|
Name |
Accession |
Description |
Interval |
E-value |
| PRK10854 |
PRK10854 |
exopolyphosphatase; Provisional |
1-513 |
0e+00 |
|
exopolyphosphatase; Provisional
Pssm-ID: 182781 [Multi-domain] Cd Length: 513 Bit Score: 1083.99 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130427 1 MPIHDKSPRPQEFAAVDLGSNSFHMVIARVVDGAMQIIGRLKQRVHLADGLGPDNMLSEEAMTRGLNCLSLFAERLQGFS 80
Cdd:PRK10854 1 MPIHDKSPRPQEFAAVDLGSNSFHMVIARVVDGAMQIIGRLKQRVHLADGLDSDNMLSEEAMERGLNCLSLFAERLQGFS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130427 81 PASVCIVGTHTLRQALNATDFLKRAEKVIPYPIEIISGNEEARLIFMGVEHTQPEKGRKLVIDIGGGSTELVIGENFEPI 160
Cdd:PRK10854 81 PANVCIVGTHTLRQALNATDFLKRAEKVIPYPIEIISGNEEARLIFMGVEHTQPEKGRKLVIDIGGGSTELVIGENFEPI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130427 161 LVESRRMGCVSFAQLYFPGGVINKENFQRARMAAAQKLETLTWQFRIQGWNVAMGASGTIKAAHEVLMEMGEKDGIITPE 240
Cdd:PRK10854 161 LVESRRMGCVSFAQLYFPGGVISKENFQRARLAAAQKLETLAWQYRIQGWNVALGASGTIKAAHEVLVEMGEKDGLITPE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130427 241 RLEKLVKEVLRHRNFASLSLPGLSEERKTVFVPGLAILCGVFDALAIRELRLSDGALREGVLYEMEGRFRHQDVRSRTAS 320
Cdd:PRK10854 241 RLEMLVKEVLKHKNFAALSLPGLSEERKTVFVPGLAILCGVFDALAIRELRLSDGALREGVLYEMEGRFRHQDIRSRTAK 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130427 321 SLANQYHIDSEQARRVLDTTMQMYEQWREQQPKLAHPQLEALLRWAAMLHEVGLNINHSGLHRHSAYILQNSDLPGFNQE 400
Cdd:PRK10854 321 SLANHYNIDREQARRVLETTMQLYEQWREQNPKLAHPQLEALLKWAAMLHEVGLNINHSGLHRHSAYILQNTDLPGFNQE 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130427 401 QQLMMATLVRYHRKAIKLDDLPRFTLFKKKQFLPLIQLLRLGVLLNNQRQATTTPPTLTLITDDSHWTLRFPHDWFSQNA 480
Cdd:PRK10854 401 QQLMLATLVRYHRKAIKLDDLPRFTLFKKKQYLPLIQLLRLGVLLNNQRQATTTPPTLRLITDDSHWTLRFPHDWFSQNA 480
|
490 500 510
....*....|....*....|....*....|...
gi 16130427 481 LVLLDLEKEQEYWEGVAGWRLKIEEESTPEIAA 513
Cdd:PRK10854 481 LVLLDLEKEQEYWEDVTGWRLKIEEESTPEIAA 513
|
|
| 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: 592.11 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130427 12 EFAAVDLGSNSFHMVIARVVDGAMQIIGRLKQRVHLADGLGPDNMLSEEAMTRGLNCLSLFAERLQGFSPASVCIVGTHT 91
Cdd:cd24116 1 EIAAIDLGSNSFHMVVARVVDGALQIISRLKQRVHLADGLDEDNVLSEEAMTRGLNCLALFAERLQGFEPESVCIVGTHT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130427 92 LRQALNATDFLKRAEKVIPYPIEIISGNEEARLIFMGVEHTQPEKGRKLVIDIGGGSTELVIGENFEPILVESRRMGCVS 171
Cdd:cd24116 81 LRQARNATDFLKRAEKVLPYPIEIISGNEEARLIYLGVAHTQPEKGRKLVIDIGGGSTELVIGEGFEPLLVESRQMGCVS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130427 172 FAQLYFPGGVINKENFQRARMAAAQKLETLTWQFRIQGWNVAMGASGTIKAAHEVLMEMGEKDGIITPERLEKLVKEVLR 251
Cdd:cd24116 161 FAQRYFAGGVISKENFQRARMAAQQKLETLAWQYRKQGWQVAFGSSGTIKAAHEVLIEMGEKDGIITPERLEKLIKEVLE 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 16130427 252 HRNFASLSLPGLSEERKTVFVPGLAILCGVFDALAIRELRLSDGALREGVLYEMEGRFR 310
Cdd:cd24116 241 ADHFDSLSLPGLSEERKPVFVPGLAILCGVFDALAIRELRLSDGALREGVLYEMEDRFR 299
|
|
| Ppx-GppA |
pfam02541 |
Ppx/GppA phosphatase family; This family consists of the N-terminal region of ... |
26-309 |
4.74e-131 |
|
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: 382.06 E-value: 4.74e-131
