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Conserved domains on  [gi|491623424|ref|WP_005480964|]
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MULTISPECIES: guanosine-5'-triphosphate,3'-diphosphate diphosphatase [Vibrio]

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;
3-494 0e+00

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


:

Pssm-ID: 236826 [Multi-domain]  Cd Length: 496  Bit Score: 903.95  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491623424   3 QAGSSPLYAAIDLGSNSFHMLVVRHIDGSVQTMAKIKRKVRLAAGLDEHNSLSMEAMQRGWDCLSLFAERLQDIPTQNIR 82
Cdd:PRK11031   1 MLSSSSLYAAIDLGSNSFHMLVVREVAGSIQTLARIKRKVRLAAGLDSDNALSNEAMERGWQCLRLFAERLQDIPPSQIR 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491623424  83 IVGTATLRTATNVDVFLEKANQILGQPIEVISGEEEAATIYKGVAHTSGGSGRRLVVDIGGASTELIIGEGFEAKALTSL 162
Cdd:PRK11031  81 VVATATLRLAVNADEFLAKAQEILGCPVQVISGEEEARLIYQGVAHTTGGADQRLVVDIGGASTELVTGTGAQATSLFSL 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491623424 163 KMGCVTWLENFFKDRQLNARNFEAAIEGAKQTIKPILEQYTDLGWDVCVGASGTVQALQEIMLAQGMDEVITHSKLKRLQ 242
Cdd:PRK11031 161 SMGCVTWLERYFKDRNLTQENFDAAEKAAREVLRPVADELREHGWQVCVGASGTVQALQEIMMAQGMDERITLAKLQQLK 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491623424 243 KQAMLADHLEELDIEGLTLERALVFPSGLSILIAIFELLEIDAMTLAGGALREGLVYEMVDELRQNDIRARTICSVQSRY 322
Cdd:PRK11031 241 QRAIQCGRLEELEIEGLTLERALVFPSGLAILIAIFEELNIESMTLAGGALREGLVYGMLHLPVEQDIRSRTLRNIQRRF 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491623424 323 QLDCQYGEQVATLAGKLLEQAGGdEWIAEPQGKVLLETTAKLHEIGLTIDFKKGGEHSAYLLQNLDLPGYTRAQKFFIGE 402
Cdd:PRK11031 321 QIDTEQAQRVAKLADNFLQQVEN-EWHLEPRSRELLISACQLHEIGLSVDFKQAPQHAAYLVRNLDLPGFTPAQKKLLAT 399
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491623424 403 IARRYRE--QLSSLPEQHAISGTSAKRVLRLLRLAVLLTHRRNPSLEPQVELLAEGDKLTLSIDAKWLEANPLTAAELEI 480
Cdd:PRK11031 400 LLLNQTNpvDLSSLHQQNALPPRVAERLCRLLRLAIIFASRRRDDLLPEVTLQANDELLTLTLPQGWLAQHPLGAEELEQ 479
                        490
                 ....*....|....
gi 491623424 481 ESNRQTDIGWPLTI 494
Cdd:PRK11031 480 ESQWQSYVHWPLEV 493
 
Name Accession Description Interval E-value
PRK11031 PRK11031
guanosine-5'-triphosphate,3'-diphosphate diphosphatase;
3-494 0e+00

