|
Name |
Accession |
Description |
Interval |
E-value |
| PRK10854 |
PRK10854 |
exopolyphosphatase; Provisional |
1-506 |
0e+00 |
|
exopolyphosphatase; Provisional
Pssm-ID: 182781 [Multi-domain] Cd Length: 513 Bit Score: 1016.58 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506350846 1 MPLIPTSPRPQEIAAVDLGSNSFHMVIARVVNGALQVLGRLKQRVHLADGLDQHHRLSEESMARGLACLALFAERLQGFP 80
Cdd:PRK10854 1 MPIHDKSPRPQEFAAVDLGSNSFHMVIARVVDGAMQIIGRLKQRVHLADGLDSDNMLSEEAMERGLNCLSLFAERLQGFS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506350846 81 AENVCIVGTHTLRQANNAQEFLKRAAKVIPYPIEIISGHEEARLIFMGVAHTQPEKGRKLVIDIGGGSTEMVIGEDFDPI 160
Cdd:PRK10854 81 PANVCIVGTHTLRQALNATDFLKRAEKVIPYPIEIISGNEEARLIFMGVEHTQPEKGRKLVIDIGGGSTELVIGENFEPI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506350846 161 LVESRRMGCVSFAQQFFADGVITATGFQRARLAAAQKLENMAWQYRIQGWNAALGASGSIKAAYEVLVAMGEKDGLLTPA 240
Cdd:PRK10854 161 LVESRRMGCVSFAQLYFPGGVISKENFQRARLAAAQKLETLAWQYRIQGWNVALGASGTIKAAHEVLVEMGEKDGLITPE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506350846 241 RLAMLCDEALRYSHVDRLRLPGLSEERRQVFVPGLAILCGVFDALAIKQLRLSDGALREGVLYEMEGRFRHQDIRSRTAR 320
Cdd:PRK10854 241 RLEMLVKEVLKHKNFAALSLPGLSEERKTVFVPGLAILCGVFDALAIRELRLSDGALREGVLYEMEGRFRHQDIRSRTAK 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506350846 321 SLADHYNIDREQAQRVQTCAQQLYAQWMAQNSRLVHPQLEALLNWASALHEVGLSINHSGMQRHSAYILQNTNLPGFTQE 400
Cdd:PRK10854 321 SLANHYNIDREQARRVLETTMQLYEQWREQNPKLAHPQLEALLKWAAMLHEVGLNINHSGLHRHSAYILQNTDLPGFNQE 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506350846 401 QQLMLATLVRCQRKALRLEELPRFTLFKKKQYLPLIQILRLATLLNNQRQSTTPPDTLQLETDGFQWVLRFPPRYLRQNS 480
Cdd:PRK10854 401 QQLMLATLVRYHRKAIKLDDLPRFTLFKKKQYLPLIQLLRLGVLLNNQRQATTTPPTLRLITDDSHWTLRFPHDWFSQNA 480
|
490 500
....*....|....*....|....*.
gi 506350846 481 LVQLDVEKEQEYWRNVDGWSLVIETQ 506
Cdd:PRK10854 481 LVLLDLEKEQEYWEDVTGWRLKIEEE 506
|
|
| ASKHA_NBD_EcPPX-like |
cd24116 |
nucleotide-binding domain (NBD) of Escherichia coli exopolyphosphatase (EcPPX) and similar ... |
12-310 |
0e+00 |
|
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: 540.50 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506350846 12 EIAAVDLGSNSFHMVIARVVNGALQVLGRLKQRVHLADGLDQHHRLSEESMARGLACLALFAERLQGFPAENVCIVGTHT 91
Cdd:cd24116 1 EIAAIDLGSNSFHMVVARVVDGALQIISRLKQRVHLADGLDEDNVLSEEAMTRGLNCLALFAERLQGFEPESVCIVGTHT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506350846 92 LRQANNAQEFLKRAAKVIPYPIEIISGHEEARLIFMGVAHTQPEKGRKLVIDIGGGSTEMVIGEDFDPILVESRRMGCVS 171
Cdd:cd24116 81 LRQARNATDFLKRAEKVLPYPIEIISGNEEARLIYLGVAHTQPEKGRKLVIDIGGGSTELVIGEGFEPLLVESRQMGCVS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506350846 172 FAQQFFADGVITATGFQRARLAAAQKLENMAWQYRIQGWNAALGASGSIKAAYEVLVAMGEKDGLLTPARLAMLCDEALR 251
Cdd:cd24116 161 FAQRYFAGGVISKENFQRARMAAQQKLETLAWQYRKQGWQVAFGSSGTIKAAHEVLIEMGEKDGIITPERLEKLIKEVLE 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 506350846 252 YSHVDRLRLPGLSEERRQVFVPGLAILCGVFDALAIKQLRLSDGALREGVLYEMEGRFR 310
Cdd:cd24116 241 ADHFDSLSLPGLSEERKPVFVPGLAILCGVFDALAIRELRLSDGALREGVLYEMEDRFR 299
|
|
| exo_poly_only |
TIGR03706 |
exopolyphosphatase; It appears that a single enzyme may act as both exopolyphosphatase (Ppx) ... |
12-307 |
1.45e-126 |
|
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: 371.11 E-value: 1.45e-126
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506350846 12 EIAAVDLGSNSFHMVIARVVNGALQVLGRLKQRVHLADGLDQHHRLSEESMARGLACLALFAERLQGFPAENVCIVGTHT 91