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130427 26 VIARVVDGAMQIIGRLKQRVHLADGLGPDNMLSEEAMTRGLNCLSLFAERLQGFSPASVCIVGTHTLRQALNATDFLKRA 105
Cdd:pfam02541 1 VIARIVAGHLQIVAREKRKVRLAEGLNSTGRLNEEAIERTISALKEFAEILQGFGVENIRAVATSALRDAVNADEFLARV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130427 106 EKVIPYPIEIISGNEEARLIFMGVEHTQPEKGRKLVIDIGGGSTELVIGENFEPILVESRRMGCVSFAQLYFPGGVINKE 185
Cdd:pfam02541 81 KKETGLPVEIISGEEEARLIYLGVVSTLGSKGRGLVIDIGGGSTELVLGENKKVRKLISLPMGCVRLTERFFHDDPLTKE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130427 186 NFQRARMAAAQKLETLTWQFRIQG-WNVAMGASGTIKAAHEVLMEMGEKDGIITPERLEKLVKEVLRHRNFASLSLPGLS 264
Cdd:pfam02541 161 EVARARDAVRKELEEPKDEVRIGGgWIRALGTSGTISALAPLMALHGIMGYEITAEELEELIEKLSQITREDRLELAGVS 240
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 16130427 265 EERKTVFVPGLAILCGVFDALAIRELRLSDGALREGVLYEMEGRF 309
Cdd:pfam02541 241 DERADVIVAGALILSAVFEALSIEAMIISDGGLREGVLYSLLLKH 285
|
|
| exo_poly_only |
TIGR03706 |
exopolyphosphatase; It appears that a single enzyme may act as both exopolyphosphatase (Ppx) ... |
12-307 |
1.68e-123 |
|
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: 363.40 E-value: 1.68e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130427 12 EFAAVDLGSNSFHMVIARVVDGAMQIIGRLKQRVHLADGLGPDNMLSEEAMTRGLNCLSLFAERLQGFSPASVCIVGTHT 91
Cdd:TIGR03706 1 PIAAIDIGSNSVRLVIARGVEGSLQVLFNEKEMVRLGEGLDSTGRLSEEAIERALEALKRFAELLRGFPVDEVRAVATAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130427 92 LRQALNATDFLKRAEKVIPYPIEIISGNEEARLIFMGVEHTQPEKGRkLVIDIGGGSTELVIGENFEPILVESRRMGCVS 171
Cdd:TIGR03706 81 LRDAKNGPEFLKEAEAILGLPIEVISGEEEARLIYLGVAHTLPIADG-LVVDIGGGSTELILGKDGEPGEGVSLPLGCVR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130427 172 FAQLYFPGGVINKENFQRARMAAAQKLETLTWqFRIQGWNVAMGASGTIKAAHEVLMEM------GEKDGIITPERLEKL 245
Cdd:TIGR03706 160 LTEQFFPDGPISKKSLKQARKAAREELASLKW-LKKGGWRPLYGVGGTWRALARLHMAQrgyplhGLHGYEITAEGLLEL 238
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 16130427 246 VKEVLRHRNFASLSLPGLSEERKTVFVPGLAILCGVFDALAIRELRLSDGALREGVLYEMEG 307
Cdd:TIGR03706 239 LEELIKLSREERLKLPGLSKDRADILPGGAAILEELFRALGIEQIIFSSGGLREGVLYELLG 300
|
|
| GppA |
COG0248 |
Exopolyphosphatase/pppGpp-phosphohydrolase [Nucleotide transport and metabolism, Signal ... |
9-315 |
7.13e-118 |
|
Exopolyphosphatase/pppGpp-phosphohydrolase [Nucleotide transport and metabolism, Signal transduction mechanisms];
Pssm-ID: 440018 [Multi-domain] Cd Length: 314 Bit Score: 349.48 E-value: 7.13e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130427 9 RPQEFAAVDLGSNSFHMVIARVV-DGAMQIIGRLKQRVHLADGLGPDNMLSEEAMTRGLNCLSLFAERLQGFSPASVCIV 87
Cdd:COG0248 1 APMRLAAIDIGSNSVRLLIAEVDeGGSFRILDREKEPVRLGEGLDATGRLSEEAIERALAALKRFAELLREYGVERVRAV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130427 88 GTHTLRQALNATDFLKRAEKVIPYPIEIISGNEEARLIFMGVEHTQP-EKGRKLVIDIGGGSTELVIGENFEPILVESRR 166
Cdd:COG0248 81 ATSALREAKNGDEFLDRVKEETGLPIEVISGEEEARLIYLGVLSGLPlSDGRGLVVDIGGGSTELILGDGGEILFSESLP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130427 167 MGCVSFAQLYFPGGVINKENFQRARMAAAQKLETLTWQFRIQGWNVAMGASGTIKAAHEVLMEMGEKDGI-----ITPER 241
