  E-value: 1.26e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176408   9 AAIDLGSNSFHMLVVREVAGSIQTLTRIKRKVRLAAGLNSENALSNEAMERGWQCLRLFAERLQDIPPSQIRVVATATLR 88
Cdd:cd24120   2 AAIDIGTNSCRLLIAEVEEGNVNPLFKKLETTRLGENVNKTGVLGKEAIERTVEVLKEYKRIADKYGVKKIIAFATSAVR 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176408  89 LAVNAGDFIAKAQEILGCPVQVISGEEEARLIYQGVAHTTGGADQR-LVVDIGGASTELVTGTGAQTTSLFSLSMGCVTW 167
Cdd:cd24120  82 DAKNKDEFIELVKRETGIKINVISGEEEAKLSFLGATSGLDSLYEKiLVIDIGGGSTEFTLGAPRGIKYVKSFNLGAVRL 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176408 168 LERYFADRNLGQENFDAAEKAAREVLRPVADELRYHGWKVCVGASGTVQALQEIMMAQGMDERITLEKLQQLKQRAI--- 244
Cdd:cd24120 162 TESFFGNDPPDYEELENMRNYVKDKLNETEKFKSLDFKLIGVAGTITTLAAIYLGLEVYDPEKVHGSKLTKEDIEENlkk 241
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*
gi 49176408 245 HCGRLEEL--EIDGLTLERALVFPSGLAILIAIFTELNIQCMTLAGGALREGLVY 297
Cdd:cd24120 242 LISLDLEErkKIPGLEPERADVIIAGTLILLEIMEILGKDFIIVSEADILEGIIL 296
ASKHA_NBD_AaPPX-GppA-like cd24118
nucleotide-binding domain (NBD) of Aquifex aeolicus exopolyphosphatase/guanosine ...
9-296 1.84e-28

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: 114.48  E-value: 1.84e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176408   9 AAIDLGSNSFHMLVVREVAGSIQTLTRIKRKVRLAAGLNSENALSNEAMERGWQCLRLFAERLQDIPPSQIRVVATATLR 88
Cdd:cd24118   2 ASIDIGSYSTRLTIADIEDGKLKILLEEGRITALGTGLKETGRLSEDRIEETLKVLKEYKKLIDEFGVERIKAVGTEAIR 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176408  89 LAVNAGDFIAKAQEILGCPVQVISGEEEARLIYQGVAHTTGGADQRLVVDIGGASTELVTGTGAQTTSLFSLSMGCVTWL 168
Cdd:cd24118  82 RAKNREEFLERVKEEVGLDLEVISPEEEGEYAFLAVAYSLKPKGEVCVVDQGGGSTEFVYGKGEKIEFLKSLPFGIVNLT 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176408 169 ERYFADRNLGQEN----FDAAEKAAREVLRPVaDELryhgwkvcVGASGTVQALQeimmaqGMDERITLEKLQQLKQRAI 244
Cdd:cd24118 162 EEFFKSDPPTEEEleslFNFLEKEISKIKKPV-DTV--------VGLGGTITTLA------ALEYNIYPYDPQKVHGKKL 226
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 49176408 245 HCGRL-------------EELEIDGLTLERALVFPSGLAILIAIFTELNIQCMTLAGGALREGLV 296
Cdd:cd24118 227 TYGRIkkwfdtlssmpseERKKIFQIEDRRAEVIIAGIAIFLKTMELFEKRSITVSDWGLLEGLL 291
 
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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