Cdd:TIGR03706 1 PIAAIDIGSNSVRLVIARGVEGSLQVLFNEKEMVRLGEGLDSTGRLSEEAIERALEALKRFAELLRGFPVDEVRAVATAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506350846 92 LRQANNAQEFLKRAAKVIPYPIEIISGHEEARLIFMGVAHTQPEKGRkLVIDIGGGSTEMVIGEDFDPILVESRRMGCVS 171
Cdd:TIGR03706 81 LRDAKNGPEFLKEAEAILGLPIEVISGEEEARLIYLGVAHTLPIADG-LVVDIGGGSTELILGKDGEPGEGVSLPLGCVR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506350846 172 FAQQFFADGVITATGFQRARLAAAQKLENMAWqYRIQGWNAALGASGSIKAAYEVLVAM------GEKDGLLTPARLAML 245
Cdd:TIGR03706 160 LTEQFFPDGPISKKSLKQARKAAREELASLKW-LKKGGWRPLYGVGGTWRALARLHMAQrgyplhGLHGYEITAEGLLEL 238
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 506350846 246 CDEALRYSHVDRLRLPGLSEERRQVFVPGLAILCGVFDALAIKQLRLSDGALREGVLYEMEG 307
Cdd:TIGR03706 239 LEELIKLSREERLKLPGLSKDRADILPGGAAILEELFRALGIEQIIFSSGGLREGVLYELLG 300
|
|
| GppA |
COG0248 |
Exopolyphosphatase/pppGpp-phosphohydrolase [Nucleotide transport and metabolism, Signal ... |
9-315 |
4.07e-124 |
|
Exopolyphosphatase/pppGpp-phosphohydrolase [Nucleotide transport and metabolism, Signal transduction mechanisms];
Pssm-ID: 440018 [Multi-domain] Cd Length: 314 Bit Score: 365.28 E-value: 4.07e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506350846 9 RPQEIAAVDLGSNSFHMVIARVV-NGALQVLGRLKQRVHLADGLDQHHRLSEESMARGLACLALFAERLQGFPAENVCIV 87
Cdd:COG0248 1 APMRLAAIDIGSNSVRLLIAEVDeGGSFRILDREKEPVRLGEGLDATGRLSEEAIERALAALKRFAELLREYGVERVRAV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506350846 88 GTHTLRQANNAQEFLKRAAKVIPYPIEIISGHEEARLIFMGVAHTQP-EKGRKLVIDIGGGSTEMVIGEDFDPILVESRR 166
Cdd:COG0248 81 ATSALREAKNGDEFLDRVKEETGLPIEVISGEEEARLIYLGVLSGLPlSDGRGLVVDIGGGSTELILGDGGEILFSESLP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506350846 167 MGCVSFAQQFFADGVITATGFQRARLAAAQKLENMAWQYRIQGWNAALGASGSIKAAYEVLVAMGEKDGL-----LTPAR 241
Cdd:COG0248 161 LGAVRLTERFFPDDPPTAEEFAAAREYIREELEPLAKELRKGGPDTLVGTGGTIRTLARLLLALGRYDEKvhgytLTREE 240
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 506350846 242 LAMLCDEALRYSHVDRLRLPGLSEERRQVFVPGLAILCGVFDALAIKQLRLSDGALREGVLYEMEGRFRHQDIR 315
Cdd:COG0248 241 LEELIERLLSLTLEERAKLPGLSPDRADVILAGAAILEALMEALGIEEIVVSDRGLREGLLYDLLGRDGKKDDR 314
|
|
| Ppx-GppA |
pfam02541 |
Ppx/GppA phosphatase family; This family consists of the N-terminal region of ... |
26-309 |
2.45e-119 |
|
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: 352.01 E-value: 2.45e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506350846 26 VIARVVNGALQVLGRLKQRVHLADGLDQHHRLSEESMARGLACLALFAERLQGFPAENVCIVGTHTLRQANNAQEFLKRA 105
Cdd:pfam02541 1 VIARIVAGHLQIVAREKRKVRLAEGLNSTGRLNEEAIERTISALKEFAEILQGFGVENIRAVATSALRDAVNADEFLARV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506350846 106 AKVIPYPIEIISGHEEARLIFMGVAHTQPEKGRKLVIDIGGGSTEMVIGEDFDPILVESRRMGCVSFAQQFFADGVITAT 185
Cdd:pfam02541 81 KKETGLPVEIISGEEEARLIYLGVVSTLGSKGRGLVIDIGGGSTELVLGENKKVRKLISLPMGCVRLTERFFHDDPLTKE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506350846 186 GFQRARLAAAQKLENMAWQYRIQG-WNAALGASGSIKAAYEVLVAMGEKDGLLTPARLAMLCDEALRYSHVDRLRLPGLS 264
Cdd:pfam02541 161 EVARARDAVRKELEEPKDEVRIGGgWIRALGTSGTISALAPLMALHGIMGYEITAEELEELIEKLSQITREDRLELAGVS 240
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 506350846 265 EERRQVFVPGLAILCGVFDALAIKQLRLSDGALREGVLYEMEGRF 309
Cdd:pfam02541 241 DERADVIVAGALILSAVFEALSIEAMIISDGGLREGVLYSLLLKH 285
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PRK10854 |
PRK10854 |