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


Pssm-ID: 236826 [Multi-domain]  Cd Length: 496  Bit Score: 903.95  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491623424   3 QAGSSPLYAAIDLGSNSFHMLVVRHIDGSVQTMAKIKRKVRLAAGLDEHNSLSMEAMQRGWDCLSLFAERLQDIPTQNIR 82
Cdd:PRK11031   1 MLSSSSLYAAIDLGSNSFHMLVVREVAGSIQTLARIKRKVRLAAGLDSDNALSNEAMERGWQCLRLFAERLQDIPPSQIR 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491623424  83 IVGTATLRTATNVDVFLEKANQILGQPIEVISGEEEAATIYKGVAHTSGGSGRRLVVDIGGASTELIIGEGFEAKALTSL 162
Cdd:PRK11031  81 VVATATLRLAVNADEFLAKAQEILGCPVQVISGEEEARLIYQGVAHTTGGADQRLVVDIGGASTELVTGTGAQATSLFSL 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491623424 163 KMGCVTWLENFFKDRQLNARNFEAAIEGAKQTIKPILEQYTDLGWDVCVGASGTVQALQEIMLAQGMDEVITHSKLKRLQ 242
Cdd:PRK11031 161 SMGCVTWLERYFKDRNLTQENFDAAEKAAREVLRPVADELREHGWQVCVGASGTVQALQEIMMAQGMDERITLAKLQQLK 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491623424 243 KQAMLADHLEELDIEGLTLERALVFPSGLSILIAIFELLEIDAMTLAGGALREGLVYEMVDELRQNDIRARTICSVQSRY 322
Cdd:PRK11031 241 QRAIQCGRLEELEIEGLTLERALVFPSGLAILIAIFEELNIESMTLAGGALREGLVYGMLHLPVEQDIRSRTLRNIQRRF 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491623424 323 QLDCQYGEQVATLAGKLLEQAGGdEWIAEPQGKVLLETTAKLHEIGLTIDFKKGGEHSAYLLQNLDLPGYTRAQKFFIGE 402
Cdd:PRK11031 321 QIDTEQAQRVAKLADNFLQQVEN-EWHLEPRSRELLISACQLHEIGLSVDFKQAPQHAAYLVRNLDLPGFTPAQKKLLAT 399
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491623424 403 IARRYRE--QLSSLPEQHAISGTSAKRVLRLLRLAVLLTHRRNPSLEPQVELLAEGDKLTLSIDAKWLEANPLTAAELEI 480
Cdd:PRK11031 400 LLLNQTNpvDLSSLHQQNALPPRVAERLCRLLRLAIIFASRRRDDLLPEVTLQANDELLTLTLPQGWLAQHPLGAEELEQ 479
                        490
                 ....*....|....
gi 491623424 481 ESNRQTDIGWPLTI 494
Cdd:PRK11031 480 ESQWQSYVHWPLEV 493
ASKHA_NBD_EcGppA-like cd24117
nucleotide-binding domain (NBD) of Escherichia coli guanosine pentaphosphate phosphohydrolase ...
11-300 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: 542.80  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491623424  11 AAIDLGSNSFHMLVVRHIDGSVQTMAKIKRKVRLAAGLDEHNSLSMEAMQRGWDCLSLFAERLQDIPTQNIRIVGTATLR 90
Cdd:cd24117    1 AAIDLGSNSFHMLVVREVAGSIQTLTKIKRKVRLAAGLDSENALSNEAMERGWQCLRLFAERLQDIPPDNIRVVATATLR 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491623424  91 TATNVDVFLEKANQILGQPIEVISGEEEAATIYKGVAHTSGGSGRRLVVDIGGASTELIIGEGFEAKALTSLKMGCVTWL 170
Cdd:cd24117   81 LATNADVFIAKAQEILGHPVQVISGEEEARLIYQGVAHTSGGAGNRLVVDIGGASTELIIGTGAQTTSLFSLSMGCVTWL 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491623424 171 ENFFKDRQLNARNFEAAIEGAKQTIKPILEQYTDLGWDVCVGASGTVQALQEIMLAQGMDEVITHSKLKRLQKQAMLADH 250
Cdd:cd24117  161 ERYFADRNLSAENFEAAIKAAREVLRPVADELRYHGWQVCVGASGTVQALQEIMVAQGMDERITLEKLQQLKQQAIHCGK 240
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|
gi 491623424 251 LEELDIEGLTLERALVFPSGLSILIAIFELLEIDAMTLAGGALREGLVYE 300
Cdd:cd24117  241 LEELEIDGLTLERALVFPSGLAILIAIFEELEIKCMTLAGGALREGLVYG 290
GppA COG0248
Exopolyphosphatase/pppGpp-phosphohydrolase [Nucleotide transport and metabolism, Signal ...
6-311 1.40e-114

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


Pssm-ID: 440018 [Multi-domain]  Cd Length: 314  Bit Score: 340.62  E-value: 1.40e-114
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491623424   6 SSPLYAAIDLGSNSFHMLVVRHI-DGSVQTMAKIKRKVRLAAGLDEHNSLSMEAMQRGWDCLSLFAERLQDIPTQNIRIV 84
Cdd:COG0248    1 APMRLAAIDIGSNSVRLLIAEVDeGGSFRILDREKEPVRLGEGLDATGRLSEEAIERALAALKRFAELLREYGVERVRAV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491623424  85 GTATLRTATNVDVFLEKANQILGQPIEVISGEEEAATIYKGVAHT-SGGSGRRLVVDIGGASTELIIGEGFEAKALTSLK 163
Cdd:COG0248   81 ATSALREAKNGDEFLDRVKEETGLPIEVISGEEEARLIYLGVLSGlPLSDGRGLVVDIGGGSTELILGDGGEILFSESLP 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491623424 164 MGCVTWLENFFKDRQLNARNFEAAIEGAKQTIKPILEQYTDLGWDVCVGASGTVQALQEIMLAQG------MDEVITHSK 237
Cdd:COG0248  161 LGAVRLTERFFPDDPPTAEEFAAAREYIREELEPLAKELRKGGPDTLVGTGGTIRTLARLLLALGrydekvHGYTLTREE 240
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 491623424 238 LKRLQKQAMLADHLEELDIEGLTLERALVFPSGLSILIAIFELLEIDAMTLAGGALREGLVYEMVDELRQNDIR 311
Cdd:COG0248  241 LEELIERLLSLTLEERAKLPGLSPDRADVILAGAAILEALMEALGIEEIVVSDRGLREGLLYDLLGRDGKKDDR 314
exo_poly_only TIGR03706
exopolyphosphatase; It appears that a single enzyme may act as both exopolyphosphatase (Ppx) ...
9-303 4.62e-99

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: 300.23  E-value: 4.62e-99
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491623424    9 LYAAIDLGSNSFHMLVVRHIDGSVQTMAKIKRKVRLAAGLDEHNSLSMEAMQRGWDCLSLFAERLQDIPTQNIRIVGTAT 88
Cdd:TIGR03706   1 PIAAIDIGSNSVRLVIARGVEGSLQVLFNEKEMVRLGEGLDSTGRLSEEAIERALEALKRFAELLRGFPVDEVRAVATAA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491623424   89 LRTATNVDVFLEKANQILGQPIEVISGEEEAATIYKGVAHTSGGSGrRLVVDIGGASTELIIGEGFEAKALTSLKMGCVT 168
Cdd:TIGR03706  81 LRDAKNGPEFLKEAEAILGLPIEVISGEEEARLIYLGVAHTLPIAD-GLVVDIGGGSTELILGKDGEPGEGVSLPLGCVR 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491623424  169 WLENFFKDRQLNARNFEAAIEGAKQTIKPIlEQYTDLGWDVCVGASGTVQALQEIMLAQ------GMDE-VITHSKLKRL 241
Cdd:TIGR03706 160 LTEQFFPDGPISKKSLKQARKAAREELASL-KWLKKGGWRPLYGVGGTWRALARLHMAQrgyplhGLHGyEITAEGLLEL 238
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 491623424  242 QKQAMLADHLEELDIEGLTLERALVFPSGLSILIAIFELLEIDAMTLAGGALREGLVYEMVD 303
Cdd:TIGR03706 239 LEELIKLSREERLKLPGLSKDRADILPGGAAILEELFRALGIEQIIFSSGGLREGVLYELLG 300
Ppx-GppA pfam02541
Ppx/GppA phosphatase family; This family consists of the N-terminal region of ...
23-301 3.75e-95