Cdd:COG0248 161 LGAVRLTERFFPDDPPTAEEFAAAREYIREELEPLAKELRKGGPDTLVGTGGTIRTLARLLLALGRYDEKvhgytLTREE 240
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 16130427 242 LEKLVKEVLRHRNFASLSLPGLSEERKTVFVPGLAILCGVFDALAIRELRLSDGALREGVLYEMEGRFRHQDVR 315
Cdd:COG0248 241 LEELIERLLSLTLEERAKLPGLSPDRADVILAGAAILEALMEALGIEEIVVSDRGLREGLLYDLLGRDGKKDDR 314
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PRK10854 |
PRK10854 |
exopolyphosphatase; Provisional |
1-513 |
0e+00 |
|
exopolyphosphatase; Provisional
Pssm-ID: 182781 [Multi-domain] Cd Length: 513 Bit Score: 1083.99 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130427 1 MPIHDKSPRPQEFAAVDLGSNSFHMVIARVVDGAMQIIGRLKQRVHLADGLGPDNMLSEEAMTRGLNCLSLFAERLQGFS 80
Cdd:PRK10854 1 MPIHDKSPRPQEFAAVDLGSNSFHMVIARVVDGAMQIIGRLKQRVHLADGLDSDNMLSEEAMERGLNCLSLFAERLQGFS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130427 81 PASVCIVGTHTLRQALNATDFLKRAEKVIPYPIEIISGNEEARLIFMGVEHTQPEKGRKLVIDIGGGSTELVIGENFEPI 160
Cdd:PRK10854 81 PANVCIVGTHTLRQALNATDFLKRAEKVIPYPIEIISGNEEARLIFMGVEHTQPEKGRKLVIDIGGGSTELVIGENFEPI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130427 161 LVESRRMGCVSFAQLYFPGGVINKENFQRARMAAAQKLETLTWQFRIQGWNVAMGASGTIKAAHEVLMEMGEKDGIITPE 240
Cdd:PRK10854 161 LVESRRMGCVSFAQLYFPGGVISKENFQRARLAAAQKLETLAWQYRIQGWNVALGASGTIKAAHEVLVEMGEKDGLITPE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130427 241 RLEKLVKEVLRHRNFASLSLPGLSEERKTVFVPGLAILCGVFDALAIRELRLSDGALREGVLYEMEGRFRHQDVRSRTAS 320
Cdd:PRK10854 241 RLEMLVKEVLKHKNFAALSLPGLSEERKTVFVPGLAILCGVFDALAIRELRLSDGALREGVLYEMEGRFRHQDIRSRTAK 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130427 321 SLANQYHIDSEQARRVLDTTMQMYEQWREQQPKLAHPQLEALLRWAAMLHEVGLNINHSGLHRHSAYILQNSDLPGFNQE 400
Cdd:PRK10854 321 SLANHYNIDREQARRVLETTMQLYEQWREQNPKLAHPQLEALLKWAAMLHEVGLNINHSGLHRHSAYILQNTDLPGFNQE 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130427 401 QQLMMATLVRYHRKAIKLDDLPRFTLFKKKQFLPLIQLLRLGVLLNNQRQATTTPPTLTLITDDSHWTLRFPHDWFSQNA 480
Cdd:PRK10854 401 QQLMLATLVRYHRKAIKLDDLPRFTLFKKKQYLPLIQLLRLGVLLNNQRQATTTPPTLRLITDDSHWTLRFPHDWFSQNA 480
|
490 500 510
....*....|....*....|....*....|...
gi 16130427 481 LVLLDLEKEQEYWEGVAGWRLKIEEESTPEIAA 513
Cdd:PRK10854 481 LVLLDLEKEQEYWEDVTGWRLKIEEESTPEIAA 513
|
|
| 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: 592.11 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130427 12 EFAAVDLGSNSFHMVIARVVDGAMQIIGRLKQRVHLADGLGPDNMLSEEAMTRGLNCLSLFAERLQGFSPASVCIVGTHT 91
Cdd:cd24116 1 EIAAIDLGSNSFHMVVARVVDGALQIISRLKQRVHLADGLDEDNVLSEEAMTRGLNCLALFAERLQGFEPESVCIVGTHT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130427 92 LRQALNATDFLKRAEKVIPYPIEIISGNEEARLIFMGVEHTQPEKGRKLVIDIGGGSTELVIGENFEPILVESRRMGCVS 171
Cdd:cd24116 81 LRQARNATDFLKRAEKVLPYPIEIISGNEEARLIYLGVAHTQPEKGRKLVIDIGGGSTELVIGEGFEPLLVESRQMGCVS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130427 172 FAQLYFPGGVINKENFQRARMAAAQKLETLTWQFRIQGWNVAMGASGTIKAAHEVLMEMGEKDGIITPERLEKLVKEVLR 251
Cdd:cd24116 161 FAQRYFAGGVISKENFQRARMAAQQKLETLAWQYRKQGWQVAFGSSGTIKAAHEVLIEMGEKDGIITPERLEKLIKEVLE 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 16130427 252 HRNFASLSLPGLSEERKTVFVPGLAILCGVFDALAIRELRLSDGALREGVLYEMEGRFR 310