exopolyphosphatase; Provisional |
1-506 |
0e+00 |
|
exopolyphosphatase; Provisional
Pssm-ID: 182781 [Multi-domain] Cd Length: 513 Bit Score: 1016.58 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506350846 1 MPLIPTSPRPQEIAAVDLGSNSFHMVIARVVNGALQVLGRLKQRVHLADGLDQHHRLSEESMARGLACLALFAERLQGFP 80
Cdd:PRK10854 1 MPIHDKSPRPQEFAAVDLGSNSFHMVIARVVDGAMQIIGRLKQRVHLADGLDSDNMLSEEAMERGLNCLSLFAERLQGFS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506350846 81 AENVCIVGTHTLRQANNAQEFLKRAAKVIPYPIEIISGHEEARLIFMGVAHTQPEKGRKLVIDIGGGSTEMVIGEDFDPI 160
Cdd:PRK10854 81 PANVCIVGTHTLRQALNATDFLKRAEKVIPYPIEIISGNEEARLIFMGVEHTQPEKGRKLVIDIGGGSTELVIGENFEPI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506350846 161 LVESRRMGCVSFAQQFFADGVITATGFQRARLAAAQKLENMAWQYRIQGWNAALGASGSIKAAYEVLVAMGEKDGLLTPA 240
Cdd:PRK10854 161 LVESRRMGCVSFAQLYFPGGVISKENFQRARLAAAQKLETLAWQYRIQGWNVALGASGTIKAAHEVLVEMGEKDGLITPE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506350846 241 RLAMLCDEALRYSHVDRLRLPGLSEERRQVFVPGLAILCGVFDALAIKQLRLSDGALREGVLYEMEGRFRHQDIRSRTAR 320
Cdd:PRK10854 241 RLEMLVKEVLKHKNFAALSLPGLSEERKTVFVPGLAILCGVFDALAIRELRLSDGALREGVLYEMEGRFRHQDIRSRTAK 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506350846 321 SLADHYNIDREQAQRVQTCAQQLYAQWMAQNSRLVHPQLEALLNWASALHEVGLSINHSGMQRHSAYILQNTNLPGFTQE 400
Cdd:PRK10854 321 SLANHYNIDREQARRVLETTMQLYEQWREQNPKLAHPQLEALLKWAAMLHEVGLNINHSGLHRHSAYILQNTDLPGFNQE 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506350846 401 QQLMLATLVRCQRKALRLEELPRFTLFKKKQYLPLIQILRLATLLNNQRQSTTPPDTLQLETDGFQWVLRFPPRYLRQNS 480
Cdd:PRK10854 401 QQLMLATLVRYHRKAIKLDDLPRFTLFKKKQYLPLIQLLRLGVLLNNQRQATTTPPTLRLITDDSHWTLRFPHDWFSQNA 480
|
490 500
....*....|....*....|....*.
gi 506350846 481 LVQLDVEKEQEYWRNVDGWSLVIETQ 506
Cdd:PRK10854 481 LVLLDLEKEQEYWEDVTGWRLKIEEE 506
|
|
| ASKHA_NBD_EcPPX-like |
cd24116 |
nucleotide-binding domain (NBD) of Escherichia coli exopolyphosphatase (EcPPX) and similar ... |
12-310 |
0e+00 |
|
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: 540.50 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506350846 12 EIAAVDLGSNSFHMVIARVVNGALQVLGRLKQRVHLADGLDQHHRLSEESMARGLACLALFAERLQGFPAENVCIVGTHT 91
Cdd:cd24116 1 EIAAIDLGSNSFHMVVARVVDGALQIISRLKQRVHLADGLDEDNVLSEEAMTRGLNCLALFAERLQGFEPESVCIVGTHT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506350846 92 LRQANNAQEFLKRAAKVIPYPIEIISGHEEARLIFMGVAHTQPEKGRKLVIDIGGGSTEMVIGEDFDPILVESRRMGCVS 171
Cdd:cd24116 81 LRQARNATDFLKRAEKVLPYPIEIISGNEEARLIYLGVAHTQPEKGRKLVIDIGGGSTELVIGEGFEPLLVESRQMGCVS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506350846 172 FAQQFFADGVITATGFQRARLAAAQKLENMAWQYRIQGWNAALGASGSIKAAYEVLVAMGEKDGLLTPARLAMLCDEALR 251
Cdd:cd24116 161 FAQRYFAGGVISKENFQRARMAAQQKLETLAWQYRKQGWQVAFGSSGTIKAAHEVLIEMGEKDGIITPERLEKLIKEVLE 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 506350846 252 YSHVDRLRLPGLSEERRQVFVPGLAILCGVFDALAIKQLRLSDGALREGVLYEMEGRFR 310
Cdd:cd24116 241 ADHFDSLSLPGLSEERKPVFVPGLAILCGVFDALAIRELRLSDGALREGVLYEMEDRFR 299
|
|
| PRK11031 |
PRK11031 |
guanosine-5'-triphosphate,3'-diphosphate diphosphatase; |
14-506 |
2.83e-157 |
|
guanosine-5'-triphosphate,3'-diphosphate diphosphatase;
Pssm-ID: 236826 [Multi-domain] Cd Length: 496 Bit Score: 456.73 E-value: 2.83e-157
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506350846 14 AAVDLGSNSFHMVIARVVNGALQVLGRLKQRVHLADGLDQHHRLSEESMARGLACLALFAERLQGFPAENVCIVGTHTLR 93