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: 289.61  E-value: 3.75e-95
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491623424   23 LVVRHIDGSVQTMAKIKRKVRLAAGLDEHNSLSMEAMQRGWDCLSLFAERLQDIPTQNIRIVGTATLRTATNVDVFLEKA 102
Cdd:pfam02541   1 VIARIVAGHLQIVAREKRKVRLAEGLNSTGRLNEEAIERTISALKEFAEILQGFGVENIRAVATSALRDAVNADEFLARV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491623424  103 NQILGQPIEVISGEEEAATIYKGVAHTSGGSGRRLVVDIGGASTELIIGEGFEAKALTSLKMGCVTWLENFFKDRQLNAR 182
Cdd:pfam02541  81 KKETGLPVEIISGEEEARLIYLGVVSTLGSKGRGLVIDIGGGSTELVLGENKKVRKLISLPMGCVRLTERFFHDDPLTKE 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491623424  183 NFEAAIEGAKQTIKPILEQY-TDLGWDVCVGASGTVQALQEIMLAQG-MDEVITHSKLKRLQKQAMLADHLEELDIEGLT 260
Cdd:pfam02541 161 EVARARDAVRKELEEPKDEVrIGGGWIRALGTSGTISALAPLMALHGiMGYEITAEELEELIEKLSQITREDRLELAGVS 240
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 491623424  261 LERALVFPSGLSILIAIFELLEIDAMTLAGGALREGLVYEM 301
Cdd:pfam02541 241 DERADVIVAGALILSAVFEALSIEAMIISDGGLREGVLYSL 281
 
Name Accession Description Interval E-value
PRK11031 PRK11031
guanosine-5'-triphosphate,3'-diphosphate diphosphatase;
3-494 0e+00

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


Pssm-ID: 236826 [Multi-domain]  Cd Length: 496  Bit Score: 903.95  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491623424   3 QAGSSPLYAAIDLGSNSFHMLVVRHIDGSVQTMAKIKRKVRLAAGLDEHNSLSMEAMQRGWDCLSLFAERLQDIPTQNIR 82
Cdd:PRK11031   1 MLSSSSLYAAIDLGSNSFHMLVVREVAGSIQTLARIKRKVRLAAGLDSDNALSNEAMERGWQCLRLFAERLQDIPPSQIR 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491623424  83 IVGTATLRTATNVDVFLEKANQILGQPIEVISGEEEAATIYKGVAHTSGGSGRRLVVDIGGASTELIIGEGFEAKALTSL 162
Cdd:PRK11031  81 VVATATLRLAVNADEFLAKAQEILGCPVQVISGEEEARLIYQGVAHTTGGADQRLVVDIGGASTELVTGTGAQATSLFSL 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491623424 163 KMGCVTWLENFFKDRQLNARNFEAAIEGAKQTIKPILEQYTDLGWDVCVGASGTVQALQEIMLAQGMDEVITHSKLKRLQ 242
Cdd:PRK11031 161 SMGCVTWLERYFKDRNLTQENFDAAEKAAREVLRPVADELREHGWQVCVGASGTVQALQEIMMAQGMDERITLAKLQQLK 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491623424 243 KQAMLADHLEELDIEGLTLERALVFPSGLSILIAIFELLEIDAMTLAGGALREGLVYEMVDELRQNDIRARTICSVQSRY 322
Cdd:PRK11031 241 QRAIQCGRLEELEIEGLTLERALVFPSGLAILIAIFEELNIESMTLAGGALREGLVYGMLHLPVEQDIRSRTLRNIQRRF 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491623424 323 QLDCQYGEQVATLAGKLLEQAGGdEWIAEPQGKVLLETTAKLHEIGLTIDFKKGGEHSAYLLQNLDLPGYTRAQKFFIGE 402
Cdd:PRK11031 321 QIDTEQAQRVAKLADNFLQQVEN-EWHLEPRSRELLISACQLHEIGLSVDFKQAPQHAAYLVRNLDLPGFTPAQKKLLAT 399
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491623424 403 IARRYRE--QLSSLPEQHAISGTSAKRVLRLLRLAVLLTHRRNPSLEPQVELLAEGDKLTLSIDAKWLEANPLTAAELEI 480
Cdd:PRK11031 400 LLLNQTNpvDLSSLHQQNALPPRVAERLCRLLRLAIIFASRRRDDLLPEVTLQANDELLTLTLPQGWLAQHPLGAEELEQ 479
                        490
                 ....*....|....
gi 491623424 481 ESNRQTDIGWPLTI 494
Cdd:PRK11031 480 ESQWQSYVHWPLEV 493
ASKHA_NBD_EcGppA-like cd24117
nucleotide-binding domain (NBD) of Escherichia coli guanosine pentaphosphate phosphohydrolase ...
11-300 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: 542.80  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491623424  11 AAIDLGSNSFHMLVVRHIDGSVQTMAKIKRKVRLAAGLDEHNSLSMEAMQRGWDCLSLFAERLQDIPTQNIRIVGTATLR 90
Cdd:cd24117    1 AAIDLGSNSFHMLVVREVAGSIQTLTKIKRKVRLAAGLDSENALSNEAMERGWQCLRLFAERLQDIPPDNIRVVATATLR 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491623424  91 TATNVDVFLEKANQILGQPIEVISGEEEAATIYKGVAHTSGGSGRRLVVDIGGASTELIIGEGFEAKALTSLKMGCVTWL 170
Cdd:cd24117   81 LATNADVFIAKAQEILGHPVQVISGEEEARLIYQGVAHTSGGAGNRLVVDIGGASTELIIGTGAQTTSLFSLSMGCVTWL 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491623424 171 ENFFKDRQLNARNFEAAIEGAKQTIKPILEQYTDLGWDVCVGASGTVQALQEIMLAQGMDEVITHSKLKRLQKQAMLADH 250
Cdd:cd24117  161 ERYFADRNLSAENFEAAIKAAREVLRPVADELRYHGWQVCVGASGTVQALQEIMVAQGMDERITLEKLQQLKQQAIHCGK 240
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|
gi 491623424 251 LEELDIEGLTLERALVFPSGLSILIAIFELLEIDAMTLAGGALREGLVYE 300
Cdd:cd24117  241 LEELEIDGLTLERALVFPSGLAILIAIFEELEIKCMTLAGGALREGLVYG 290
ASKHA_NBD_EcPPX-GppA-like cd24053
nucleotide-binding domain (NBD) of Escherichia coli exopolyphosphatase (EcPPX), guanosine ...
11-300 1.79e-131

