|
Name |
Accession |
Description |
Interval |
E-value |
| PRK05253 |
PRK05253 |
sulfate adenylyltransferase subunit CysD; |
22-322 |
0e+00 |
|
sulfate adenylyltransferase subunit CysD;
Pssm-ID: 235375 Cd Length: 301 Bit Score: 645.27 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498361442 22 TRERLTHLQQLEAESIHIIREVAAEFENPVMMYSIGKDSSVMLHLARKAFYPGKIPFPMLHVDTNWKFKEMIKFRDETAK 101
Cdd:PRK05253 2 DQYRLTHLDQLEAESIHILREVAAEFENPVMLYSIGKDSSVMLHLARKAFYPGKLPFPLLHVDTGWKFPEMIEFRDRRAK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498361442 102 KFGLDLIVHKNPDGLAMDINPFVHGSSKHTDIMKTEGLKQALNKYGFDAAFGGARRDEEKSRAKERVYSFRDKSHRWDPK 181
Cdd:PRK05253 82 ELGLELIVHSNPEGIARGINPFRHGSAKHTNAMKTEGLKQALEKYGFDAAFGGARRDEEKSRAKERIFSFRDEFGQWDPK 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498361442 182 NQRPELWRVYNSQVNKGESIRVFPLSNWTELDIWQYIYLENIDIVPLYFAAMRPVVDRGGIKIMVdDDRMPIGPEDEVKQ 261
Cdd:PRK05253 162 NQRPELWNLYNGRINKGEHIRVFPLSNWTELDIWQYIERENIPIVPLYFAHERPVVERDGMLIMV-DDRMPLRPGEVVEE 240
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 498361442 262 ELVRFRTLGCYPLTGAIESNATTLPEIIEEMLITTSSERQGRLIDHDQAGSMEQKKRQGYF 322
Cdd:PRK05253 241 RMVRFRTLGCYPCTGAVESEAATLEEIIAEMLVTRTSERGGRAIDDDQEASMEKRKREGYF 301
|
|
| CysD |
TIGR02039 |
sulfate adenylyltransferase, small subunit; Metabolic assimilation of sulfur from inorganic ... |
29-322 |
0e+00 |
|
sulfate adenylyltransferase, small subunit; Metabolic assimilation of sulfur from inorganic sulfate, requires sulfate activation by coupling to a nucleoside, for the production of high-energy nucleoside phosphosulfates. This pathway appears to be similar in all prokaryotic organisms. Activation is first achieved through sulfation of sulfate with ATP by sulfate adenylyltransferase (ATP sulfurylase) to produce 5'-phosphosulfate (APS), coupled by GTP hydrolysis. Subsequently, APS is phosphorylated by an APS kinase to produce 3'-phosphoadenosine-5'-phosphosulfate (PAPS). In Escherichia coli, ATP sulfurylase is a heterodimer composed of two subunits encoded by cysD and cysN, with APS kinase encoded by cysC. These genes are located in a unidirectionally transcribed gene cluster, and have been shown to be required for the synthesis of sulfur-containing amino acids. Homologous to this E.coli activation pathway are nodPQH gene products found among members of the Rhizobiaceae family. These gene products have been shown to exhibit ATP sulfurase and APS kinase activity, yet are involved in Nod factor sulfation, and sulfation of other macromolecules. [Central intermediary metabolism, Sulfur metabolism]
Pssm-ID: 131094 Cd Length: 294 Bit Score: 558.58 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498361442 29 LQQLEAESIHIIREVAAEFENPVMMYSIGKDSSVMLHLARKAFYPGKIPFPMLHVDTNWKFKEMIKFRDETAKKFGLDLI 108
Cdd:TIGR02039 1 LRALESEAIHIIREVAAEFERPVMLYSIGKDSSVLLHLARKAFYPGPLPFPLLHVDTGWKFREMIAFRDHMVAKYGLRLI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498361442 109 VHKNPDGLAMDINPFVHGSSKHTDIMKTEGLKQALNKYGFDAAFGGARRDEEKSRAKERVYSFRDKSHRWDPKNQRPELW 188
Cdd:TIGR02039 81 VHSNEEGIADGINPFTEGSALHTDIMKTEALRQALDKNQFDAAFGGARRDEEKSRAKERIFSFRNAFHQWDPKKQRPELW 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498361442 189 RVYNSQVNKGESIRVFPLSNWTELDIWQYIYLENIDIVPLYFAAMRPVVDRGGIKIMVDDDRMPIGPEDEVKQELVRFRT 268
Cdd:TIGR02039 161 NLYNGRISKGESVRVFPLSNWTELDIWRYIAAENIPIVPLYFAAKRPVVQRDGMLIMVDDVRMPLAPGEVVKERMVRFRT 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 498361442 269 LGCYPLTGAIESNATTLPEIIEEMLITTSSERQGRLIDHDQAGSMEQKKRQGYF 322
Cdd:TIGR02039 241 LGCYPLTGAIESDAATVEEIIAETAAARTSERQGRAIDRDQAASMEDKKREGYF 294
|
|
| Sulfate_adenylyltransferase_2 |
cd23946 |
Sulfate adenylyltransferase subunit 2; Sulfate adenylyltransferase subunits 1 and 2 form ATP ... |
28-241 |
8.40e-156 |
|
Sulfate adenylyltransferase subunit 2; Sulfate adenylyltransferase subunits 1 and 2 form ATP sulfurylase (ATPS) that catalyzes the adenylation of sulfate producing adenosine 5'-phosphosulfate (APS) and diphosphate, the first enzymatic step in the sulfur assimilation pathway. APS synthesis involves the formation of a high-energy phosphoric-sulfuric acid anhydride bond driven by GTP hydrolysis by CysN, coupled to ATP hydrolysis by CysD. CysD belongs to the ATP pyrophosphatase (ATP PPase) family of proteins, members of which include PAPS reductase, GMP synthetase, asparagine synthetase, and NAD(+) synthetase. This subunit is responsible for directly forming APS under control of the G protein. A modified version of the P loop (PP-loop), the fingerprint peptide of mononucleotide-binding proteins, is present in the active site of the protein, which appears to be a positively charged cleft containing a number of conserved arginine and lysine residues.