Cdd:PRK11031 9 AAIDLGSNSFHMLVVREVAGSIQTLARIKRKVRLAAGLDSDNALSNEAMERGWQCLRLFAERLQDIPPSQIRVVATATLR 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506350846 94 QANNAQEFLKRAAKVIPYPIEIISGHEEARLIFMGVAHTQPEKGRKLVIDIGGGSTEMVIGEDFDPILVESRRMGCVSFA 173
Cdd:PRK11031 89 LAVNADEFLAKAQEILGCPVQVISGEEEARLIYQGVAHTTGGADQRLVVDIGGASTELVTGTGAQATSLFSLSMGCVTWL 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506350846 174 QQFFADGVITATGFQRARLAAAQKLENMAWQYRIQGWNAALGASGSIKAAYEVLVAMGeKDGLLTPARLAMLCDEALRYS 253
Cdd:PRK11031 169 ERYFKDRNLTQENFDAAEKAAREVLRPVADELREHGWQVCVGASGTVQALQEIMMAQG-MDERITLAKLQQLKQRAIQCG 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506350846 254 HVDRLRLPGLSEERRQVFVPGLAILCGVFDALAIKQLRLSDGALREGVLYEMEGRFRHQDIRSRTARSLADHYNIDREQA 333
Cdd:PRK11031 248 RLEELEIEGLTLERALVFPSGLAILIAIFEELNIESMTLAGGALREGLVYGMLHLPVEQDIRSRTLRNIQRRFQIDTEQA 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506350846 334 QRVQTCAQQLYAQwmAQNSRLVHPQLEALLNWASALHEVGLSINHSGMQRHSAYILQNTNLPGFTQEQQLMLATLVRCQR 413
Cdd:PRK11031 328 QRVAKLADNFLQQ--VENEWHLEPRSRELLISACQLHEIGLSVDFKQAPQHAAYLVRNLDLPGFTPAQKKLLATLLLNQT 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506350846 414 KALRLEELPRFTLFKKKQYLPLIQILRLATLLNNQRQSTTPPdTLQLETDGFQWVLRFPPRYLRQNSLVQLDVEKEQEyW 493
Cdd:PRK11031 406 NPVDLSSLHQQNALPPRVAERLCRLLRLAIIFASRRRDDLLP-EVTLQANDELLTLTLPQGWLAQHPLGAEELEQESQ-W 483
|
490
....*....|...
gi 506350846 494 RNVDGWSLVIETQ 506
Cdd:PRK11031 484 QSYVHWPLEVEEL 496
|
|
| ASKHA_NBD_EcPPX-GppA-like |
cd24053 |
nucleotide-binding domain (NBD) of Escherichia coli exopolyphosphatase (EcPPX), guanosine ... |
14-304 |
2.26e-147 |
|
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: 423.48 E-value: 2.26e-147
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506350846 14 AAVDLGSNSFHMVIARVVNGALQVLGRLKQRVHLADGLDQHHRLSEESMARGLACLALFAERLQGFPAENVCIVGTHTLR 93
Cdd:cd24053 1 AAVDLGSNSFHLLIARVDDGRLRVVDRLKERVRLAAGLDADGRLSPEAIERALECLARFGERLAGFPPDRVRVVGTNTLR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506350846 94 QANNAQEFLKRAAKVIPYPIEIISGHEEARLIFMGVAHTQPEK-GRKLVIDIGGGSTEMVIGEDFDPILVESRRMGCVSF 172
Cdd:cd24053 81 VARNAQQFLARAESALGHPIEVISGEEEARLIYLGVAHTLPDDsGRRLVIDIGGGSTELIIGEGFEPEFLESLPLGCVSY 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506350846 173 AQQFFADGVITATGFQRARLAAAQKLENMAWQYRIQGWNAALGASGSIKAAYEVLVAMGEKDGLLTPARLAMLCDEALRY 252
Cdd:cd24053 161 TKRFFPDGEITAEAFQAAVAAARQELEPIAARYKALGWDQAVGSSGTIKAIARVLEALGWGGGGITREGLEKLREELLRA 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 506350846 253 SHVDRLRLPGLSEERRQVFVPGLAILCGVFDALAIKQLRLSDGALREGVLYE 304
Cdd:cd24053 241 GSVARLDLPGLSPDRRAVFAGGLAILLALFEELGIDQLTVSDGALREGVLYD 292
|
|
| exo_poly_only |
TIGR03706 |
exopolyphosphatase; It appears that a single enzyme may act as both exopolyphosphatase (Ppx) ... |
12-307 |
1.45e-126 |
|
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: 371.11 E-value: 1.45e-126
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506350846 12 EIAAVDLGSNSFHMVIARVVNGALQVLGRLKQRVHLADGLDQHHRLSEESMARGLACLALFAERLQGFPAENVCIVGTHT 91
Cdd:TIGR03706 1 PIAAIDIGSNSVRLVIARGVEGSLQVLFNEKEMVRLGEGLDSTGRLSEEAIERALEALKRFAELLRGFPVDEVRAVATAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506350846 92 LRQANNAQEFLKRAAKVIPYPIEIISGHEEARLIFMGVAHTQPEKGRkLVIDIGGGSTEMVIGEDFDPILVESRRMGCVS 171
Cdd:TIGR03706 81 LRDAKNGPEFLKEAEAILGLPIEVISGEEEARLIYLGVAHTLPIADG-LVVDIGGGSTELILGKDGEPGEGVSLPLGCVR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506350846 172 FAQQFFADGVITATGFQRARLAAAQKLENMAWqYRIQGWNAALGASGSIKAAYEVLVAM------GEKDGLLTPARLAML 245
