|
Name |
Accession |
Description |
Interval |
E-value |
| PRK05253 |
PRK05253 |
sulfate adenylyltransferase subunit CysD; |
3-304 |
0e+00 |
|
sulfate adenylyltransferase subunit CysD;
Pssm-ID: 235375 Cd Length: 301 Bit Score: 671.08 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490868236 3 LNEERLTHLKQLEAESIHIIREVAAEFENPVMLYSIGKDSAVMLHLALKAFYPAKLPFPLLHVDTGWKFKDMITFRDNMA 82
Cdd:PRK05253 1 MDQYRLTHLDQLEAESIHILREVAAEFENPVMLYSIGKDSSVMLHLARKAFYPGKLPFPLLHVDTGWKFPEMIEFRDRRA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490868236 83 KTHGFDLIVHQNKEGVEAGINPFDHGSSKYTDIMKTQGLKQALDKYGFDAAFGGARRDEEKSRAKERVYSFRDSKHRWDP 162
Cdd:PRK05253 81 KELGLELIVHSNPEGIARGINPFRHGSAKHTNAMKTEGLKQALEKYGFDAAFGGARRDEEKSRAKERIFSFRDEFGQWDP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490868236 163 KNQRPELWNLYNGKVNKGESIRVFPLSNWTELDIWQYIYLESIPLVPLYLAAERPVVERSGTLIMVDDeRMPLKEGEVPQ 242
Cdd:PRK05253 161 KNQRPELWNLYNGRINKGEHIRVFPLSNWTELDIWQYIERENIPIVPLYFAHERPVVERDGMLIMVDD-RMPLRPGEVVE 239
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490868236 243 MKSVRFRTLGCYPLTGAVESTANTLPEIIQEMLLATSSERQGRMIDHDEAGSMEKKKQEGYF 304
Cdd:PRK05253 240 ERMVRFRTLGCYPCTGAVESEAATLEEIIAEMLVTRTSERGGRAIDDDQEASMEKRKREGYF 301
|
|
| CysD |
TIGR02039 |
sulfate adenylyltransferase, small subunit; Metabolic assimilation of sulfur from inorganic ... |
11-304 |
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: 565.13 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490868236 11 LKQLEAESIHIIREVAAEFENPVMLYSIGKDSAVMLHLALKAFYPAKLPFPLLHVDTGWKFKDMITFRDNMAKTHGFDLI 90
Cdd:TIGR02039 1 LRALESEAIHIIREVAAEFERPVMLYSIGKDSSVLLHLARKAFYPGPLPFPLLHVDTGWKFREMIAFRDHMVAKYGLRLI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490868236 91 VHQNKEGVEAGINPFDHGSSKYTDIMKTQGLKQALDKYGFDAAFGGARRDEEKSRAKERVYSFRDSKHRWDPKNQRPELW 170
Cdd:TIGR02039 81 VHSNEEGIADGINPFTEGSALHTDIMKTEALRQALDKNQFDAAFGGARRDEEKSRAKERIFSFRNAFHQWDPKKQRPELW 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490868236 171 NLYNGKVNKGESIRVFPLSNWTELDIWQYIYLESIPLVPLYLAAERPVVERSGTLIMVDDERMPLKEGEVPQMKSVRFRT 250
Cdd:TIGR02039 161 NLYNGRISKGESVRVFPLSNWTELDIWRYIAAENIPIVPLYFAAKRPVVQRDGMLIMVDDVRMPLAPGEVVKERMVRFRT 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 490868236 251 LGCYPLTGAVESTANTLPEIIQEMLLATSSERQGRMIDHDEAGSMEKKKQEGYF 304
Cdd:TIGR02039 241 LGCYPLTGAIESDAATVEEIIAETAAARTSERQGRAIDRDQAASMEDKKREGYF 294
|
|
| Sulfate_adenylyltransferase_2 |
cd23946 |
Sulfate adenylyltransferase subunit 2; Sulfate adenylyltransferase subunits 1 and 2 form ATP ... |
10-223 |
1.48e-155 |
|
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: 433.08 E-value: 1.48e-155
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490868236 10 HLKQLEAESIHIIREVAAEFENPVMLYSIGKDSAVMLHLALKAFYPAKLPFPLLHVDTGWKFKDMITFRDNMAKTHGFDL 89
Cdd:cd23946 1 HLRQLEAESIHIIREVAAEFSNPVMLYSIGKDSSVMLHLARKAFYPGKPPFPLLHVDTTWKFREMIEFRDRVAKEYGLDL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490868236 90 IVHQNKEGVEAGINPFDHGSSKYTDIMKTQGLKQALDKYGFDAAFGGARRDEEKSRAKERVYSFRDSKHRWDPKNQRPEL 169