Cdd:cd24116 241 ADHFDSLSLPGLSEERKPVFVPGLAILCGVFDALAIRELRLSDGALREGVLYEMEDRFR 299
|
|
| ASKHA_NBD_EcPPX-GppA-like |
cd24053 |
nucleotide-binding domain (NBD) of Escherichia coli exopolyphosphatase (EcPPX), guanosine ... |
14-304 |
2.19e-157 |
|
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: 449.29 E-value: 2.19e-157
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130427 14 AAVDLGSNSFHMVIARVVDGAMQIIGRLKQRVHLADGLGPDNMLSEEAMTRGLNCLSLFAERLQGFSPASVCIVGTHTLR 93
Cdd:cd24053 1 AAVDLGSNSFHLLIARVDDGRLRVVDRLKERVRLAAGLDADGRLSPEAIERALECLARFGERLAGFPPDRVRVVGTNTLR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130427 94 QALNATDFLKRAEKVIPYPIEIISGNEEARLIFMGVEHTQPEK-GRKLVIDIGGGSTELVIGENFEPILVESRRMGCVSF 172
Cdd:cd24053 81 VARNAQQFLARAESALGHPIEVISGEEEARLIYLGVAHTLPDDsGRRLVIDIGGGSTELIIGEGFEPEFLESLPLGCVSY 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130427 173 AQLYFPGGVINKENFQRARMAAAQKLETLTWQFRIQGWNVAMGASGTIKAAHEVLMEMGEKDGIITPERLEKLVKEVLRH 252
Cdd:cd24053 161 TKRFFPDGEITAEAFQAAVAAARQELEPIAARYKALGWDQAVGSSGTIKAIARVLEALGWGGGGITREGLEKLREELLRA 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 16130427 253 RNFASLSLPGLSEERKTVFVPGLAILCGVFDALAIRELRLSDGALREGVLYE 304
Cdd:cd24053 241 GSVARLDLPGLSPDRRAVFAGGLAILLALFEELGIDQLTVSDGALREGVLYD 292
|
|
| PRK11031 |
PRK11031 |
guanosine-5'-triphosphate,3'-diphosphate diphosphatase; |
13-505 |
2.61e-153 |
|
guanosine-5'-triphosphate,3'-diphosphate diphosphatase;
Pssm-ID: 236826 [Multi-domain] Cd Length: 496 Bit Score: 446.71 E-value: 2.61e-153
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130427 13 FAAVDLGSNSFHMVIARVVDGAMQIIGRLKQRVHLADGLGPDNMLSEEAMTRGLNCLSLFAERLQGFSPASVCIVGTHTL 92
Cdd:PRK11031 8 YAAIDLGSNSFHMLVVREVAGSIQTLARIKRKVRLAAGLDSDNALSNEAMERGWQCLRLFAERLQDIPPSQIRVVATATL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130427 93 RQALNATDFLKRAEKVIPYPIEIISGNEEARLIFMGVEHTQPEKGRKLVIDIGGGSTELVIGENFEPILVESRRMGCVSF 172
Cdd:PRK11031 88 RLAVNADEFLAKAQEILGCPVQVISGEEEARLIYQGVAHTTGGADQRLVVDIGGASTELVTGTGAQATSLFSLSMGCVTW 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130427 173 AQLYFPGGVINKENFQRARMAAAQKLETLTWQFRIQGWNVAMGASGTIKAAHEVLMEMGeKDGIITPERLEKLVKEVLRH 252
Cdd:PRK11031 168 LERYFKDRNLTQENFDAAEKAAREVLRPVADELREHGWQVCVGASGTVQALQEIMMAQG-MDERITLAKLQQLKQRAIQC 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130427 253 RNFASLSLPGLSEERKTVFVPGLAILCGVFDALAIRELRLSDGALREGVLYEMEGRFRHQDVRSRTASSLANQYHIDSEQ 332
Cdd:PRK11031 247 GRLEELEIEGLTLERALVFPSGLAILIAIFEELNIESMTLAGGALREGLVYGMLHLPVEQDIRSRTLRNIQRRFQIDTEQ 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130427 333 ARRVLDTTMQMYEQWREQQPklAHPQLEALLRWAAMLHEVGLNINHSGLHRHSAYILQNSDLPGFNQEQQLMMATLVRYH 412
Cdd:PRK11031 327 AQRVAKLADNFLQQVENEWH--LEPRSRELLISACQLHEIGLSVDFKQAPQHAAYLVRNLDLPGFTPAQKKLLATLLLNQ 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130427 413 RKAIKLddlprfTLFKKKQFLPLIQ------LLRLGVLLNNQRQATTTPPTLTLITDDShWTLRFPHDWFSQNALVLLDL 486
Cdd:PRK11031 405 TNPVDL------SSLHQQNALPPRVaerlcrLLRLAIIFASRRRDDLLPEVTLQANDEL-LTLTLPQGWLAQHPLGAEEL 477
|
490
....*....|....*....