Pssm-ID: 467511 Cd Length: 214 Bit Score: 434.62 E-value: 8.40e-156
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498361442 28 HLQQLEAESIHIIREVAAEFENPVMMYSIGKDSSVMLHLARKAFYPGKIPFPMLHVDTNWKFKEMIKFRDETAKKFGLDL 107
Cdd:cd23946 1 HLRQLEAESIHIIREVAAEFSNPVMLYSIGKDSSVMLHLARKAFYPGKPPFPLLHVDTTWKFREMIEFRDRVAKEYGLDL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498361442 108 IVHKNPDGLAMDINPFVHGSSKHTDIMKTEGLKQALNKYGFDAAFGGARRDEEKSRAKERVYSFRDKSHRWDPKNQRPEL 187
Cdd:cd23946 81 IVHVNPDGVEAGINPFTHGSAKHTDIMKTEGLKQALDKYGFDAAFGGARRDEEKSRAKERVYSFRDSNHRWDPKNQRPEL 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 498361442 188 WRVYNSQVNKGESIRVFPLSNWTELDIWQYIYLENIDIVPLYFAAMRPVVDRGG 241
Cdd:cd23946 161 WNQYNGRVKKGESIRVFPLSNWTELDIWQYIYLENIPIVPLYFAAERPVIERDG 214
|
|
| CysD |
COG0175 |
3'-phosphoadenosine 5'-phosphosulfate sulfotransferase (PAPS reductase)/FAD synthetase or ... |
23-320 |
6.09e-85 |
|
3'-phosphoadenosine 5'-phosphosulfate sulfotransferase (PAPS reductase)/FAD synthetase or related enzyme [Amino acid transport and metabolism, Coenzyme transport and metabolism]; 3'-phosphoadenosine 5'-phosphosulfate sulfotransferase (PAPS reductase)/FAD synthetase or related enzyme is part of the Pathway/BioSystem: Cysteine biosynthesis
Pssm-ID: 439945 [Multi-domain] Cd Length: 232 Bit Score: 255.54 E-value: 6.09e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498361442 23 RERLTHL-QQLEAESIHIIREVAAEF-ENPVMMYSIGKDSSVMLHLARKAfypgKIPFPMLHVDTNWKFKEMIKFRDETA 100
Cdd:COG0175 7 DDLLEELnAELEAEAIEILREAAAEFgGRVVVSSSGGKDSTVLLHLAAKF----KPPIPVLFLDTGYEFPETYEFRDRLA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498361442 101 KKFGLDLIVHKNPDGLAMD-----INPFVHGSSKHTDIMKTEGLKQALNKYGFDAAFGGARRDEEKSRAKERVYSfrdks 175
Cdd:COG0175 83 ERLGLDLIVVRPEDAFAEQlaefgPPLFYRDPRWCCKIRKVEPLKRALAGYDFDAWITGLRRDESPTRAKEPVVE----- 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498361442 176 hrWDPknqrpelwrvynsqvnKGESIRVFPLSNWTELDIWQYIYLENIDIVPLYFaamrpvvdrggikimvdddrmpigp 255
Cdd:COG0175 158 --WDP----------------VGGLIKVNPLADWTELDVWAYIRREDLPYNPLYD------------------------- 194
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 498361442 256 edevkqelVRFRTLGCYPLTGAIESNattlpeiieEMlittssERQGRLIDHDQAgsmeqKKRQG 320
Cdd:COG0175 195 --------QGYPSIGCAPCTRAVESG---------ED------ERAGRWWDEEKE-----RKECG 231
|
|
| PAPS_reduct |
pfam01507 |
Phosphoadenosine phosphosulfate reductase family; This domain is found in phosphoadenosine ... |
49-277 |
4.36e-71 |
|
Phosphoadenosine phosphosulfate reductase family; This domain is found in phosphoadenosine phosphosulfate (PAPS) reductase enzymes or PAPS sulfotransferase. PAPS reductase is part of the adenine nucleotide alpha hydrolases superfamily also including N type ATP PPases and ATP sulphurylases. The enzyme uses thioredoxin as an electron donor for the reduction of PAPS to phospho-adenosine-phosphate (PAP). It is also found in NodP nodulation protein P from Rhizobium which has ATP sulfurylase activity (sulfate adenylate transferase).