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: 382.65  E-value: 1.79e-131
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491623424  11 AAIDLGSNSFHMLVVRHIDGSVQTMAKIKRKVRLAAGLDEHNSLSMEAMQRGWDCLSLFAERLQDIPTQNIRIVGTATLR 90
Cdd:cd24053    1 AAVDLGSNSFHLLIARVDDGRLRVVDRLKERVRLAAGLDADGRLSPEAIERALECLARFGERLAGFPPDRVRVVGTNTLR 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491623424  91 TATNVDVFLEKANQILGQPIEVISGEEEAATIYKGVAHT-SGGSGRRLVVDIGGASTELIIGEGFEAKALTSLKMGCVTW 169
Cdd:cd24053   81 VARNAQQFLARAESALGHPIEVISGEEEARLIYLGVAHTlPDDSGRRLVIDIGGGSTELIIGEGFEPEFLESLPLGCVSY 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491623424 170 LENFFKDRQLNARNFEAAIEGAKQTIKPILEQYTDLGWDVCVGASGTVQALQEIMLAQGMDE-VITHSKLKRLQKQAMLA 248
Cdd:cd24053  161 TKRFFPDGEITAEAFQAAVAAARQELEPIAARYKALGWDQAVGSSGTIKAIARVLEALGWGGgGITREGLEKLREELLRA 240
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|..
gi 491623424 249 DHLEELDIEGLTLERALVFPSGLSILIAIFELLEIDAMTLAGGALREGLVYE 300
Cdd:cd24053  241 GSVARLDLPGLSPDRRAVFAGGLAILLALFEELGIDQLTVSDGALREGVLYD 292
PRK10854 PRK10854
exopolyphosphatase; Provisional
10-494 3.33e-128

exopolyphosphatase; Provisional


Pssm-ID: 182781 [Multi-domain]  Cd Length: 513  Bit Score: 382.54  E-value: 3.33e-128
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491623424  10 YAAIDLGSNSFHMLVVRHIDGSVQTMAKIKRKVRLAAGLDEHNSLSMEAMQRGWDCLSLFAERLQDIPTQNIRIVGTATL 89
Cdd:PRK10854  13 FAAVDLGSNSFHMVIARVVDGAMQIIGRLKQRVHLADGLDSDNMLSEEAMERGLNCLSLFAERLQGFSPANVCIVGTHTL 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491623424  90 RTATNVDVFLEKANQILGQPIEVISGEEEAATIYKGVAHTSGGSGRRLVVDIGGASTELIIGEGFEAKALTSLKMGCVTW 169
Cdd:PRK10854  93 RQALNATDFLKRAEKVIPYPIEIISGNEEARLIFMGVEHTQPEKGRKLVIDIGGGSTELVIGENFEPILVESRRMGCVSF 172
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491623424 170 LENFFKDRQLNARNFEAAIEGAKQTIKPILEQYTDLGWDVCVGASGTVQALQEIMLAQG-MDEVITHSKLKRLQKQAMLA 248
Cdd:PRK10854 173 AQLYFPGGVISKENFQRARLAAAQKLETLAWQYRIQGWNVALGASGTIKAAHEVLVEMGeKDGLITPERLEMLVKEVLKH 252
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491623424 249 DHLEELDIEGLTLERALVFPSGLSILIAIFELLEIDAMTLAGGALREGLVYEMVDELRQNDIRARTICSVQSRYQLDCQY 328
Cdd:PRK10854 253 KNFAALSLPGLSEERKTVFVPGLAILCGVFDALAIRELRLSDGALREGVLYEMEGRFRHQDIRSRTAKSLANHYNIDREQ 332
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491623424 329 GEQVATLAGKLLEQ-AGGDEWIAEPQGKVLLETTAKLHEIGLTIDFKKGGEHSAYLLQNLDLPGYTRAQKFFIGEIARRY 407
Cdd:PRK10854 333 ARRVLETTMQLYEQwREQNPKLAHPQLEALLKWAAMLHEVGLNINHSGLHRHSAYILQNTDLPGFNQEQQLMLATLVRYH 412
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491623424 408 RE--QLSSLPEQHAISGTSAKRVLRLLRLAVLLTHRRNPSLEPQ-VELLAEGDKLTLSIDAKWLEANPLTAAELEIESNR 484
Cdd:PRK10854 413 RKaiKLDDLPRFTLFKKKQYLPLIQLLRLGVLLNNQRQATTTPPtLRLITDDSHWTLRFPHDWFSQNALVLLDLEKEQEY 492
                        490
                 ....*....|.
gi 491623424 485 QTDI-GWPLTI 494
Cdd:PRK10854 493 WEDVtGWRLKI 503
ASKHA_NBD_EcPPX-like cd24116
nucleotide-binding domain (NBD) of Escherichia coli exopolyphosphatase (EcPPX) and similar ...
11-306 1.61e-122