gi 16130427 487 EKEQEyWEGVAGWRLKIEE 505
Cdd:PRK11031 478 EQESQ-WQSYVHWPLEVEE 495
|
|
| Ppx-GppA |
pfam02541 |
Ppx/GppA phosphatase family; This family consists of the N-terminal region of ... |
26-309 |
4.74e-131 |
|
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: 382.06 E-value: 4.74e-131
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130427 26 VIARVVDGAMQIIGRLKQRVHLADGLGPDNMLSEEAMTRGLNCLSLFAERLQGFSPASVCIVGTHTLRQALNATDFLKRA 105
Cdd:pfam02541 1 VIARIVAGHLQIVAREKRKVRLAEGLNSTGRLNEEAIERTISALKEFAEILQGFGVENIRAVATSALRDAVNADEFLARV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130427 106 EKVIPYPIEIISGNEEARLIFMGVEHTQPEKGRKLVIDIGGGSTELVIGENFEPILVESRRMGCVSFAQLYFPGGVINKE 185
Cdd:pfam02541 81 KKETGLPVEIISGEEEARLIYLGVVSTLGSKGRGLVIDIGGGSTELVLGENKKVRKLISLPMGCVRLTERFFHDDPLTKE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130427 186 NFQRARMAAAQKLETLTWQFRIQG-WNVAMGASGTIKAAHEVLMEMGEKDGIITPERLEKLVKEVLRHRNFASLSLPGLS 264
Cdd:pfam02541 161 EVARARDAVRKELEEPKDEVRIGGgWIRALGTSGTISALAPLMALHGIMGYEITAEELEELIEKLSQITREDRLELAGVS 240
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 16130427 265 EERKTVFVPGLAILCGVFDALAIRELRLSDGALREGVLYEMEGRF 309
Cdd:pfam02541 241 DERADVIVAGALILSAVFEALSIEAMIISDGGLREGVLYSLLLKH 285
|
|
| exo_poly_only |
TIGR03706 |
exopolyphosphatase; It appears that a single enzyme may act as both exopolyphosphatase (Ppx) ... |
12-307 |
1.68e-123 |
|
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: 363.40 E-value: 1.68e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130427 12 EFAAVDLGSNSFHMVIARVVDGAMQIIGRLKQRVHLADGLGPDNMLSEEAMTRGLNCLSLFAERLQGFSPASVCIVGTHT 91
Cdd:TIGR03706 1 PIAAIDIGSNSVRLVIARGVEGSLQVLFNEKEMVRLGEGLDSTGRLSEEAIERALEALKRFAELLRGFPVDEVRAVATAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130427 92 LRQALNATDFLKRAEKVIPYPIEIISGNEEARLIFMGVEHTQPEKGRkLVIDIGGGSTELVIGENFEPILVESRRMGCVS 171
Cdd:TIGR03706 81 LRDAKNGPEFLKEAEAILGLPIEVISGEEEARLIYLGVAHTLPIADG-LVVDIGGGSTELILGKDGEPGEGVSLPLGCVR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130427 172 FAQLYFPGGVINKENFQRARMAAAQKLETLTWqFRIQGWNVAMGASGTIKAAHEVLMEM------GEKDGIITPERLEKL 245
Cdd:TIGR03706 160 LTEQFFPDGPISKKSLKQARKAAREELASLKW-LKKGGWRPLYGVGGTWRALARLHMAQrgyplhGLHGYEITAEGLLEL 238
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 16130427 246 VKEVLRHRNFASLSLPGLSEERKTVFVPGLAILCGVFDALAIRELRLSDGALREGVLYEMEG 307
Cdd:TIGR03706 239 LEELIKLSREERLKLPGLSKDRADILPGGAAILEELFRALGIEQIIFSSGGLREGVLYELLG 300
|
|
| GppA |
COG0248 |
Exopolyphosphatase/pppGpp-phosphohydrolase [Nucleotide transport and metabolism, Signal ... |
9-315 |
7.13e-118 |
|
Exopolyphosphatase/pppGpp-phosphohydrolase [Nucleotide transport and metabolism, Signal transduction mechanisms];
Pssm-ID: 440018 [Multi-domain] Cd Length: 314 Bit Score: 349.48 E-value: 7.13e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130427 9 RPQEFAAVDLGSNSFHMVIARVV-DGAMQIIGRLKQRVHLADGLGPDNMLSEEAMTRGLNCLSLFAERLQGFSPASVCIV 87
Cdd:COG0248 1 APMRLAAIDIGSNSVRLLIAEVDeGGSFRILDREKEPVRLGEGLDATGRLSEEAIERALAALKRFAELLREYGVERVRAV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130427 88 GTHTLRQALNATDFLKRAEKVIPYPIEIISGNEEARLIFMGVEHTQP-EKGRKLVIDIGGGSTELVIGENFEPILVESRR 166
Cdd:COG0248 81 ATSALREAKNGDEFLDRVKEETGLPIEVISGEEEARLIYLGVLSGLPlSDGRGLVVDIGGGSTELILGDGGEILFSESLP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130427 167 MGCVSFAQLYFPGGVINKENFQRARMAAAQKLETLTWQFRIQGWNVAMGASGTIKAAHEVLMEMGEKDGI-----ITPER 241
Cdd:COG0248 161 LGAVRLTERFFPDDPPTAEEFAAAREYIREELEPLAKELRKGGPDTLVGTGGTIRTLARLLLALGRYDEKvhgytLTREE 240