Cdd:TIGR03706 160 LTEQFFPDGPISKKSLKQARKAAREELASLKW-LKKGGWRPLYGVGGTWRALARLHMAQrgyplhGLHGYEITAEGLLEL 238
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 506350846 246 CDEALRYSHVDRLRLPGLSEERRQVFVPGLAILCGVFDALAIKQLRLSDGALREGVLYEMEG 307
Cdd:TIGR03706 239 LEELIKLSREERLKLPGLSKDRADILPGGAAILEELFRALGIEQIIFSSGGLREGVLYELLG 300
|
|
| GppA |
COG0248 |
Exopolyphosphatase/pppGpp-phosphohydrolase [Nucleotide transport and metabolism, Signal ... |
9-315 |
4.07e-124 |
|
Exopolyphosphatase/pppGpp-phosphohydrolase [Nucleotide transport and metabolism, Signal transduction mechanisms];
Pssm-ID: 440018 [Multi-domain] Cd Length: 314 Bit Score: 365.28 E-value: 4.07e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506350846 9 RPQEIAAVDLGSNSFHMVIARVV-NGALQVLGRLKQRVHLADGLDQHHRLSEESMARGLACLALFAERLQGFPAENVCIV 87
Cdd:COG0248 1 APMRLAAIDIGSNSVRLLIAEVDeGGSFRILDREKEPVRLGEGLDATGRLSEEAIERALAALKRFAELLREYGVERVRAV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506350846 88 GTHTLRQANNAQEFLKRAAKVIPYPIEIISGHEEARLIFMGVAHTQP-EKGRKLVIDIGGGSTEMVIGEDFDPILVESRR 166
Cdd:COG0248 81 ATSALREAKNGDEFLDRVKEETGLPIEVISGEEEARLIYLGVLSGLPlSDGRGLVVDIGGGSTELILGDGGEILFSESLP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506350846 167 MGCVSFAQQFFADGVITATGFQRARLAAAQKLENMAWQYRIQGWNAALGASGSIKAAYEVLVAMGEKDGL-----LTPAR 241
Cdd:COG0248 161 LGAVRLTERFFPDDPPTAEEFAAAREYIREELEPLAKELRKGGPDTLVGTGGTIRTLARLLLALGRYDEKvhgytLTREE 240
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 506350846 242 LAMLCDEALRYSHVDRLRLPGLSEERRQVFVPGLAILCGVFDALAIKQLRLSDGALREGVLYEMEGRFRHQDIR 315
Cdd:COG0248 241 LEELIERLLSLTLEERAKLPGLSPDRADVILAGAAILEALMEALGIEEIVVSDRGLREGLLYDLLGRDGKKDDR 314
|
|
| Ppx-GppA |
pfam02541 |
Ppx/GppA phosphatase family; This family consists of the N-terminal region of ... |
26-309 |
2.45e-119 |
|
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: 352.01 E-value: 2.45e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506350846 26 VIARVVNGALQVLGRLKQRVHLADGLDQHHRLSEESMARGLACLALFAERLQGFPAENVCIVGTHTLRQANNAQEFLKRA 105
Cdd:pfam02541 1 VIARIVAGHLQIVAREKRKVRLAEGLNSTGRLNEEAIERTISALKEFAEILQGFGVENIRAVATSALRDAVNADEFLARV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506350846 106 AKVIPYPIEIISGHEEARLIFMGVAHTQPEKGRKLVIDIGGGSTEMVIGEDFDPILVESRRMGCVSFAQQFFADGVITAT 185
Cdd:pfam02541 81 KKETGLPVEIISGEEEARLIYLGVVSTLGSKGRGLVIDIGGGSTELVLGENKKVRKLISLPMGCVRLTERFFHDDPLTKE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506350846 186 GFQRARLAAAQKLENMAWQYRIQG-WNAALGASGSIKAAYEVLVAMGEKDGLLTPARLAMLCDEALRYSHVDRLRLPGLS 264
Cdd:pfam02541 161 EVARARDAVRKELEEPKDEVRIGGgWIRALGTSGTISALAPLMALHGIMGYEITAEELEELIEKLSQITREDRLELAGVS 240
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 506350846 265 EERRQVFVPGLAILCGVFDALAIKQLRLSDGALREGVLYEMEGRF 309
Cdd:pfam02541 241 DERADVIVAGALILSAVFEALSIEAMIISDGGLREGVLYSLLLKH 285
|
|
| ASKHA_NBD_EcGppA-like |
cd24117 |
nucleotide-binding domain (NBD) of Escherichia coli guanosine pentaphosphate phosphohydrolase ... |
14-304 |
3.82e-117 |
|
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: 346.73 E-value: 3.82e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506350846 14 AAVDLGSNSFHMVIARVVNGALQVLGRLKQRVHLADGLDQHHRLSEESMARGLACLALFAERLQGFPAENVCIVGTHTLR 93
Cdd:cd24117 1 AAIDLGSNSFHMLVVREVAGSIQTLTKIKRKVRLAAGLDSENALSNEAMERGWQCLRLFAERLQDIPPDNIRVVATATLR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506350846 94 QANNAQEFLKRAAKVIPYPIEIISGHEEARLIFMGVAHTQPEKGRKLVIDIGGGSTEMVIGEDFDPILVESRRMGCVSFA 173