Cdd:cd23946 81 IVHVNPDGVEAGINPFTHGSAKHTDIMKTEGLKQALDKYGFDAAFGGARRDEEKSRAKERVYSFRDSNHRWDPKNQRPEL 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 490868236 170 WNLYNGKVNKGESIRVFPLSNWTELDIWQYIYLESIPLVPLYLAAERPVVERSG 223
Cdd:cd23946 161 WNQYNGRVKKGESIRVFPLSNWTELDIWQYIYLENIPIVPLYFAAERPVIERDG 214
|
|
| CysD |
COG0175 |
3'-phosphoadenosine 5'-phosphosulfate sulfotransferase (PAPS reductase)/FAD synthetase or ... |
5-302 |
8.04e-87 |
|
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: 259.39 E-value: 8.04e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490868236 5 EERLTHLKQ-LEAESIHIIREVAAEF-ENPVMLYSIGKDSAVMLHLALKAfypaKLPFPLLHVDTGWKFKDMITFRDNMA 82
Cdd:COG0175 7 DDLLEELNAeLEAEAIEILREAAAEFgGRVVVSSSGGKDSTVLLHLAAKF----KPPIPVLFLDTGYEFPETYEFRDRLA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490868236 83 KTHGFDLIVHQNKEGVEA-----GINPFDHGSSKYTDIMKTQGLKQALDKYGFDAAFGGARRDEEKSRAKERVYSfrdsk 157
Cdd:COG0175 83 ERLGLDLIVVRPEDAFAEqlaefGPPLFYRDPRWCCKIRKVEPLKRALAGYDFDAWITGLRRDESPTRAKEPVVE----- 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490868236 158 hrWDPknqrpelwnlyngkvnKGESIRVFPLSNWTELDIWQYIYLESIPLVPLYlaaerpvversgtlimvddermplke 237
Cdd:COG0175 158 --WDP----------------VGGLIKVNPLADWTELDVWAYIRREDLPYNPLY-------------------------- 193
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 490868236 238 gevpqmkSVRFRTLGCYPLTGAVEStantlPEIiqemllatssERQGRMIDHDEAgsmekKKQEG 302
Cdd:COG0175 194 -------DQGYPSIGCAPCTRAVES-----GED----------ERAGRWWDEEKE-----RKECG 231
|
|
| PAPS_reduct |
pfam01507 |
Phosphoadenosine phosphosulfate reductase family; This domain is found in phosphoadenosine ... |
31-259 |
7.88e-69 |
|
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: 211.77 E-value: 7.88e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490868236 31 NPVMLYSIGKDSAVMLHLALKAFYPaklpFPLLHVDTGWKFKDMITFRDNMAKTHGFDLIVHQNKEGVEAGINPFDHGSS 110
Cdd:pfam01507 1 ELVVSFSGGKDSLVLLHLASKAFPP----GPVIFIDTGYEFPETYEFVDELEEKYGLNLKVYLPEDSFAEGINPEGIPSS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490868236 111 ---KYTDIMKTQGLKQALDKYGFDAAFGGARRDEEKSRAKERVYSFRDSKHRwdpknqrpelwnlyngkvnkgeSIRVFP 187
Cdd:pfam01507 77 lyrRCCRLRKVEPLKRALKELGFDAWFTGLRRDESPSRAKLPIVSIDGDFPK----------------------VIKVFP 134
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490868236 188 LSNWTELDIWQYIYLESIPLVPLYLAAerpvversgtlimvddermplkegevpqmksvrFRTLGCYPLTGA 259
Cdd:pfam01507 135 LLNWTETDVWQYILANNVPYNPLYDQG---------------------------------YRSIGCYPCTGP 173
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PRK05253 |
PRK05253 |
sulfate adenylyltransferase subunit CysD; |
3-304 |
0e+00 |
|
sulfate adenylyltransferase subunit CysD;
Pssm-ID: 235375 Cd Length: 301 Bit Score: 671.08 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490868236 3 LNEERLTHLKQLEAESIHIIREVAAEFENPVMLYSIGKDSAVMLHLALKAFYPAKLPFPLLHVDTGWKFKDMITFRDNMA 82