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: 360.22  E-value: 1.61e-122
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491623424  11 AAIDLGSNSFHMLVVRHIDGSVQTMAKIKRKVRLAAGLDEHNSLSMEAMQRGWDCLSLFAERLQDIPTQNIRIVGTATLR 90
Cdd:cd24116    3 AAIDLGSNSFHMVVARVVDGALQIISRLKQRVHLADGLDEDNVLSEEAMTRGLNCLALFAERLQGFEPESVCIVGTHTLR 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491623424  91 TATNVDVFLEKANQILGQPIEVISGEEEAATIYKGVAHTSGGSGRRLVVDIGGASTELIIGEGFEAKALTSLKMGCVTWL 170
Cdd:cd24116   83 QARNATDFLKRAEKVLPYPIEIISGNEEARLIYLGVAHTQPEKGRKLVIDIGGGSTELVIGEGFEPLLVESRQMGCVSFA 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491623424 171 ENFFKDRQLNARNFEAAIEGAKQTIKPILEQYTDLGWDVCVGASGTVQALQEIMLAQGM-DEVITHSKLKRLQKQAMLAD 249
Cdd:cd24116  163 QRYFAGGVISKENFQRARMAAQQKLETLAWQYRKQGWQVAFGSSGTIKAAHEVLIEMGEkDGIITPERLEKLIKEVLEAD 242
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 491623424 250 HLEELDIEGLTLERALVFPSGLSILIAIFELLEIDAMTLAGGALREGLVYEMVDELR 306
Cdd:cd24116  243 HFDSLSLPGLSEERKPVFVPGLAILCGVFDALAIRELRLSDGALREGVLYEMEDRFR 299
GppA COG0248
Exopolyphosphatase/pppGpp-phosphohydrolase [Nucleotide transport and metabolism, Signal ...
6-311 1.40e-114

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


Pssm-ID: 440018 [Multi-domain]  Cd Length: 314  Bit Score: 340.62  E-value: 1.40e-114
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491623424   6 SSPLYAAIDLGSNSFHMLVVRHI-DGSVQTMAKIKRKVRLAAGLDEHNSLSMEAMQRGWDCLSLFAERLQDIPTQNIRIV 84
Cdd:COG0248    1 APMRLAAIDIGSNSVRLLIAEVDeGGSFRILDREKEPVRLGEGLDATGRLSEEAIERALAALKRFAELLREYGVERVRAV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491623424  85 GTATLRTATNVDVFLEKANQILGQPIEVISGEEEAATIYKGVAHT-SGGSGRRLVVDIGGASTELIIGEGFEAKALTSLK 163
Cdd:COG0248   81 ATSALREAKNGDEFLDRVKEETGLPIEVISGEEEARLIYLGVLSGlPLSDGRGLVVDIGGGSTELILGDGGEILFSESLP 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491623424 164 MGCVTWLENFFKDRQLNARNFEAAIEGAKQTIKPILEQYTDLGWDVCVGASGTVQALQEIMLAQG------MDEVITHSK 237
Cdd:COG0248  161 LGAVRLTERFFPDDPPTAEEFAAAREYIREELEPLAKELRKGGPDTLVGTGGTIRTLARLLLALGrydekvHGYTLTREE 240
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 491623424 238 LKRLQKQAMLADHLEELDIEGLTLERALVFPSGLSILIAIFELLEIDAMTLAGGALREGLVYEMVDELRQNDIR 311
Cdd:COG0248  241 LEELIERLLSLTLEERAKLPGLSPDRADVILAGAAILEALMEALGIEEIVVSDRGLREGLLYDLLGRDGKKDDR 314
exo_poly_only TIGR03706
exopolyphosphatase; It appears that a single enzyme may act as both exopolyphosphatase (Ppx) ...
9-303 4.62e-99

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: 300.23  E-value: 4.62e-99
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491623424    9 LYAAIDLGSNSFHMLVVRHIDGSVQTMAKIKRKVRLAAGLDEHNSLSMEAMQRGWDCLSLFAERLQDIPTQNIRIVGTAT 88
Cdd:TIGR03706   1 PIAAIDIGSNSVRLVIARGVEGSLQVLFNEKEMVRLGEGLDSTGRLSEEAIERALEALKRFAELLRGFPVDEVRAVATAA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491623424   89 LRTATNVDVFLEKANQILGQPIEVISGEEEAATIYKGVAHTSGGSGrRLVVDIGGASTELIIGEGFEAKALTSLKMGCVT 168
Cdd:TIGR03706  81 LRDAKNGPEFLKEAEAILGLPIEVISGEEEARLIYLGVAHTLPIAD-GLVVDIGGGSTELILGKDGEPGEGVSLPLGCVR 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491623424  169 WLENFFKDRQLNARNFEAAIEGAKQTIKPIlEQYTDLGWDVCVGASGTVQALQEIMLAQ------GMDE-VITHSKLKRL 241
Cdd:TIGR03706 160 LTEQFFPDGPISKKSLKQARKAAREELASL-KWLKKGGWRPLYGVGGTWRALARLHMAQrgyplhGLHGyEITAEGLLEL 238
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 491623424  242 QKQAMLADHLEELDIEGLTLERALVFPSGLSILIAIFELLEIDAMTLAGGALREGLVYEMVD 303
Cdd:TIGR03706 239 LEELIKLSREERLKLPGLSKDRADILPGGAAILEELFRALGIEQIIFSSGGLREGVLYELLG 300
Ppx-GppA pfam02541
Ppx/GppA phosphatase family; This family consists of the N-terminal region of ...
23-301 3.75e-95