Pssm-ID: 396201 [Multi-domain] Cd Length: 173 Bit Score: 217.93 E-value: 4.36e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498361442 49 NPVMMYSIGKDSSVMLHLARKAFYPGkipfPMLHVDTNWKFKEMIKFRDETAKKFGLDLIVHKNPDGLAMDINPFVHGSS 128
Cdd:pfam01507 1 ELVVSFSGGKDSLVLLHLASKAFPPG----PVIFIDTGYEFPETYEFVDELEEKYGLNLKVYLPEDSFAEGINPEGIPSS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498361442 129 ---KHTDIMKTEGLKQALNKYGFDAAFGGARRDEEKSRAKERVYSFRDKSHRwdpknqrpelwrvynsqvnkgeSIRVFP 205
Cdd:pfam01507 77 lyrRCCRLRKVEPLKRALKELGFDAWFTGLRRDESPSRAKLPIVSIDGDFPK----------------------VIKVFP 134
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 498361442 206 LSNWTELDIWQYIYLENIDIVPLYFAAmrpvvdrggikimvdddrmpigpedevkqelvrFRTLGCYPLTGA 277
Cdd:pfam01507 135 LLNWTETDVWQYILANNVPYNPLYDQG---------------------------------YRSIGCYPCTGP 173
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PRK05253 |
PRK05253 |
sulfate adenylyltransferase subunit CysD; |
22-322 |
0e+00 |
|
sulfate adenylyltransferase subunit CysD;
Pssm-ID: 235375 Cd Length: 301 Bit Score: 645.27 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498361442 22 TRERLTHLQQLEAESIHIIREVAAEFENPVMMYSIGKDSSVMLHLARKAFYPGKIPFPMLHVDTNWKFKEMIKFRDETAK 101
Cdd:PRK05253 2 DQYRLTHLDQLEAESIHILREVAAEFENPVMLYSIGKDSSVMLHLARKAFYPGKLPFPLLHVDTGWKFPEMIEFRDRRAK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498361442 102 KFGLDLIVHKNPDGLAMDINPFVHGSSKHTDIMKTEGLKQALNKYGFDAAFGGARRDEEKSRAKERVYSFRDKSHRWDPK 181
Cdd:PRK05253 82 ELGLELIVHSNPEGIARGINPFRHGSAKHTNAMKTEGLKQALEKYGFDAAFGGARRDEEKSRAKERIFSFRDEFGQWDPK 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498361442 182 NQRPELWRVYNSQVNKGESIRVFPLSNWTELDIWQYIYLENIDIVPLYFAAMRPVVDRGGIKIMVdDDRMPIGPEDEVKQ 261
Cdd:PRK05253 162 NQRPELWNLYNGRINKGEHIRVFPLSNWTELDIWQYIERENIPIVPLYFAHERPVVERDGMLIMV-DDRMPLRPGEVVEE 240
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 498361442 262 ELVRFRTLGCYPLTGAIESNATTLPEIIEEMLITTSSERQGRLIDHDQAGSMEQKKRQGYF 322
Cdd:PRK05253 241 RMVRFRTLGCYPCTGAVESEAATLEEIIAEMLVTRTSERGGRAIDDDQEASMEKRKREGYF 301
|
|
| CysD |
TIGR02039 |
sulfate adenylyltransferase, small subunit; Metabolic assimilation of sulfur from inorganic ... |
29-322 |
0e+00 |
|
sulfate adenylyltransferase, small subunit; Metabolic assimilation of sulfur from inorganic sulfate, requires sulfate activation by coupling to a nucleoside, for the production of high-energy nucleoside phosphosulfates. This pathway appears to be similar in all prokaryotic organisms. Activation is first achieved through sulfation of sulfate with ATP by sulfate adenylyltransferase (ATP sulfurylase) to produce 5'-phosphosulfate (APS), coupled by GTP hydrolysis. Subsequently, APS is phosphorylated by an APS kinase to produce 3'-phosphoadenosine-5'-phosphosulfate (PAPS). In Escherichia coli, ATP sulfurylase is a heterodimer composed of two subunits encoded by cysD and cysN, with APS kinase encoded by cysC. These genes are located in a unidirectionally transcribed gene cluster, and have been shown to be required for the synthesis of sulfur-containing amino acids. Homologous to this E.coli activation pathway are nodPQH gene products found among members of the Rhizobiaceae family. These gene products have been shown to exhibit ATP sulfurase and APS kinase activity, yet are involved in Nod factor sulfation, and sulfation of other macromolecules. [Central intermediary metabolism, Sulfur metabolism]
Pssm-ID: 131094 Cd Length: 294 Bit Score: 558.58 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498361442 29 LQQLEAESIHIIREVAAEFENPVMMYSIGKDSSVMLHLARKAFYPGKIPFPMLHVDTNWKFKEMIKFRDETAKKFGLDLI 108
Cdd:TIGR02039 1 LRALESEAIHIIREVAAEFERPVMLYSIGKDSSVLLHLARKAFYPGPLPFPLLHVDTGWKFREMIAFRDHMVAKYGLRLI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498361442 109 VHKNPDGLAMDINPFVHGSSKHTDIMKTEGLKQALNKYGFDAAFGGARRDEEKSRAKERVYSFRDKSHRWDPKNQRPELW 188