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 16130427 242 LEKLVKEVLRHRNFASLSLPGLSEERKTVFVPGLAILCGVFDALAIRELRLSDGALREGVLYEMEGRFRHQDVR 315
Cdd:COG0248 241 LEELIERLLSLTLEERAKLPGLSPDRADVILAGAAILEALMEALGIEEIVVSDRGLREGLLYDLLGRDGKKDDR 314
|
|
| ASKHA_NBD_EcGppA-like |
cd24117 |
nucleotide-binding domain (NBD) of Escherichia coli guanosine pentaphosphate phosphohydrolase ... |
14-304 |
1.70e-115 |
|
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: 342.49 E-value: 1.70e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130427 14 AAVDLGSNSFHMVIARVVDGAMQIIGRLKQRVHLADGLGPDNMLSEEAMTRGLNCLSLFAERLQGFSPASVCIVGTHTLR 93
Cdd:cd24117 1 AAIDLGSNSFHMLVVREVAGSIQTLTKIKRKVRLAAGLDSENALSNEAMERGWQCLRLFAERLQDIPPDNIRVVATATLR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130427 94 QALNATDFLKRAEKVIPYPIEIISGNEEARLIFMGVEHTQPEKGRKLVIDIGGGSTELVIGENFEPILVESRRMGCVSFA 173
Cdd:cd24117 81 LATNADVFIAKAQEILGHPVQVISGEEEARLIYQGVAHTSGGAGNRLVVDIGGASTELIIGTGAQTTSLFSLSMGCVTWL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130427 174 QLYFPGGVINKENFQRARMAAAQKLETLTWQFRIQGWNVAMGASGTIKAAHEVLMEMGeKDGIITPERLEKLVKEVLRHR 253
Cdd:cd24117 161 ERYFADRNLSAENFEAAIKAAREVLRPVADELRYHGWQVCVGASGTVQALQEIMVAQG-MDERITLEKLQQLKQQAIHCG 239
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 16130427 254 NFASLSLPGLSEERKTVFVPGLAILCGVFDALAIRELRLSDGALREGVLYE 304
Cdd:cd24117 240 KLEELEIDGLTLERALVFPSGLAILIAIFEELEIKCMTLAGGALREGLVYG 290
|
|
| ASKHA_NBD_PPX_GppA |
cd24006 |
nucleotide-binding domain (NBD) of the exopolyphosphatase/guanosine pentaphosphate ... |
14-304 |
1.26e-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: 255.54 E-value: 1.26e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130427 14 AAVDLGSNSFHMVIARVV-DGAMQIIGRLKQRVHLADGLGPDNMLSEEAMTRGLNCLSLFAERLQGFSPASVCIVGTHTL 92
Cdd:cd24006 1 AAIDIGSNSIRLLIAEVDpDGSFRILERLREPVRLGEDVFTTGRISEEAIERAVEALRRFKKLADEYGVKRIRAVATSAV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130427 93 RQALNATDFLKRAEKVIPYPIEIISGNEEARLIFMGVEHTQP-EKGRKLVIDIGGGSTELVIGENFEPILVESRRMGCVS 171
Cdd:cd24006 81 REASNGDEFLERIKRETGIDVEIISGEEEARLIYLAVRSGLPlGDGNALIVDIGGGSTELTLGDNGEILFSESLPLGAVR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130427 172 FAQLYFPGGVINKENFQRARMAAAQKLETLTWQFRIqGWNVAMGASGTIKAAHEVLMEMGEKDGI--ITPERLEKLVKEV 249
Cdd:cd24006 161 LTERFLKDDPPSELLEEYLRSFVRSVLRPLPKRRKI-KFDVAIGSGGTILALAAMALARKGKPHGyeISREELKALYDEL 239
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 16130427 250 LRHRNFASLSLPGLSEERKTVFVPGLAILCGVFDALAIRELRLSDGALREGVLYE 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 |
1.45e-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: 214.27 E-value: 1.45e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130427 13 FAAVDLGSNSFHMVIARVVDGAMQIIGRLKQRVHLADGLGPDNMLSEEAMTRGLNCLSLFAERLQGFSPASVCIVGTHTL 92
Cdd:cd24054 1 IAAIDIGTNSVRLLIAEVDGGGLRVLLDERRITRLGEGLDETGRLSPEAIERTLEALKEFKKIAREYGVEKIRAVATSAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130427 93 RQALNATDFLKRAEKVIPYPIEIISGNEEARLIFMGVEHTQPE-KGRKLVIDIGGGSTELVIGENFEPILVESRRMGCVS 171
Cdd:cd24054 81 RDAKNRDEFLERVKEETGLEIEIISGEEEARLSFLGALSGLPLpDGPILVIDIGGGSTELILGKGGGILFSVSLPLGAVR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130427 172 FAQLYFPGGVINKENFQRARMAAAQKLETLTWQFRIQgwnVAMGASGTIK--AAheVLMEMGEKDG------IITPERLE 243
Cdd:cd24054 161 LTERFLKSDPPSEEELEALREAIRELLEELLLPPKPD---RLVGVGGTATtlAA--IDLGLEEYDPekihgyVLSLEELE 235
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 16130427 244 KLVKEVLRHRNFASLSLPGLSEERKTVFVPGLAILCGVFDALAIRELRLSDGALREGVLYE 304
Cdd:cd24054 236 ELIDRLASMSLEERRKLPGLEPGRADIILAGALILLEILEYLGADELTVSDRGLREGLLLE 296
|
|