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: 289.61  E-value: 3.75e-95
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491623424   23 LVVRHIDGSVQTMAKIKRKVRLAAGLDEHNSLSMEAMQRGWDCLSLFAERLQDIPTQNIRIVGTATLRTATNVDVFLEKA 102
Cdd:pfam02541   1 VIARIVAGHLQIVAREKRKVRLAEGLNSTGRLNEEAIERTISALKEFAEILQGFGVENIRAVATSALRDAVNADEFLARV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491623424  103 NQILGQPIEVISGEEEAATIYKGVAHTSGGSGRRLVVDIGGASTELIIGEGFEAKALTSLKMGCVTWLENFFKDRQLNAR 182
Cdd:pfam02541  81 KKETGLPVEIISGEEEARLIYLGVVSTLGSKGRGLVIDIGGGSTELVLGENKKVRKLISLPMGCVRLTERFFHDDPLTKE 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491623424  183 NFEAAIEGAKQTIKPILEQY-TDLGWDVCVGASGTVQALQEIMLAQG-MDEVITHSKLKRLQKQAMLADHLEELDIEGLT 260
Cdd:pfam02541 161 EVARARDAVRKELEEPKDEVrIGGGWIRALGTSGTISALAPLMALHGiMGYEITAEELEELIEKLSQITREDRLELAGVS 240
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 491623424  261 LERALVFPSGLSILIAIFELLEIDAMTLAGGALREGLVYEM 301
Cdd:pfam02541 241 DERADVIVAGALILSAVFEALSIEAMIISDGGLREGVLYSL 281
ASKHA_NBD_AaPPX-GppA_MtPPX2-like cd24054
nucleotide-binding domain (NBD) of Aquifex aeolicus PPX/GppA, Mycobacterium tuberculosis PPX2, ...
10-300 1.37e-65

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: 213.88  E-value: 1.37e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491623424  10 YAAIDLGSNSFHMLVVRHIDGSVQTMAKIKRKVRLAAGLDEHNSLSMEAMQRGWDCLSLFAERLQDIPTQNIRIVGTATL 89
Cdd:cd24054    1 IAAIDIGTNSVRLLIAEVDGGGLRVLLDERRITRLGEGLDETGRLSPEAIERTLEALKEFKKIAREYGVEKIRAVATSAL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491623424  90 RTATNVDVFLEKANQILGQPIEVISGEEEAATIYKGVAHTSG-GSGRRLVVDIGGASTELIIGEGFEAKALTSLKMGCVT 168
Cdd:cd24054   81 RDAKNRDEFLERVKEETGLEIEIISGEEEARLSFLGALSGLPlPDGPILVIDIGGGSTELILGKGGGILFSVSLPLGAVR 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491623424 169 WLENFFKDRQLNARNFEAAIEGAKQTIKPILEQYTDlgwDVCVGASGTVQALqeIMLAQGMD----EVITHSKLKRlQKQ 244
Cdd:cd24054  161 LTERFLKSDPPSEEELEALREAIRELLEELLLPPKP---DRLVGVGGTATTL--AAIDLGLEeydpEKIHGYVLSL-EEL 234
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 491623424 245 AMLADHLEELDIE------GLTLERALVFPSGLSILIAIFELLEIDAMTLAGGALREGLVYE 300
Cdd:cd24054  235 EELIDRLASMSLEerrklpGLEPGRADIILAGALILLEILEYLGADELTVSDRGLREGLLLE 296
ASKHA_NBD_PPX_GppA cd24006
nucleotide-binding domain (NBD) of the exopolyphosphatase/guanosine pentaphosphate ...
11-300 1.57e-65

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: 213.55  E-value: 1.57e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491623424  11 AAIDLGSNSFHMLVVR-HIDGSVQTMAKIKRKVRLAAGLDEHNSLSMEAMQRGWDCLSLFAERLQDIPTQNIRIVGTATL 89
Cdd:cd24006    1 AAIDIGSNSIRLLIAEvDPDGSFRILERLREPVRLGEDVFTTGRISEEAIERAVEALRRFKKLADEYGVKRIRAVATSAV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491623424  90 RTATNVDVFLEKANQILGQPIEVISGEEEAATIYKGVAHT-SGGSGRRLVVDIGGASTELIIGEGFEAKALTSLKMGCVT 168
Cdd:cd24006   81 REASNGDEFLERIKRETGIDVEIISGEEEARLIYLAVRSGlPLGDGNALIVDIGGGSTELTLGDNGEILFSESLPLGAVR 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491623424 169 WLENFFKDRQLNARNFEaAIEGAKQTIKPILEQYTDLGWDVCVGASGTVQALQEIMLAQGMDEVITHSKLKRLQKqamLA 248
Cdd:cd24006  161 LTERFLKDDPPSELLEE-YLRSFVRSVLRPLPKRRKIKFDVAIGSGGTILALAAMALARKGKPHGYEISREELKA---LY 236
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 491623424 249 DHLEELDIE------GLTLERALVFPSGLSILIAIFELLEIDAMTLAGGALREGLVYE 300
Cdd:cd24006  237 DELLRLSLEerrkkyGLSPDRADVIVPAALILLELLELLGAEEIIVPDVGLRDGLLLD 294
ASKHA_NBD_HpPPX-GppA-like cd24052
nucleotide-binding domain (NBD) of Helicobacter pylori exopolyphosphatase/guanosine ...
10-302 1.54e-48