Cdd:TIGR02039 81 VHSNEEGIADGINPFTEGSALHTDIMKTEALRQALDKNQFDAAFGGARRDEEKSRAKERIFSFRNAFHQWDPKKQRPELW 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498361442 189 RVYNSQVNKGESIRVFPLSNWTELDIWQYIYLENIDIVPLYFAAMRPVVDRGGIKIMVDDDRMPIGPEDEVKQELVRFRT 268
Cdd:TIGR02039 161 NLYNGRISKGESVRVFPLSNWTELDIWRYIAAENIPIVPLYFAAKRPVVQRDGMLIMVDDVRMPLAPGEVVKERMVRFRT 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 498361442 269 LGCYPLTGAIESNATTLPEIIEEMLITTSSERQGRLIDHDQAGSMEQKKRQGYF 322
Cdd:TIGR02039 241 LGCYPLTGAIESDAATVEEIIAETAAARTSERQGRAIDRDQAASMEDKKREGYF 294
|
|
| PRK12563 |
PRK12563 |
sulfate adenylyltransferase subunit CysD; |
19-322 |
0e+00 |
|
sulfate adenylyltransferase subunit CysD;
Pssm-ID: 237138 Cd Length: 312 Bit Score: 549.39 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498361442 19 AGVTRERLTHLQQLEAESIHIIREVAAEFENPVMMYSIGKDSSVMLHLARKAFYPGKIPFPMLHVDTNWKFKEMIKFRDE 98
Cdd:PRK12563 9 AGASTSRMGHLDRLEAESIHILREVVAECSKPVMLYSIGKDSVVMLHLAMKAFRPTRPPFPLLHVDTTWKFREMIDFRDR 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498361442 99 TAKKFGLDLIVHKNPDGLAMDINPFVHGSSKHTDIMKTEGLKQALNKYGFDAAFGGARRDEEKSRAKERVYSFRDKSHRW 178
Cdd:PRK12563 89 RAKELGLDLVVHHNPDGIARGIVPFRHGSALHTDVAKTQGLKQALDHHGFDAAIGGARRDEEKSRAKERIFSFRSAFHRW 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498361442 179 DPKNQRPELWRVYNSQVNKGESIRVFPLSNWTELDIWQYIYLENIDIVPLYFAAMRPVVDRGGIKIMVDDDRMPIGPEDE 258
Cdd:PRK12563 169 DPKAQRPELWSLYNARLRRGESLRVFPLSNWTELDVWQYIAREKIPLVPLYFAKRRPVVERDGLLIMVDDERTPLRPGET 248
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 498361442 259 VKQELVRFRTLGCYPLTGAIESNATTLPEIIEEMLITTSSERQGRLIDHDQAGSMEQKKRQGYF 322
Cdd:PRK12563 249 PQQRKVRFRTLGCYPLTGAVESDADTVEKIIQEMAVTRISERQGRMIDQDSAASMEKKKKEGYF 312
|
|
| Sulfate_adenylyltransferase_2 |
cd23946 |
Sulfate adenylyltransferase subunit 2; Sulfate adenylyltransferase subunits 1 and 2 form ATP ... |
28-241 |
8.40e-156 |
|
Sulfate adenylyltransferase subunit 2; Sulfate adenylyltransferase subunits 1 and 2 form ATP sulfurylase (ATPS) that catalyzes the adenylation of sulfate producing adenosine 5'-phosphosulfate (APS) and diphosphate, the first enzymatic step in the sulfur assimilation pathway. APS synthesis involves the formation of a high-energy phosphoric-sulfuric acid anhydride bond driven by GTP hydrolysis by CysN, coupled to ATP hydrolysis by CysD. CysD belongs to the ATP pyrophosphatase (ATP PPase) family of proteins, members of which include PAPS reductase, GMP synthetase, asparagine synthetase, and NAD(+) synthetase. This subunit is responsible for directly forming APS under control of the G protein. A modified version of the P loop (PP-loop), the fingerprint peptide of mononucleotide-binding proteins, is present in the active site of the protein, which appears to be a positively charged cleft containing a number of conserved arginine and lysine residues.
Pssm-ID: 467511 Cd Length: 214 Bit Score: 434.62 E-value: 8.40e-156
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498361442 28 HLQQLEAESIHIIREVAAEFENPVMMYSIGKDSSVMLHLARKAFYPGKIPFPMLHVDTNWKFKEMIKFRDETAKKFGLDL 107
Cdd:cd23946 1 HLRQLEAESIHIIREVAAEFSNPVMLYSIGKDSSVMLHLARKAFYPGKPPFPLLHVDTTWKFREMIEFRDRVAKEYGLDL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498361442 108 IVHKNPDGLAMDINPFVHGSSKHTDIMKTEGLKQALNKYGFDAAFGGARRDEEKSRAKERVYSFRDKSHRWDPKNQRPEL 187
Cdd:cd23946 81 IVHVNPDGVEAGINPFTHGSAKHTDIMKTEGLKQALDKYGFDAAFGGARRDEEKSRAKERVYSFRDSNHRWDPKNQRPEL 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 498361442 188 WRVYNSQVNKGESIRVFPLSNWTELDIWQYIYLENIDIVPLYFAAMRPVVDRGG 241
Cdd:cd23946 161 WNQYNGRVKKGESIRVFPLSNWTELDIWQYIYLENIPIVPLYFAAERPVIERDG 214
|
|
| CysD |
COG0175 |
3'-phosphoadenosine 5'-phosphosulfate sulfotransferase (PAPS reductase)/FAD synthetase or ... |
23-320 |
6.09e-85 |
|
3'-phosphoadenosine 5'-phosphosulfate sulfotransferase (PAPS reductase)/FAD synthetase or related enzyme [Amino acid transport and metabolism, Coenzyme transport and metabolism]; 3'-phosphoadenosine 5'-phosphosulfate sulfotransferase (PAPS reductase)/FAD synthetase or related enzyme is part of the Pathway/BioSystem: Cysteine biosynthesis