Cdd:cd24117 81 LATNADVFIAKAQEILGHPVQVISGEEEARLIYQGVAHTSGGAGNRLVVDIGGASTELIIGTGAQTTSLFSLSMGCVTWL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506350846 174 QQFFADGVITATGFQRARLAAAQKLENMAWQYRIQGWNAALGASGSIKAAYEVLVAMGeKDGLLTPARLAMLCDEALRYS 253
Cdd:cd24117 161 ERYFADRNLSAENFEAAIKAAREVLRPVADELRYHGWQVCVGASGTVQALQEIMVAQG-MDERITLEKLQQLKQQAIHCG 239
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 506350846 254 HVDRLRLPGLSEERRQVFVPGLAILCGVFDALAIKQLRLSDGALREGVLYE 304
Cdd:cd24117 240 KLEELEIDGLTLERALVFPSGLAILIAIFEELEIKCMTLAGGALREGLVYG 290
|
|
| ASKHA_NBD_PPX_GppA |
cd24006 |
nucleotide-binding domain (NBD) of the exopolyphosphatase/guanosine pentaphosphate ... |
14-304 |
3.85e-81 |
|
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: 254.38 E-value: 3.85e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506350846 14 AAVDLGSNSFHMVIARVV-NGALQVLGRLKQRVHLADGLDQHHRLSEESMARGLACLALFAERLQGFPAENVCIVGTHTL 92
Cdd:cd24006 1 AAIDIGSNSIRLLIAEVDpDGSFRILERLREPVRLGEDVFTTGRISEEAIERAVEALRRFKKLADEYGVKRIRAVATSAV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506350846 93 RQANNAQEFLKRAAKVIPYPIEIISGHEEARLIFMGVAHTQP-EKGRKLVIDIGGGSTEMVIGEDFDPILVESRRMGCVS 171
Cdd:cd24006 81 REASNGDEFLERIKRETGIDVEIISGEEEARLIYLAVRSGLPlGDGNALIVDIGGGSTELTLGDNGEILFSESLPLGAVR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506350846 172 FAQQFFADGVITATGFQRARLAAAQKLENMAWQYRIqGWNAALGASGSIKAAYEVLVAMGEKDGL--LTPARLAMLCDEA 249
Cdd:cd24006 161 LTERFLKDDPPSELLEEYLRSFVRSVLRPLPKRRKI-KFDVAIGSGGTILALAAMALARKGKPHGyeISREELKALYDEL 239
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 506350846 250 LRYSHVDRLRLPGLSEERRQVFVPGLAILCGVFDALAIKQLRLSDGALREGVLYE 304
Cdd:cd24006 240 LRLSLEERRKKYGLSPDRADVIVPAALILLELLELLGAEEIIVPDVGLRDGLLLD 294
|
|
| ASKHA_NBD_AaPPX-GppA_MtPPX2-like |
cd24054 |
nucleotide-binding domain (NBD) of Aquifex aeolicus PPX/GppA, Mycobacterium tuberculosis PPX2, ... |
13-304 |
9.48e-69 |
|
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: 222.35 E-value: 9.48e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506350846 13 IAAVDLGSNSFHMVIARVVNGALQVLGRLKQRVHLADGLDQHHRLSEESMARGLACLALFAERLQGFPAENVCIVGTHTL 92
Cdd:cd24054 1 IAAIDIGTNSVRLLIAEVDGGGLRVLLDERRITRLGEGLDETGRLSPEAIERTLEALKEFKKIAREYGVEKIRAVATSAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506350846 93 RQANNAQEFLKRAAKVIPYPIEIISGHEEARLIFMGVAHTQPE-KGRKLVIDIGGGSTEMVIGEDFDPILVESRRMGCVS 171
Cdd:cd24054 81 RDAKNRDEFLERVKEETGLEIEIISGEEEARLSFLGALSGLPLpDGPILVIDIGGGSTELILGKGGGILFSVSLPLGAVR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506350846 172 FAQQFFADGVITATGFQRARLAAAQKLENMAWQYRIQgwnAALGASGSIKAayevLVAMGEK---------DGL-LTPAR 241
Cdd:cd24054 161 LTERFLKSDPPSEEELEALREAIRELLEELLLPPKPD---RLVGVGGTATT----LAAIDLGleeydpekiHGYvLSLEE 233
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 506350846 242 LAMLCDEALRYSHVDRLRLPGLSEERRQVFVPGLAILCGVFDALAIKQLRLSDGALREGVLYE 304
Cdd:cd24054 234 LEELIDRLASMSLEERRKLPGLEPGRADIILAGALILLEILEYLGADELTVSDRGLREGLLLE 296
|
|
| ASKHA_NBD_HpPPX-GppA-like |
cd24052 |
nucleotide-binding domain (NBD) of Helicobacter pylori exopolyphosphatase/guanosine ... |
13-305 |
1.34e-60 |
|
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: 201.17 E-value: 1.34e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506350846 13 IAAVDLGSNSFHMVIARVVNGALQVLGRLKQRVHLADGLDQHHRLSEESMARGLACLALFAERLQGFPAENVCIVGTHTL 92