Cdd:PRK05253 1 MDQYRLTHLDQLEAESIHILREVAAEFENPVMLYSIGKDSSVMLHLARKAFYPGKLPFPLLHVDTGWKFPEMIEFRDRRA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490868236 83 KTHGFDLIVHQNKEGVEAGINPFDHGSSKYTDIMKTQGLKQALDKYGFDAAFGGARRDEEKSRAKERVYSFRDSKHRWDP 162
Cdd:PRK05253 81 KELGLELIVHSNPEGIARGINPFRHGSAKHTNAMKTEGLKQALEKYGFDAAFGGARRDEEKSRAKERIFSFRDEFGQWDP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490868236 163 KNQRPELWNLYNGKVNKGESIRVFPLSNWTELDIWQYIYLESIPLVPLYLAAERPVVERSGTLIMVDDeRMPLKEGEVPQ 242
Cdd:PRK05253 161 KNQRPELWNLYNGRINKGEHIRVFPLSNWTELDIWQYIERENIPIVPLYFAHERPVVERDGMLIMVDD-RMPLRPGEVVE 239
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490868236 243 MKSVRFRTLGCYPLTGAVESTANTLPEIIQEMLLATSSERQGRMIDHDEAGSMEKKKQEGYF 304
Cdd:PRK05253 240 ERMVRFRTLGCYPCTGAVESEAATLEEIIAEMLVTRTSERGGRAIDDDQEASMEKRKREGYF 301
|
|
| PRK12563 |
PRK12563 |
sulfate adenylyltransferase subunit CysD; |
6-304 |
0e+00 |
|
sulfate adenylyltransferase subunit CysD;
Pssm-ID: 237138 Cd Length: 312 Bit Score: 582.13 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490868236 6 ERLTHLKQLEAESIHIIREVAAEFENPVMLYSIGKDSAVMLHLALKAFYPAKLPFPLLHVDTGWKFKDMITFRDNMAKTH 85
Cdd:PRK12563 14 SRMGHLDRLEAESIHILREVVAECSKPVMLYSIGKDSVVMLHLAMKAFRPTRPPFPLLHVDTTWKFREMIDFRDRRAKEL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490868236 86 GFDLIVHQNKEGVEAGINPFDHGSSKYTDIMKTQGLKQALDKYGFDAAFGGARRDEEKSRAKERVYSFRDSKHRWDPKNQ 165
Cdd:PRK12563 94 GLDLVVHHNPDGIARGIVPFRHGSALHTDVAKTQGLKQALDHHGFDAAIGGARRDEEKSRAKERIFSFRSAFHRWDPKAQ 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490868236 166 RPELWNLYNGKVNKGESIRVFPLSNWTELDIWQYIYLESIPLVPLYLAAERPVVERSGTLIMVDDERMPLKEGEVPQMKS 245
Cdd:PRK12563 174 RPELWSLYNARLRRGESLRVFPLSNWTELDVWQYIAREKIPLVPLYFAKRRPVVERDGLLIMVDDERTPLRPGETPQQRK 253
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 490868236 246 VRFRTLGCYPLTGAVESTANTLPEIIQEMLLATSSERQGRMIDHDEAGSMEKKKQEGYF 304
Cdd:PRK12563 254 VRFRTLGCYPLTGAVESDADTVEKIIQEMAVTRISERQGRMIDQDSAASMEKKKKEGYF 312
|
|
| CysD |
TIGR02039 |
sulfate adenylyltransferase, small subunit; Metabolic assimilation of sulfur from inorganic ... |
11-304 |
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: 565.13 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490868236 11 LKQLEAESIHIIREVAAEFENPVMLYSIGKDSAVMLHLALKAFYPAKLPFPLLHVDTGWKFKDMITFRDNMAKTHGFDLI 90
Cdd:TIGR02039 1 LRALESEAIHIIREVAAEFERPVMLYSIGKDSSVLLHLARKAFYPGPLPFPLLHVDTGWKFREMIAFRDHMVAKYGLRLI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490868236 91 VHQNKEGVEAGINPFDHGSSKYTDIMKTQGLKQALDKYGFDAAFGGARRDEEKSRAKERVYSFRDSKHRWDPKNQRPELW 170
Cdd:TIGR02039 81 VHSNEEGIADGINPFTEGSALHTDIMKTEALRQALDKNQFDAAFGGARRDEEKSRAKERIFSFRNAFHQWDPKKQRPELW 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490868236 171 NLYNGKVNKGESIRVFPLSNWTELDIWQYIYLESIPLVPLYLAAERPVVERSGTLIMVDDERMPLKEGEVPQMKSVRFRT 250
Cdd:TIGR02039 161 NLYNGRISKGESVRVFPLSNWTELDIWRYIAAENIPIVPLYFAAKRPVVQRDGMLIMVDDVRMPLAPGEVVKERMVRFRT 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 490868236 251 LGCYPLTGAVESTANTLPEIIQEMLLATSSERQGRMIDHDEAGSMEKKKQEGYF 304