| ASKHA_NBD_HpPPX-GppA-like |
cd24052 |
nucleotide-binding domain (NBD) of Helicobacter pylori exopolyphosphatase/guanosine ... |
13-305 |
6.39e-62 |
|
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: 204.64 E-value: 6.39e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130427 13 FAAVDLGSNSFHMVIARVVDGAMQIIGRLKQRVHLADGLGPDNMLSEEAMTRGLNCLSLFAERLQGFSPASVCIVGTHTL 92
Cdd:cd24052 1 IAIIDIGSNSIRLVIYEIEGGSFRLLFNEKETVGLGEYLDEDGKLSEEGIERAIKALKRFKKICEALGVDEIIAFATAAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130427 93 RQALNATDFLKRAEKVIPYPIEIISGNEEARLIFMGVEHTQP-EKGrkLVIDIGGGSTELVIGENFEPILVESRRMGCVS 171
Cdd:cd24052 81 RNAKNGEEFLERIKKETGIDIRVLSGEEEAYYGFLGVLNSLPlADG--LVVDIGGGSTELVLFKNGKIKESISLPLGSLR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130427 172 FAQLYFPGGVINKENFQRARMAAAQKLETLTWQFRIQGWN-VAMGasGTIKAAHEVLMEMGEKD------GIITPERLEK 244
Cdd:cd24052 159 LYERFVSGILPTEKELKKIRKFIKKELKKLPWLKEKKGLPlYGVG--GTIRALAKLHMELKNYPldilhgYTISAEELDE 236
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 16130427 245 LVKEVLRHRNFASLSLPGLSEERKTVFVPGLAILCGVFDALAIRELRLSDGALREGVLYEM 305
Cdd:cd24052 237 LLKKLKKLDKEERKKILGLSPDRADTIPPGALILKELLKYFGAKEIIVSGYGLREGYLYEK 297
|
|
| ASKHA_NBD_ChPPX-like |
cd24055 |
nucleotide-binding domain (NBD) of Cytophaga hutchinsonii exopolyphosphatase (ChPPX) and ... |
14-304 |
5.42e-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: 5.42e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130427 14 AAVDLGSNSFHMVIARVVDGAMQIIGRLKQRVHLADGLGPDNMLSEEAMTRGLNCLSLFAERLQGFSPASVCIVGTHTLR 93
Cdd:cd24055 2 AVIDLGTNTFNLLIAEVDDGSFEILYREKVPVKLGKGGINIGIITDDAFERALDALKSFKQIAKQYGVDEIVAVGTSALR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130427 94 QALNATDFLKRAEKVIPYPIEIISGNEEARLIFMGVEHTQP-EKGRKLVIDIGGGSTELVIGENFEPILVESRRMGCVSF 172
Cdd:cd24055 82 SAENGQEFIEKIKEELGIDIEIISGEREAELIYKGVRQAVPlTDEPALIMDIGGGSVEFILANNEQILWKKSFPIGVARL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130427 173 AQLYFPGGVINKEnfQRARMAA--AQKLETLTWQFRIQGWNVAMGASGT-------IKAAHEVLMEMGEKDGIITPERLE 243
Cdd:cd24055 162 LEKFHPNDPISPE--DIERLEAflDEELADLFEALDQYKPTVLIGSSGSfdtlaemIEANKGRTPPAGQSSYEISLEEFE 239
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 16130427 244 KLVKEVLRhRNFAS-LSLPGLSEERKTVFVPGLAILCGVFDALAIRELRLSDGALREGVLYE 304
Cdd:cd24055 240 ALYQRLLT-STLEErLAIPGMIPMRADMIVVAAILIQHVLEKFGIPEIVVSPYALKEGLLFE 300
|
|
| ASKHA_NBD_MtPPX2-like |
cd24119 |
nucleotide-binding domain (NBD) of Mycobacterium tuberculosis exopolyphosphatase 2 (MtPPX2) ... |
14-302 |
1.66e-44 |
|
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: 158.58 E-value: 1.66e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130427 14 AAVDLGSNSFHMVIARVVDGAMQIIGRLKQRVHLADGLGPDNMLSEEAMTRGLNCLSLFAERLQGFSPASVCIVGTHTLR 93
Cdd:cd24119 2 AAIDIGTNSVRLLVADVDEGGLREVVRRTRITRLGEGVDATGRLSPEAIERTLAALAEYAALIRELGVERVRVVATSASR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130427 94 QALNATDFLKRAEKVIPYPIEIISGNEEARLIFMGVEHTQPEKGRKLVIDIGGGSTELVIGENFEPILVESRRMGCVSFA 173
Cdd:cd24119 82 DASNRDDFLDRLESVLGVRPEVISGEEEARLSFLGATSGLPAPGPVLVVDIGGGSTELVLGRAGEVEAAISLDIGSVRLT 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130427 174 QLYFPGGVINKENFQRARMAAAqklETLTWQFRIQGWNVA---MGASGTIKAAHEVLMEMGEKDgiitPERLEKL----- 245
Cdd:cd24119 162 ERFLHSDPPTAEELEAARADVD---AQLDEALDVVSLERAtrlVGVAGTVTTLAALALGLPEYD----PERVHGYrlsld 234
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 16130427 246 -VKEVLRHRNFASLS----LPGLSEERKTVFVPGLAILCGVFDALAIRELRLSDGALREGVL 302
Cdd:cd24119 235 qVEAVLRRLSAMTLEeraaLPGLQPGRADVIVAGAVILSEVLRRLGIDEVVVSEHDILDGIA 296
|
|