Pssm-ID: 439945 [Multi-domain] Cd Length: 232 Bit Score: 255.54 E-value: 6.09e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498361442 23 RERLTHL-QQLEAESIHIIREVAAEF-ENPVMMYSIGKDSSVMLHLARKAfypgKIPFPMLHVDTNWKFKEMIKFRDETA 100
Cdd:COG0175 7 DDLLEELnAELEAEAIEILREAAAEFgGRVVVSSSGGKDSTVLLHLAAKF----KPPIPVLFLDTGYEFPETYEFRDRLA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498361442 101 KKFGLDLIVHKNPDGLAMD-----INPFVHGSSKHTDIMKTEGLKQALNKYGFDAAFGGARRDEEKSRAKERVYSfrdks 175
Cdd:COG0175 83 ERLGLDLIVVRPEDAFAEQlaefgPPLFYRDPRWCCKIRKVEPLKRALAGYDFDAWITGLRRDESPTRAKEPVVE----- 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498361442 176 hrWDPknqrpelwrvynsqvnKGESIRVFPLSNWTELDIWQYIYLENIDIVPLYFaamrpvvdrggikimvdddrmpigp 255
Cdd:COG0175 158 --WDP----------------VGGLIKVNPLADWTELDVWAYIRREDLPYNPLYD------------------------- 194
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 498361442 256 edevkqelVRFRTLGCYPLTGAIESNattlpeiieEMlittssERQGRLIDHDQAgsmeqKKRQG 320
Cdd:COG0175 195 --------QGYPSIGCAPCTRAVESG---------ED------ERAGRWWDEEKE-----RKECG 231
|
|
| PAPS_reduct |
pfam01507 |
Phosphoadenosine phosphosulfate reductase family; This domain is found in phosphoadenosine ... |
49-277 |
4.36e-71 |
|
Phosphoadenosine phosphosulfate reductase family; This domain is found in phosphoadenosine phosphosulfate (PAPS) reductase enzymes or PAPS sulfotransferase. PAPS reductase is part of the adenine nucleotide alpha hydrolases superfamily also including N type ATP PPases and ATP sulphurylases. The enzyme uses thioredoxin as an electron donor for the reduction of PAPS to phospho-adenosine-phosphate (PAP). It is also found in NodP nodulation protein P from Rhizobium which has ATP sulfurylase activity (sulfate adenylate transferase).
Pssm-ID: 396201 [Multi-domain] Cd Length: 173 Bit Score: 217.93 E-value: 4.36e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498361442 49 NPVMMYSIGKDSSVMLHLARKAFYPGkipfPMLHVDTNWKFKEMIKFRDETAKKFGLDLIVHKNPDGLAMDINPFVHGSS 128
Cdd:pfam01507 1 ELVVSFSGGKDSLVLLHLASKAFPPG----PVIFIDTGYEFPETYEFVDELEEKYGLNLKVYLPEDSFAEGINPEGIPSS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498361442 129 ---KHTDIMKTEGLKQALNKYGFDAAFGGARRDEEKSRAKERVYSFRDKSHRwdpknqrpelwrvynsqvnkgeSIRVFP 205
Cdd:pfam01507 77 lyrRCCRLRKVEPLKRALKELGFDAWFTGLRRDESPSRAKLPIVSIDGDFPK----------------------VIKVFP 134
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 498361442 206 LSNWTELDIWQYIYLENIDIVPLYFAAmrpvvdrggikimvdddrmpigpedevkqelvrFRTLGCYPLTGA 277
Cdd:pfam01507 135 LLNWTETDVWQYILANNVPYNPLYDQG---------------------------------YRSIGCYPCTGP 173
|
|
| PAPS_reductase-like_YbdN |
cd23947 |
uncharacterized phosphoadenosine phosphosulfate reductase-like proteins, similar to ... |
36-229 |
2.47e-24 |
|
uncharacterized phosphoadenosine phosphosulfate reductase-like proteins, similar to Escherichia coli YbdN; This subgroup contains Escherichia coli YbdN and other phosphoadenosine phosphosulfate (PAPS) reductase (or PAPS sulfotransferase EC 1.8.4.8)-like proteins. PAPS reductase is part of the adenine nucleotide alpha hydrolases superfamily also including N-type ATP PPases and ATP sulfurylases. A highly modified version of the P loop, the fingerprint peptide of mononucleotide-binding proteins, is present in the active site of the protein, which appears to be a positively charged cleft containing a number of conserved arginine and lysine residues. Although PAPS reductase has no ATPase activity, it shows a striking similarity to the structure of the ATP pyrophosphatase (ATP PPase) domain of GMP synthetase, indicating that both enzyme families have evolved from a common ancestral nucleotide-binding fold. The enzyme uses thioredoxin as an electron donor for the reduction of PAPS to phospho-adenosine-phosphate (PAP).