Cdd:TIGR02039 241 LGCYPLTGAIESDAATVEEIIAETAAARTSERQGRAIDRDQAASMEDKKREGYF 294
|
|
| Sulfate_adenylyltransferase_2 |
cd23946 |
Sulfate adenylyltransferase subunit 2; Sulfate adenylyltransferase subunits 1 and 2 form ATP ... |
10-223 |
1.48e-155 |
|
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: 433.08 E-value: 1.48e-155
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490868236 10 HLKQLEAESIHIIREVAAEFENPVMLYSIGKDSAVMLHLALKAFYPAKLPFPLLHVDTGWKFKDMITFRDNMAKTHGFDL 89
Cdd:cd23946 1 HLRQLEAESIHIIREVAAEFSNPVMLYSIGKDSSVMLHLARKAFYPGKPPFPLLHVDTTWKFREMIEFRDRVAKEYGLDL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490868236 90 IVHQNKEGVEAGINPFDHGSSKYTDIMKTQGLKQALDKYGFDAAFGGARRDEEKSRAKERVYSFRDSKHRWDPKNQRPEL 169
Cdd:cd23946 81 IVHVNPDGVEAGINPFTHGSAKHTDIMKTEGLKQALDKYGFDAAFGGARRDEEKSRAKERVYSFRDSNHRWDPKNQRPEL 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 490868236 170 WNLYNGKVNKGESIRVFPLSNWTELDIWQYIYLESIPLVPLYLAAERPVVERSG 223
Cdd:cd23946 161 WNQYNGRVKKGESIRVFPLSNWTELDIWQYIYLENIPIVPLYFAAERPVIERDG 214
|
|
| CysD |
COG0175 |
3'-phosphoadenosine 5'-phosphosulfate sulfotransferase (PAPS reductase)/FAD synthetase or ... |
5-302 |
8.04e-87 |
|
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: 259.39 E-value: 8.04e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490868236 5 EERLTHLKQ-LEAESIHIIREVAAEF-ENPVMLYSIGKDSAVMLHLALKAfypaKLPFPLLHVDTGWKFKDMITFRDNMA 82
Cdd:COG0175 7 DDLLEELNAeLEAEAIEILREAAAEFgGRVVVSSSGGKDSTVLLHLAAKF----KPPIPVLFLDTGYEFPETYEFRDRLA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490868236 83 KTHGFDLIVHQNKEGVEA-----GINPFDHGSSKYTDIMKTQGLKQALDKYGFDAAFGGARRDEEKSRAKERVYSfrdsk 157
Cdd:COG0175 83 ERLGLDLIVVRPEDAFAEqlaefGPPLFYRDPRWCCKIRKVEPLKRALAGYDFDAWITGLRRDESPTRAKEPVVE----- 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490868236 158 hrWDPknqrpelwnlyngkvnKGESIRVFPLSNWTELDIWQYIYLESIPLVPLYlaaerpvversgtlimvddermplke 237
Cdd:COG0175 158 --WDP----------------VGGLIKVNPLADWTELDVWAYIRREDLPYNPLY-------------------------- 193
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 490868236 238 gevpqmkSVRFRTLGCYPLTGAVEStantlPEIiqemllatssERQGRMIDHDEAgsmekKKQEG 302
Cdd:COG0175 194 -------DQGYPSIGCAPCTRAVES-----GED----------ERAGRWWDEEKE-----RKECG 231
|
|
| PAPS_reduct |
pfam01507 |
Phosphoadenosine phosphosulfate reductase family; This domain is found in phosphoadenosine ... |
31-259 |
7.88e-69 |
|
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: 211.77 E-value: 7.88e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490868236 31 NPVMLYSIGKDSAVMLHLALKAFYPaklpFPLLHVDTGWKFKDMITFRDNMAKTHGFDLIVHQNKEGVEAGINPFDHGSS 110
Cdd:pfam01507 1 ELVVSFSGGKDSLVLLHLASKAFPP----GPVIFIDTGYEFPETYEFVDELEEKYGLNLKVYLPEDSFAEGINPEGIPSS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490868236 111 ---KYTDIMKTQGLKQALDKYGFDAAFGGARRDEEKSRAKERVYSFRDSKHRwdpknqrpelwnlyngkvnkgeSIRVFP 187