| ASKHA_NBD_MtPPX1-like |
cd24056 |
nucleotide-binding domain (NBD) of Mycobacterium tuberculosis exopolyphosphatase 1 (MtPPX1) ... |
13-305 |
4.30e-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: 149.68 E-value: 4.30e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130427 13 FAAVDLGSNSFHMVIARVV-DGAMQIIGRLKQRVHLADGLGPDNMLSEEAMTRGLNCLSLFAERLQGFSPASVCIVGTHT 91
Cdd:cd24056 2 LAALDVGSNTFHLLVADVEgDGRLEPVADEKVMLRLGEDVARTGEIGPEAIDRAAEAVRRFVELARRLGAEELLAVATSA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130427 92 LRQALNATDFLKRAEKVIPYPIEIISGNEEARLIFMGVEH-TQPEKGRKLVIDIGGGSTELVIGENFEPILVESRRMGCV 170
Cdd:cd24056 82 LREAENGPEVLDRVEAETGVPVRVLSGEEEARLTFLGARAaLGWSSGPLLVLDLGGGSLELAVGVDGRPEWAASLPLGSG 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130427 171 SFAQLYFPGGVINKENFQRARMAAAQKLETLTWQFRIQGWNVAMGASGTIKAAHEVLMEMGEKDG-----IITPERLEKL 245
Cdd:cd24056 162 RLTARFLSSDPPSPEEVRALRAAVRAELAPALDRVRAGEPRRAVATGGTARALARLAGAARSPVGplnqrSLTREDLREL 241
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130427 246 VKEVLRHRNFASLSLPGLSEERKTVFVPGLAILCGVFDALAIRELRLSDGALREGVLYEM 305
Cdd:cd24056 242 RRRLASLSAAERAELPGIDPRRADLLPAGALVLEALLDALGLEELVVSEWGLREGVILDE 301
|
|
| ASKHA_NBD_AroB-like |
cd24120 |
nucleotide-binding domain (NBD) of Fusobacterium nucleatum bifunctional 3-dehydroquinate ... |
14-304 |
9.98e-38 |
|
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: 140.14 E-value: 9.98e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130427 14 AAVDLGSNSFHMVIARVVDGAMQIIGRLKQRVHLADGLGPDNMLSEEAMTRGLNCLSLFAERLQGFSPASVCIVGTHTLR 93
Cdd:cd24120 2 AAIDIGTNSCRLLIAEVEEGNVNPLFKKLETTRLGENVNKTGVLGKEAIERTVEVLKEYKRIADKYGVKKIIAFATSAVR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130427 94 QALNATDFLKRAEKVIPYPIEIISGNEEARLIFMGV-EHTQPEKGRKLVIDIGGGSTELVIGENFEPILVESRRMGCVSF 172
Cdd:cd24120 82 DAKNKDEFIELVKRETGIKINVISGEEEAKLSFLGAtSGLDSLYEKILVIDIGGGSTEFTLGAPRGIKYVKSFNLGAVRL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130427 173 AQLYFPGGVINKENFQRARMAAAQKLETLTWQfrIQGWNVAMGASGTIKAAHEVLMEMGEKDgiitPERLE--KLVKEVL 250
Cdd:cd24120 162 TESFFGNDPPDYEELENMRNYVKDKLNETEKF--KSLDFKLIGVAGTITTLAAIYLGLEVYD----PEKVHgsKLTKEDI 235
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 16130427 251 RH--RNFASLSL------PGLSEERKTVFVPGLAILCGVFDALAIRELRLSDGALREGVLYE 304
Cdd:cd24120 236 EEnlKKLISLDLeerkkiPGLEPERADVIIAGTLILLEIMEILGKDFIIVSEADILEGIILT 297
|
|
| ASKHA_NBD_AaPPX-GppA-like |
cd24118 |
nucleotide-binding domain (NBD) of Aquifex aeolicus exopolyphosphatase/guanosine ... |
14-304 |
2.31e-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: 131.04 E-value: 2.31e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130427 14 AAVDLGSNSFHMVIARVVDGAMQIIGRLKQRVHLADGLGPDNMLSEEAMTRGLNCLSLFAERLQGFSPASVCIVGTHTLR 93
Cdd:cd24118 2 ASIDIGSYSTRLTIADIEDGKLKILLEEGRITALGTGLKETGRLSEDRIEETLKVLKEYKKLIDEFGVERIKAVGTEAIR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130427 94 QALNATDFLKRAEKVIPYPIEIISGNEEARLIFMGVEHTQPEKGRKLVIDIGGGSTELVIGENFEPILVESRRMGCVSFA 173
Cdd:cd24118 82 RAKNREEFLERVKEEVGLDLEVISPEEEGEYAFLAVAYSLKPKGEVCVVDQGGGSTEFVYGKGEKIEFLKSLPFGIVNLT 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130427 174 QLYFPGGVINKE------NFQRARMAAAQKLEtltwqFRIqgwnVAMGASGTIKAAHEVLME---MGEKDG-IITPERLE 243
Cdd:cd24118 162 EEFFKSDPPTEEeleslfNFLEKEISKIKKPV-----DTV----VGLGGTITTLAALEYNIYpydPQKVHGkKLTYGRIK 232
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 16130427 244 KLVKEVLRHRNFASLSLPGLSEERKTVFVPGLAILCGVFDALAIRELRLSDGALREGVLYE 304
Cdd:cd24118 233 KWFDTLSSMPSEERKKIFQIEDRRAEVIIAGIAIFLKTMELFEKRSITVSDWGLLEGLLVE 293
|
|
| |