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: 169.20  E-value: 1.54e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491623424  10 YAAIDLGSNSFHMLVVRHIDGSVQTMAKIKRKVRLAAGLDEHNSLSMEAMQRGWDCLSLFAERLQDIPTQNIRIVGTATL 89
Cdd:cd24052    1 IAIIDIGSNSIRLVIYEIEGGSFRLLFNEKETVGLGEYLDEDGKLSEEGIERAIKALKRFKKICEALGVDEIIAFATAAL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491623424  90 RTATNVDVFLEKANQILGQPIEVISGEEEAATIYKGVAHT----SGgsgrrLVVDIGGASTELIIGEGFEAKALTSLKMG 165
Cdd:cd24052   81 RNAKNGEEFLERIKKETGIDIRVLSGEEEAYYGFLGVLNSlplaDG-----LVVDIGGGSTELVLFKNGKIKESISLPLG 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491623424 166 CVTWLENFFKDRQLNarnfEAAIEGAKQTIKpilEQYTDLGWD--------VCVGasGTVQALQEIM-------LAQGMD 230
Cdd:cd24052  156 SLRLYERFVSGILPT----EKELKKIRKFIK---KELKKLPWLkekkglplYGVG--GTIRALAKLHmelknypLDILHG 226
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 491623424 231 EVITHSKLKRLQKQaMLADHLEEL-DIEGLTLERALVFPSGLSILIAIFELLEIDAMTLAGGALREGLVYEMV 302
Cdd:cd24052  227 YTISAEELDELLKK-LKKLDKEERkKILGLSPDRADTIPPGALILKELLKYFGAKEIIVSGYGLREGYLYEKL 298
ASKHA_NBD_ChPPX-like cd24055
nucleotide-binding domain (NBD) of Cytophaga hutchinsonii exopolyphosphatase (ChPPX) and ...
11-300 4.20e-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: 162.73  E-value: 4.20e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491623424  11 AAIDLGSNSFHMLVVRHIDGSVQTMAKIKRKVRLAAGLDEHNSLSMEAMQRGWDCLSLFAERLQDIPTQNIRIVGTATLR 90
Cdd:cd24055    2 AVIDLGTNTFNLLIAEVDDGSFEILYREKVPVKLGKGGINIGIITDDAFERALDALKSFKQIAKQYGVDEIVAVGTSALR 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491623424  91 TATNVDVFLEKANQILGQPIEVISGEEEAATIYKGVAHT-SGGSGRRLVVDIGGASTELIIGEGFEAKALTSLKMGcVTW 169
Cdd:cd24055   82 SAENGQEFIEKIKEELGIDIEIISGEREAELIYKGVRQAvPLTDEPALIMDIGGGSVEFILANNEQILWKKSFPIG-VAR 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491623424 170 LENFFKDRQLNARNFEAAIEG-AKQTIKPILEQYTDLGWDVCVGASGTVQALQEIMLAQ-----GMDEVITHSKLKRLQK 243
Cdd:cd24055  161 LLEKFHPNDPISPEDIERLEAfLDEELADLFEALDQYKPTVLIGSSGSFDTLAEMIEANkgrtpPAGQSSYEISLEEFEA 240
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 491623424 244 --QAMLADHLEE-LDIEGLTLERA-LVFPSGLSILIaIFELLEIDAMTLAGGALREGLVYE 300
Cdd:cd24055  241 lyQRLLTSTLEErLAIPGMIPMRAdMIVVAAILIQH-VLEKFGIPEIVVSPYALKEGLLFE 300
ASKHA_NBD_MtPPX2-like cd24119
nucleotide-binding domain (NBD) of Mycobacterium tuberculosis exopolyphosphatase 2 (MtPPX2) ...
11-298 2.18e-43

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: 155.50  E-value: 2.18e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491623424  11 AAIDLGSNSFHMLVVRHIDGSVQTMAKIKRKVRLAAGLDEHNSLSMEAMQRGWDCLSLFAERLQDIPTQNIRIVGTATLR 90
Cdd:cd24119    2 AAIDIGTNSVRLLVADVDEGGLREVVRRTRITRLGEGVDATGRLSPEAIERTLAALAEYAALIRELGVERVRVVATSASR 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491623424  91 TATNVDVFLEKANQILGQPIEVISGEEEAATIYKGVAHTSGGSGRRLVVDIGGASTELIIGEGFEAKALTSLKMGCVTWL 170
Cdd:cd24119   82 DASNRDDFLDRLESVLGVRPEVISGEEEARLSFLGATSGLPAPGPVLVVDIGGGSTELVLGRAGEVEAAISLDIGSVRLT 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491623424 171 ENFFKDRQLNARNFEAAIEGAKQTIKPILEQYTDLGWDVCVGASGTVQALqeIMLAQGMD----EVITHSKLKRLQKQAm 246
Cdd:cd24119  162 ERFLHSDPPTAEELEAARADVDAQLDEALDVVSLERATRLVGVAGTVTTL--AALALGLPeydpERVHGYRLSLDQVEA- 238
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 491623424 247 LADHLEELDIE------GLTLERALVFPSGLSILIAIFELLEIDAMTLAGGALREGLV 298
Cdd:cd24119  239 VLRRLSAMTLEeraalpGLQPGRADVIVAGAVILSEVLRRLGIDEVVVSEHDILDGIA 296
ASKHA_NBD_MtPPX1-like cd24056
nucleotide-binding domain (NBD) of Mycobacterium tuberculosis exopolyphosphatase 1 (MtPPX1) ...
11-302 5.97e-41