Cdd:cd24052 1 IAIIDIGSNSIRLVIYEIEGGSFRLLFNEKETVGLGEYLDEDGKLSEEGIERAIKALKRFKKICEALGVDEIIAFATAAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506350846 93 RQANNAQEFLKRAAKVIPYPIEIISGHEEARLIFMGVAHTQP-EKGrkLVIDIGGGSTEMVIGEDFDPILVESRRMGCVS 171
Cdd:cd24052 81 RNAKNGEEFLERIKKETGIDIRVLSGEEEAYYGFLGVLNSLPlADG--LVVDIGGGSTELVLFKNGKIKESISLPLGSLR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506350846 172 FAQQFFADGVITATGFQRARLAAAQKLENMAWQYRIQGWNA-ALGasGSIKAAYEVLVAMGEKD------GLLTPARLAM 244
Cdd:cd24052 159 LYERFVSGILPTEKELKKIRKFIKKELKKLPWLKEKKGLPLyGVG--GTIRALAKLHMELKNYPldilhgYTISAEELDE 236
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 506350846 245 LCDEALRYSHVDRLRLPGLSEERRQVFVPGLAILCGVFDALAIKQLRLSDGALREGVLYEM 305
Cdd:cd24052 237 LLKKLKKLDKEERKKILGLSPDRADTIPPGALILKELLKYFGAKEIIVSGYGLREGYLYEK 297
|
|
| ASKHA_NBD_MtPPX2-like |
cd24119 |
nucleotide-binding domain (NBD) of Mycobacterium tuberculosis exopolyphosphatase 2 (MtPPX2) ... |
13-302 |
1.14e-50 |
|
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: 175.14 E-value: 1.14e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506350846 13 IAAVDLGSNSFHMVIARVVNGALQVLGRLKQRVHLADGLDQHHRLSEESMARGLACLALFAERLQGFPAENVCIVGTHTL 92
Cdd:cd24119 1 VAAIDIGTNSVRLLVADVDEGGLREVVRRTRITRLGEGVDATGRLSPEAIERTLAALAEYAALIRELGVERVRVVATSAS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506350846 93 RQANNAQEFLKRAAKVIPYPIEIISGHEEARLIFMGVAHTQPEKGRKLVIDIGGGSTEMVIGEDFDPILVESRRMGCVSF 172
Cdd:cd24119 81 RDASNRDDFLDRLESVLGVRPEVISGEEEARLSFLGATSGLPAPGPVLVVDIGGGSTELVLGRAGEVEAAISLDIGSVRL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506350846 173 AQQFFADGVITATGFQRARLAAAQKLENMAWQYRIQGWNAALGASGSIkaayEVLVAMGEkdGL------------LTPA 240
Cdd:cd24119 161 TERFLHSDPPTAEELEAARADVDAQLDEALDVVSLERATRLVGVAGTV----TTLAALAL--GLpeydpervhgyrLSLD 234
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 506350846 241 RLAMLCDEALRYSHVDRLRLPGLSEERRQVFVPGLAILCGVFDALAIKQLRLSDGALREGVL 302
Cdd:cd24119 235 QVEAVLRRLSAMTLEERAALPGLQPGRADVIVAGAVILSEVLRRLGIDEVVVSEHDILDGIA 296
|
|
| ASKHA_NBD_ChPPX-like |
cd24055 |
nucleotide-binding domain (NBD) of Cytophaga hutchinsonii exopolyphosphatase (ChPPX) and ... |
13-304 |
4.71e-50 |
|
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: 173.52 E-value: 4.71e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506350846 13 IAAVDLGSNSFHMVIARVVNGALQVLGRLKQRVHLADGLDQHHRLSEESMARGLACLALFAERLQGFPAENVCIVGTHTL 92
Cdd:cd24055 1 IAVIDLGTNTFNLLIAEVDDGSFEILYREKVPVKLGKGGINIGIITDDAFERALDALKSFKQIAKQYGVDEIVAVGTSAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506350846 93 RQANNAQEFLKRAAKVIPYPIEIISGHEEARLIFMGVAHTQP-EKGRKLVIDIGGGSTEMVIGEDFDPILVESRRMGcVS 171
Cdd:cd24055 81 RSAENGQEFIEKIKEELGIDIEIISGEREAELIYKGVRQAVPlTDEPALIMDIGGGSVEFILANNEQILWKKSFPIG-VA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506350846 172 FAQQFF-------ADGVITATGFQRARLAAaqkLENMAWQYRIQgwnAALGASGSikaaYEVLVAM-----------GEK 233
Cdd:cd24055 160 RLLEKFhpndpisPEDIERLEAFLDEELAD---LFEALDQYKPT---VLIGSSGS----FDTLAEMieankgrtppaGQS 229
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 506350846 234 DGLLTPARLAMLCDEALRYSHVDRLRLPGLSEERRQVFVPGLAILCGVFDALAIKQLRLSDGALREGVLYE 304
Cdd:cd24055 230 SYEISLEEFEALYQRLLTSTLEERLAIPGMIPMRADMIVVAAILIQHVLEKFGIPEIVVSPYALKEGLLFE 300
|
|
| ASKHA_NBD_MtPPX1-like |
cd24056 |
nucleotide-binding domain (NBD) of Mycobacterium tuberculosis exopolyphosphatase 1 (MtPPX1) ... |
14-305 |
2.23e-48 |
|