Cdd:pfam01507 77 lyrRCCRLRKVEPLKRALKELGFDAWFTGLRRDESPSRAKLPIVSIDGDFPK----------------------VIKVFP 134
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490868236 188 LSNWTELDIWQYIYLESIPLVPLYLAAerpvversgtlimvddermplkegevpqmksvrFRTLGCYPLTGA 259
Cdd:pfam01507 135 LLNWTETDVWQYILANNVPYNPLYDQG---------------------------------YRSIGCYPCTGP 173
|
|
| PAPS_reductase-like_YbdN |
cd23947 |
uncharacterized phosphoadenosine phosphosulfate reductase-like proteins, similar to ... |
18-211 |
4.01e-23 |
|
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: 94.38 E-value: 4.01e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490868236 18 SIHIIREVAAEFENPVMLYSIGKDSAVMLHLALKAFYPAKLPFPLLHVDTGWKFKDMITFRDNMAKTHGFDlIVHQ---- 93
Cdd:cd23947 1 ALERIRKVFEEFDPVIVSFSGGKDSLVLLHLALEALRRLRKDVYVVFIDTGIEFPETIDFVEKLAETLGLD-VEAArppl 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490868236 94 ----NKEGVEAGINPFDHGSSKY------TDIMKTQGLKQAL-DKYGFDAAFG-GARRDEEKSRAKE-RVYSFRDSKHRW 160
Cdd:cd23947 80 flewLTSNFQPQWDPIWDNPPPPrdyrwcCDELKLEPFTKWLkEKKPEGVLLLvGIRADESLNRAKRpRVYRKYGWRNST 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 490868236 161 DPKnqrpelwnlyngkvnkgeSIRVFPLSNWTELDIWQYIYLESIPLVPLY 211
Cdd:cd23947 160 LPG------------------QIVAYPIKDWSVEDVWLYILRHGLPYNPLY 192
|
|
| PRK13795 |
PRK13795 |
hypothetical protein; Provisional |
9-211 |
3.36e-16 |
|
hypothetical protein; Provisional
Pssm-ID: 237510 [Multi-domain] Cd Length: 636 Bit Score: 78.88 E-value: 3.36e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490868236 9 THLKQLEAESIHIIREVAAEFENPVML-YSIGKDSAVMLHLALKAFypakLPFPLLHVDTGWKFKDMITFRDNMAKTHGF 87
Cdd:PRK13795 222 KHLEEKEKEAVNFIRGVAEKYNLPVSVsFSGGKDSLVVLDLAREAL----KDFKAFFNNTGLEFPETVENVKEVAEEYGI 297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490868236 88 DLIVhqnkegVEAGiNPFDHGSSKY-------------------TDIMKTQGLKQALdkygfdaAFGGARRDEEKSRAKe 148
Cdd:PRK13795 298 ELIE------ADAG-DAFWRAVEKFgppardyrwcckvcklgpiTRAIKENFPKGCL-------TFVGQRKYESFSRAK- 362
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490868236 149 rvySFRDSKHRWDPkNQrpelwnlyngkvnkgesIRVFPLSNWTELDIWQYIYLESIPLVPLY 211
Cdd:PRK13795 363 ---SPRVWRNPWVP-NQ-----------------IGASPIQDWTALEVWLYIFWRKLPYNPLY 404
|
|
| PAPS_reductase |
cd23945 |
Phosphoadenylyl-sulfate reductase (thioredoxin); Phosphoadenosine phosphosulfate (PAPS) ... |
21-211 |
8.58e-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: 73.79 E-value: 8.58e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490868236 21 IIREVAAEFENPVMLYSIGKDSAVMLHLALKAfypaKLPFPLLHVDTGWKFKDMITFRDNMAKTHGFDLIVHQNK----- 95
Cdd:cd23945 5 LLWAAEEFGPKLVFATSFGAEDAVILDLLSKV----RPDIPVVFLDTGYLFPETYDLIDEVEARYGLNIEVYFPEgteae 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490868236 96 -EGVEAGINPFD-HGSSKYTDIMKTQGLKQALDKYGFDAAFGGARRDEEKSRAKERVYSfrdskhrWDPKNQRPelwnly 173
Cdd:cd23945 81 eEALEGGLNEFYlEDEERYDCCRKRKPFPLALALLGVKAWITGRRRDQSPTRANLPIVE-------VDEEGGLV------ 147
|
170 180 190
....*....|....*....|....*....|....*...