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: 148.91  E-value: 5.97e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491623424  11 AAIDLGSNSFHMLVVR-HIDGSVQTMAKIKRKVRLAAGLDEHNSLSMEAMQRgwdcLSLFAERLQDIPTQN----IRIVG 85
Cdd:cd24056    3 AALDVGSNTFHLLVADvEGDGRLEPVADEKVMLRLGEDVARTGEIGPEAIDR----AAEAVRRFVELARRLgaeeLLAVA 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491623424  86 TATLRTATNVDVFLEKANQILGQPIEVISGEEEAATIYKGVAHTSG-GSGRRLVVDIGGASTELIIGEGFEAKALTSLKM 164
Cdd:cd24056   79 TSALREAENGPEVLDRVEAETGVPVRVLSGEEEARLTFLGARAALGwSSGPLLVLDLGGGSLELAVGVDGRPEWAASLPL 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491623424 165 GcVTWL-ENFFKDRQLNARNFEAAIEGAKQTIKPILEQYTDLGWDVCVGASGTVQALQEIMLA-QGMDEVITHSKLKRLQ 242
Cdd:cd24056  159 G-SGRLtARFLSSDPPSPEEVRALRAAVRAELAPALDRVRAGEPRRAVATGGTARALARLAGAaRSPVGPLNQRSLTRED 237
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 491623424 243 KQAMLA-----DHLEELDIEGLTLERALVFPSGLSILIAIFELLEIDAMTLAGGALREGLVYEMV 302
Cdd:cd24056  238 LRELRRrlaslSAAERAELPGIDPRRADLLPAGALVLEALLDALGLEELVVSEWGLREGVILDEL 302
ASKHA_NBD_AroB-like cd24120
nucleotide-binding domain (NBD) of Fusobacterium nucleatum bifunctional 3-dehydroquinate ...
11-300 3.99e-36

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: 135.52  E-value: 3.99e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491623424  11 AAIDLGSNSFHMLVVRHIDGSVQTMAKIKRKVRLAAGLDEHNSLSMEAMQRGWDCLSLFAERLQDIPTQNIRIVGTATLR 90
Cdd:cd24120    2 AAIDIGTNSCRLLIAEVEEGNVNPLFKKLETTRLGENVNKTGVLGKEAIERTVEVLKEYKRIADKYGVKKIIAFATSAVR 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491623424  91 TATNVDVFLEKANQILGQPIEVISGEEEAATIYKGVAH-TSGGSGRRLVVDIGGASTELIIGEGFEAKALTSLKMGCVTW 169
Cdd:cd24120   82 DAKNKDEFIELVKRETGIKINVISGEEEAKLSFLGATSgLDSLYEKILVIDIGGGSTEFTLGAPRGIKYVKSFNLGAVRL 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491623424 170 LENFFKDRQLNARNFEAAIEGAKQTIKPILEQYTDLGWDVCVGASGTVQALQEIMLAQGMDEVITHSKLKRLQKQAMLA- 248
Cdd:cd24120  162 TESFFGNDPPDYEELENMRNYVKDKLNETEKFKSLDFKLIGVAGTITTLAAIYLGLEVYDPEKVHGSKLTKEDIEENLKk 241
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 491623424 249 ----DHLEELDIEGLTLERALVFPSGLSILIAIFELLEIDAMTLAGGALREGLVYE 300
Cdd:cd24120  242 lislDLEERKKIPGLEPERADVIIAGTLILLEIMEILGKDFIIVSEADILEGIILT 297
ASKHA_NBD_AaPPX-GppA-like cd24118
nucleotide-binding domain (NBD) of Aquifex aeolicus exopolyphosphatase/guanosine ...
11-300 3.68e-34

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: 130.27  E-value: 3.68e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491623424  11 AAIDLGSNSFHMLVVRHIDGSVQTMAKIKRKVRLAAGLDEHNSLSMEAMQRGWDCLSLFAERLQDIPTQNIRIVGTATLR 90
Cdd:cd24118    2 ASIDIGSYSTRLTIADIEDGKLKILLEEGRITALGTGLKETGRLSEDRIEETLKVLKEYKKLIDEFGVERIKAVGTEAIR 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491623424  91 TATNVDVFLEKANQILGQPIEVISGEEEAATIYKGVAHTSGGSGRRLVVDIGGASTELIIGEGFEAKALTSLKMGCVTWL 170
Cdd:cd24118   82 RAKNREEFLERVKEEVGLDLEVISPEEEGEYAFLAVAYSLKPKGEVCVVDQGGGSTEFVYGKGEKIEFLKSLPFGIVNLT 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491623424 171 ENFFKDRQLNARNFEAAIEGAKQTIKPIleqytDLGWDVCVGASGTVQALqeIMLAQGMD----EVITHSKLKRLQKQAM 246
Cdd:cd24118  162 EEFFKSDPPTEEELESLFNFLEKEISKI-----KKPVDTVVGLGGTITTL--AALEYNIYpydpQKVHGKKLTYGRIKKW 234
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 491623424 247 LaDHLEELDIEG----LTLE--RALVFPSGLSILIAIFELLEIDAMTLAGGALREGLVYE 300
Cdd:cd24118  235 F-DTLSSMPSEErkkiFQIEdrRAEVIIAGIAIFLKTMELFEKRSITVSDWGLLEGLLVE 293
 
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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