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: 168.94 E-value: 2.23e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506350846 14 AAVDLGSNSFHMVIARVV-NGALQVLGRLKQRVHLADGLDQHHRLSEESMARGLACLALFAERLQGFPAENVCIVGTHTL 92
Cdd:cd24056 3 AALDVGSNTFHLLVADVEgDGRLEPVADEKVMLRLGEDVARTGEIGPEAIDRAAEAVRRFVELARRLGAEELLAVATSAL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506350846 93 RQANNAQEFLKRAAKVIPYPIEIISGHEEARLIFMGVAH-TQPEKGRKLVIDIGGGSTEMVIGEDFDPILVESRRMGCVS 171
Cdd:cd24056 83 REAENGPEVLDRVEAETGVPVRVLSGEEEARLTFLGARAaLGWSSGPLLVLDLGGGSLELAVGVDGRPEWAASLPLGSGR 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506350846 172 FAQQFFADGVITATGFQRARLAAAQKLENMAWQYRIQGWNAALGASGSIKAAYEVLVAMGEKDGL-----LTPARLAMLC 246
Cdd:cd24056 163 LTARFLSSDPPSPEEVRALRAAVRAELAPALDRVRAGEPRRAVATGGTARALARLAGAARSPVGPlnqrsLTREDLRELR 242
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 506350846 247 DEALRYSHVDRLRLPGLSEERRQVFVPGLAILCGVFDALAIKQLRLSDGALREGVLYEM 305
Cdd:cd24056 243 RRLASLSAAERAELPGIDPRRADLLPAGALVLEALLDALGLEELVVSEWGLREGVILDE 301
|
|
| ASKHA_NBD_AaPPX-GppA-like |
cd24118 |
nucleotide-binding domain (NBD) of Aquifex aeolicus exopolyphosphatase/guanosine ... |
13-304 |
3.90e-39 |
|
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: 144.14 E-value: 3.90e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506350846 13 IAAVDLGSNSFHMVIARVVNGALQVLGRLKQRVHLADGLDQHHRLSEESMARGLACLALFAERLQGFPAENVCIVGTHTL 92
Cdd:cd24118 1 IASIDIGSYSTRLTIADIEDGKLKILLEEGRITALGTGLKETGRLSEDRIEETLKVLKEYKKLIDEFGVERIKAVGTEAI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506350846 93 RQANNAQEFLKRAAKVIPYPIEIISGHEEARLIFMGVAHTQPEKGRKLVIDIGGGSTEMVIGEDFDPILVESRRMGCVSF 172
Cdd:cd24118 81 RRAKNREEFLERVKEEVGLDLEVISPEEEGEYAFLAVAYSLKPKGEVCVVDQGGGSTEFVYGKGEKIEFLKSLPFGIVNL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506350846 173 AQQFFADGVITAtgfqrarlAAAQKLENMAWQYRI---QGWNAALGASGSIKAayevLVAMGEK---------DG-LLTP 239
Cdd:cd24118 161 TEEFFKSDPPTE--------EELESLFNFLEKEISkikKPVDTVVGLGGTITT----LAALEYNiypydpqkvHGkKLTY 228
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 506350846 240 ARLAMLCDEALRYSHVDRLRLPGLSEERRQVFVPGLAILCGVFDALAIKQLRLSDGALREGVLYE 304
Cdd:cd24118 229 GRIKKWFDTLSSMPSEERKKIFQIEDRRAEVIIAGIAIFLKTMELFEKRSITVSDWGLLEGLLVE 293
|
|
| ASKHA_NBD_AroB-like |
cd24120 |
nucleotide-binding domain (NBD) of Fusobacterium nucleatum bifunctional 3-dehydroquinate ... |
13-304 |
2.41e-34 |
|
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: 130.90 E-value: 2.41e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506350846 13 IAAVDLGSNSFHMVIARVVNGALQVLGRLKQRVHLADGLDQHHRLSEESMARGLACLALFAERLQGFPAENVCIVGTHTL 92
Cdd:cd24120 1 KAAIDIGTNSCRLLIAEVEEGNVNPLFKKLETTRLGENVNKTGVLGKEAIERTVEVLKEYKRIADKYGVKKIIAFATSAV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506350846 93 RQANNAQEFLKRAAKVIPYPIEIISGHEEARLIFMGVAH-TQPEKGRKLVIDIGGGSTEMVIGEDFDPILVESRRMGCVS 171
Cdd:cd24120 81 RDAKNKDEFIELVKRETGIKINVISGEEEAKLSFLGATSgLDSLYEKILVIDIGGGSTEFTLGAPRGIKYVKSFNLGAVR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506350846 172 FAQQFFADGVITATGFQRARLAAAQKLENMAWQyrIQGWNAALGASGSIKAAYEVLVAMGEKD------GLLTPARLAML 245
Cdd:cd24120 161 LTESFFGNDPPDYEELENMRNYVKDKLNETEKF--KSLDFKLIGVAGTITTLAAIYLGLEVYDpekvhgSKLTKEDIEEN 238
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 506350846 246 CDEALRYSHVDRLRLPGLSEERRQVFVPGLAILCGVFDALAIKQLRLSDGALREGVLYE 304
Cdd:cd24120 239 LKKLISLDLEERKKIPGLEPERADVIIAGTLILLEIMEILGKDFIIVSEADILEGIILT 297
|
|
| |