Pssm-ID: 467512 [Multi-domain] Cd Length: 206 Bit Score: 97.85 E-value: 2.47e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498361442 36 SIHIIREVAAEFENPVMMYSIGKDSSVMLHLARKAFYPGKIPFPMLHVDTNWKFKEMIKFRDETAKKFGLDLIVHKNPDG 115
Cdd:cd23947 1 ALERIRKVFEEFDPVIVSFSGGKDSLVLLHLALEALRRLRKDVYVVFIDTGIEFPETIDFVEKLAETLGLDVEAARPPLF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498361442 116 L-------------AMDINPFVHGSSKHTDIMKTEGLKQALN-KYGFDAAFG-GARRDEEKSRAKErvysfrdkshrwdP 180
Cdd:cd23947 81 LewltsnfqpqwdpIWDNPPPPRDYRWCCDELKLEPFTKWLKeKKPEGVLLLvGIRADESLNRAKR-------------P 147
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 498361442 181 KNQRPELWRvyNSQVNKgeSIRVFPLSNWTELDIWQYIYLENIDIVPLY 229
Cdd:cd23947 148 RVYRKYGWR--NSTLPG--QIVAYPIKDWSVEDVWLYILRHGLPYNPLY 192
|
|
| PRK13795 |
PRK13795 |
hypothetical protein; Provisional |
27-229 |
2.31e-17 |
|
hypothetical protein; Provisional
Pssm-ID: 237510 [Multi-domain] Cd Length: 636 Bit Score: 82.73 E-value: 2.31e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498361442 27 THLQQLEAESIHIIREVAAEFENPVMM-YSIGKDSSVMLHLARKAFYPGKIPFpmlhVDTNWKFKEMIKFRDETAKKFGL 105
Cdd:PRK13795 222 KHLEEKEKEAVNFIRGVAEKYNLPVSVsFSGGKDSLVVLDLAREALKDFKAFF----NNTGLEFPETVENVKEVAEEYGI 297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498361442 106 DLIVHKNPDGLAMDINPF------------VHGSSKHTDIMKTEGLKQALnkygfdaAFGGARRDEEKSRAKervysfrd 173
Cdd:PRK13795 298 ELIEADAGDAFWRAVEKFgppardyrwcckVCKLGPITRAIKENFPKGCL-------TFVGQRKYESFSRAK-------- 362
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 498361442 174 kshrwdpknqRPELWRvyNSQVnkGESIRVFPLSNWTELDIWQYIYLENIDIVPLY 229
Cdd:PRK13795 363 ----------SPRVWR--NPWV--PNQIGASPIQDWTALEVWLYIFWRKLPYNPLY 404
|
|
| PAPS_reductase |
cd23945 |
Phosphoadenylyl-sulfate reductase (thioredoxin); Phosphoadenosine phosphosulfate (PAPS) ... |
39-230 |
1.83e-16 |
|
Phosphoadenylyl-sulfate reductase (thioredoxin); Phosphoadenosine phosphosulfate (PAPS) reductase (or PAPS sulfotransferase EC 1.8.4.8) is part of the adenine nucleotide alpha hydrolase superfamily that also includes N-type ATP PPases and ATP sulfurylases. A highly modified version of the P loop, the fingerprint peptide of mononucleotide-binding proteins, is present in the active site of the protein, which appears to be a positively charged cleft containing a number of conserved arginine and lysine residues. Although PAPS reductase has no ATPase activity, it shows a striking similarity to the structure of the ATP pyrophosphatase (ATP PPase) domain of GMP synthetase, indicating that both enzyme families have evolved from a common ancestral nucleotide-binding fold. The enzyme uses thioredoxin as an electron donor for the reduction of PAPS to phospho-adenosine-phosphate (PAP).
Pssm-ID: 467510 [Multi-domain] Cd Length: 183 Bit Score: 76.10 E-value: 1.83e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498361442 39 IIREVAAEFENPVMMYSIGKDSSVMLHLARKAFYPGKIPFpmlhVDTNWKFKEMIKFRDETAKKFGLDLIVHKNPDGLAM 118
Cdd:cd23945 5 LLWAAEEFGPKLVFATSFGAEDAVILDLLSKVRPDIPVVF----LDTGYLFPETYDLIDEVEARYGLNIEVYFPEGTEAE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498361442 119 D------INPF-VHGSSKHTDIMKTEGLKQALNKYGFDAAFGGARRDEEKSRAKERVYSfrdkshrWDPKNQRpelwrvy 191
Cdd:cd23945 81 EealeggLNEFyLEDEERYDCCRKRKPFPLALALLGVKAWITGRRRDQSPTRANLPIVE-------VDEEGGL------- 146
|
170 180 190
....*....|....*....|....*....|....*....
gi 498361442 192 nsqvnkgesIRVFPLSNWTELDIWQYIYLENIDIVPLYF 230
Cdd:cd23945 147 ---------VKINPLADWTWEDVWAYIREHDLPYNPLHD 176
|
|
| FAD_synthase |
cd23948 |
FAD synthase; FAD synthase (FMN:ATP adenylyl transferase (FMNAT); FAD pyrophosphorylase; ... |
35-229 |
3.07e-15 |
|
FAD synthase; FAD synthase (FMN:ATP adenylyl transferase (FMNAT); FAD pyrophosphorylase; Flavin adenine dinucleotide synthase (FADS); EC 2.7.7.2) is involved in the biochemical pathway for converting riboflavin into FAD. By sequence comparison, bacterial and eukaryotic FMNAT enzymes belong to two different protein superfamilies and apparently utilize different sets of active-site residues to accomplish the same chemistry. This subfamily includes eukaryotic FMNATs, which are members of the 3'-phosphoadenosine 5'-phosphosulfate (PAPS) reductase-like family belonging to the adenine nucleotide alpha hydrolase superfamily, which has conserved motifs different from those of nucleotidylyl transferases.
Pssm-ID: 467513 [Multi-domain] Cd Length: 179 Bit Score: 72.55 E-value: 3.07e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498361442 35 ESIHIIREVAAEFENPVMMYSI--GKDSSVMLHLAR----KAFYPGKIPFPMLHVDTNWKFKEMIKFRDETAKKFGLDLI 108
Cdd:cd23948 4 SALEVIEEALDKYGPEEIAISFngGKDCTVLLHLLRaalkRKYPSPLTPLKALYIKSPDPFPEVEEFVEDTAKRYNLDLI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498361442 109 VHKNPdglamdinpfvhgsskhtdiMKtEGLKQALNKYG-FDAAFGGARRDEEKSrakERVYSFRDKSHRWdpknqrPEL 187
Cdd:cd23948 84 TIDGP--------------------MK-EGLEELLKEHPiIKAVFMGTRRTDPHG---ENLKPFSPTDPGW------PQF 133
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 498361442 188 wrvynsqvnkgesIRVFPLSNWTELDIWQYIYLENIDIVPLY 229
Cdd:cd23948 134 -------------MRVNPILDWSYHDVWEFLRTLNLPYCSLY 162
|
|
| PRK13794 |
PRK13794 |
hypothetical protein; Provisional |
29-229 |
3.32e-14 |
|
hypothetical protein; Provisional
Pssm-ID: 237509 [Multi-domain] Cd Length: 479 Bit Score: 72.78 E-value: 3.32e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498361442 29 LQQLEAESIHIIREVAAEFENPVMM-YSIGKDSSVMLHLARKAFypgKIPFPMLHVDTNWKFKEMIKFRDETAKKFGLDL 107
Cdd:PRK13794 228 LDKYERNSIGFIRNTAEKINKPVTVaYSGGKDSLATLLLALKAL---GINFPVLFNDTGLEFPETLENVEDVEKHYGLEI 304
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498361442 108 IVHKNPDglamdinpFVHGSSKH----------TDIMKTEGLKQAL-NKYGFDA-AFGGARRDEEKSRAKervysfrdks 175
Cdd:PRK13794 305 IRTKSEE--------FWEKLEEYgppardnrwcSEVCKLEPLGKLIdEKYEGEClSFVGQRKYESFNRSK---------- 366
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 498361442 176 hrwdpknqRPELWRvyNSQVNKgeSIRVFPLSNWTELDIWQYIYLENIDIVPLY 229
Cdd:PRK13794 367 --------KPRIWR--NPYIKK--QILAAPILHWTAMHVWIYLFREKAPYNKLY 408
|
|
| PRK02090 |
PRK02090 |
phosphoadenylyl-sulfate reductase; |
11-218 |
8.17e-14 |
|
phosphoadenylyl-sulfate reductase;
Pssm-ID: 234997 Cd Length: 241 Bit Score: 69.87 E-value: 8.17e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498361442 11 PSDAQSIRAGVTRERLTHLQQLEaesihIIREVAAEF-ENPVMMYSIGKDSSVMLHLARKAfypgKIPFPMLHVDTNWKF 89
Cdd:PRK02090 8 PKADLALDLAELNAELEGASAQE-----RLAWALENFgGRLALVSSFGAEDAVLLHLVAQV----DPDIPVIFLDTGYLF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498361442 90 KEMIKFRDETAKKFGLDLIV-HKNPDGLAMDIN------PFVHGSSKHTDIMKTEGLKQALNkyGFDAAFGGARRDEEKS 162
Cdd:PRK02090 79 PETYRFIDELTERLLLNLKVyRPDASAAEQEARygglweQSVEDRDECCRIRKVEPLNRALA--GLDAWITGLRREQSGT 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 498361442 163 RAKERVYSfrdkshrWDpknqrpelwrvynsqvnkGESIRVFPLSNWTELDIWQYI 218
Cdd:PRK02090 157 RANLPVLE-------ID------------------GGRFKINPLADWTNEDVWAYL 187
|
|
| cysH |
TIGR00434 |
phosophoadenylyl-sulfate reductase (thioredoxin); This enzyme, involved in the assimilation of ... |
51-229 |
3.50e-13 |
|
phosophoadenylyl-sulfate reductase (thioredoxin); This enzyme, involved in the assimilation of inorganic sulfate, is designated cysH in Bacteria and MET16 in Saccharomyces cerevisiae. Synonyms include phosphoadenosine phosphosulfate reductase, PAPS reductase, and PAPS reductase, thioredoxin-dependent. In a reaction requiring reduced thioredoxin and NADPH, it converts 3(prime)-phosphoadenylylsulfate (PAPS) to sulfite and adenosine 3(prime),5(prime) diphosphate (PAP). A related family of plant enzymes, scoring below the trusted cutoff, differs in having a thioredoxin-like C-terminal domain, not requiring thioredoxin, and in having a preference for 5(prime)-adenylylsulfate (APS) over PAPS. [Central intermediary metabolism, Sulfur metabolism]
Pssm-ID: 129526 Cd Length: 212 Bit Score: 67.50 E-value: 3.50e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498361442 51 VMMYSIGKDSSVMLHLARKAfypgKIPFPMLHVDTNWKFKEMIKFRDETAKKFGLDLIVHKNPDGLAMDINPF-----VH 125
Cdd:TIGR00434 17 VYSTSFGIQGAVLLDLVSKI----SPDIPVIFLDTGYHFPETYELIDELTERYPLNIKVYKPDLSLAEQAAKYgdklwEQ 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498361442 126 GSSKHTDIMKTEGLKQALNKYGFDAAFGGARRDEEKSRAKERVYSFRDKShrwdpknqrpelwrvynsqvnkgESIRVFP 205
Cdd:TIGR00434 93 DPNKYDYLRKVEPMHRALKELHASAWFTGLRRDQGPSRANLSILNIDEKF-----------------------GILKVLP 149
|
170 180
....*....|....*....|....
gi 498361442 206 LSNWTELDIWQYIYLENIDIVPLY 229
Cdd:TIGR00434 150 LIDWTWKDVYQYIDAHNLPYNPLH 173
|
|
| PAPS_reductase |
TIGR02057 |
phosphoadenosine phosphosulfate reductase, thioredoxin dependent; Requiring thioredoxin as an ... |
51-238 |
5.43e-11 |
|
phosphoadenosine phosphosulfate reductase, thioredoxin dependent; Requiring thioredoxin as an electron donor, phosphoadenosine phosphosulfate reductase catalyzes the reduction of 3'-phosphoadenylylsulfate (PAPS) to sulfite and phospho-adenosine-phosphate (PAP). Found in enterobacteria, cyanobacteria, and yeast, PAPS reductase is related to a group of plant (TIGR00424) and bacterial (TIGR02055) enzymes preferring 5'-adenylylsulfate (APS) over PAPS as a substrate for reduction to sulfite. [Central intermediary metabolism, Sulfur metabolism]
Pssm-ID: 131112 Cd Length: 226 Bit Score: 61.39 E-value: 5.43e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498361442 51 VMMYSIGKDSSVMLHLARKAFYPgkiPFPMLHVDTNWKFKEMIKFRDETAKKFGLDLIVHKNPDGLAMDINPFVHGS--- 127
Cdd:TIGR02057 29 VQTSAFGIQALVTLHLLSSISEP---MIPVIFIDTLYHFPQTLTLKDELTKKYYQTLNLYKYDGCESEADFEAKYGKllw 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498361442 128 ----SKHTDIMKTEGLKQALNKYGFDAAFGGARRDEEKSRAKERVYSFRDKSHRwdpknqrpelwrvynsqvnkgesIRV 203
Cdd:TIGR02057 106 qkdiEKYDYIAKVEPMQRALKELNASAWFTGRRRDQGSARANLPVIEIDEQNGI-----------------------LKV 162
|
170 180 190
....*....|....*....|....*....|....*
gi 498361442 204 FPLSNWTELDIWQYIYLENIDIVPLYFAAMRPVVD 238
Cdd:TIGR02057 163 NPLIDWTFEQVYQYLDAHNVPYNPLLDQGYRSIGD 197
|
|
| PRK08557 |
PRK08557 |
hypothetical protein; Provisional |
23-229 |
4.89e-10 |
|
hypothetical protein; Provisional
Pssm-ID: 181465 [Multi-domain] Cd Length: 417 Bit Score: 60.15 E-value: 4.89e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498361442 23 RERLTHLQQLEAESIHIIREVAAEFENPVMM----YSIGKDSSVMLHLARKAfypgkIP-FPMLHVDTNWKFKEMIKFRD 97
Cdd:PRK08557 153 EKNKERIEKLEENSLSILKDYIEKYKNKGYAinasFSGGKDSSVSTLLAKEV-----IPdLEVIFIDTGLEYPETINYVK 227
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498361442 98 ETAKKFGLDLIVHK--------NPDGLAMDINPFVHgsskhtDIMKTEGLKQALNK-YGFDAAF--GGARRDEEKSRAK- 165
Cdd:PRK08557 228 DFAKKYDLNLDTLDgdnfwenlEKEGIPTKDNRWCN------SACKLMPLKEYLKKkYGNKKVLtiDGSRKYESFTRANl 301
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 498361442 166 --ERVYSFRDkshrwdpkNQrpelwrvynsqvnkgesIRVFPLSNWTELDIWQYIYLENIDIVPLY 229
Cdd:PRK08557 302 dyERKSGFID--------FQ-----------------TNVFPILDWNSLDIWSYIYLNDILYNPLY 342
|
|
| PRK08576 |
PRK08576 |
hypothetical protein; Provisional |
29-231 |
1.12e-09 |
|
hypothetical protein; Provisional
Pssm-ID: 236300 [Multi-domain] Cd Length: 438 Bit Score: 58.94 E-value: 1.12e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498361442 29 LQQLEAESIHIIREVaaEFENPVMMYSIGKDSSVMLHLARKAFypGKIPfpMLHVDTNWKFKEMIKFRDETAKKFGLDLI 108
Cdd:PRK08576 218 LEAFEKASIKFLRKF--EEWTVIVPWSGGKDSTAALLLAKKAF--GDVT--AVYVDTGYEMPLTDEYVEKVAEKLGVDLI 291
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498361442 109 VHKNPDGLAMDINPFVHGSSKHTDIMKTEGLKQALNKYGFDAAFGGARRDEEKSRAKervysfrdkshrwdpknqRPElw 188
Cdd:PRK08576 292 RAGVDVPMPIEKYGMPTHSNRWCTKLKVEALEEAIRELEDGLLVVGDRDGESARRRL------------------RPP-- 351
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 498361442 189 rVYNSQVNKGESIRVFPLSNWTELDIWQYIYLENIDIVPLYFA 231
Cdd:PRK08576 352 -VVERKTNFGKILVVMPIKFWSGAMVQLYILMNGLELNPLYYK 393
|
|
| AANH-like |
cd01986 |
adenine nucleotide alpha hydrolase (AANH)-like proteins; This group of adenine nucleotide ... |
50-118 |
3.37e-08 |
|
adenine nucleotide alpha hydrolase (AANH)-like proteins; This group of adenine nucleotide alpha hydrolase (AANH)-like proteins includes N-type ATP PPases and ATP sulfurylases. The domain forms an alpha/beta/alpha fold which binds to adenosine nucleotide.
Pssm-ID: 467490 [Multi-domain] Cd Length: 74 Bit Score: 49.76 E-value: 3.37e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 498361442 50 PVMMYSIGKDSSVMLHLARKAFYpgKIPFPMLHVDTNWKFKEMIKFRDETAKKFGLDLIVHKNPDGLAM 118
Cdd:cd01986 1 VVVGYSGGKDSSVALHLASRLGR--KAEVAVVHIDHGIGFKEEAESVASIARRSILKKLAEKGARAIAT 67
|
|
| |