gi 490868236 174 ngKVNkgesirvfPLSNWTELDIWQYIYLESIPLVPLY 211
Cdd:cd23945 148 --KIN--------PLADWTWEDVWAYIREHDLPYNPLH 175
|
|
| PRK02090 |
PRK02090 |
phosphoadenylyl-sulfate reductase; |
9-211 |
7.00e-15 |
|
phosphoadenylyl-sulfate reductase;
Pssm-ID: 234997 Cd Length: 241 Bit Score: 72.56 E-value: 7.00e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490868236 9 THLKQLEAEsiHIIREVAAEF-ENPVMLYSIGKDSAVMLHLALKAfypaKLPFPLLHVDTGWKFKDMITFRDNMAKTHGF 87
Cdd:PRK02090 21 AELEGASAQ--ERLAWALENFgGRLALVSSFGAEDAVLLHLVAQV----DPDIPVIFLDTGYLFPETYRFIDELTERLLL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490868236 88 DLIVHQ---------------NKEGVEaginpfDHGssKYTDIMKTQGLKQALDkyGFDAAFGGARRDEEKSRAKERVYS 152
Cdd:PRK02090 95 NLKVYRpdasaaeqearygglWEQSVE------DRD--ECCRIRKVEPLNRALA--GLDAWITGLRREQSGTRANLPVLE 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 490868236 153 FRDSKHrwdpknqrpelwnlyngKVNkgesirvfPLSNWTELDIWQYIYLESIPLVPLY 211
Cdd:PRK02090 165 IDGGRF-----------------KIN--------PLADWTNEDVWAYLKEHDLPYHPLV 198
|
|
| PRK13794 |
PRK13794 |
hypothetical protein; Provisional |
11-211 |
8.29e-15 |
|
hypothetical protein; Provisional
Pssm-ID: 237509 [Multi-domain] Cd Length: 479 Bit Score: 74.32 E-value: 8.29e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490868236 11 LKQLEAESIHIIREVAAEFENPVML-YSIGKDSAVMLHLALKAFypaKLPFPLLHVDTGWKFKDMITFRDNMAKTHGFDL 89
Cdd:PRK13794 228 LDKYERNSIGFIRNTAEKINKPVTVaYSGGKDSLATLLLALKAL---GINFPVLFNDTGLEFPETLENVEDVEKHYGLEI 304
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490868236 90 IVHQNK---EGVEA-GINPFDhgSSKYTDIMKTQGLKQALD-KYGFDA-AFGGARRDEEKSRAKervysfrdskhrwdpk 163
Cdd:PRK13794 305 IRTKSEefwEKLEEyGPPARD--NRWCSEVCKLEPLGKLIDeKYEGEClSFVGQRKYESFNRSK---------------- 366
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 490868236 164 nqRPELWNlyNGKVNKgeSIRVFPLSNWTELDIWQYIYLESIPLVPLY 211
Cdd:PRK13794 367 --KPRIWR--NPYIKK--QILAAPILHWTAMHVWIYLFREKAPYNKLY 408
|
|
| cysH |
TIGR00434 |
phosophoadenylyl-sulfate reductase (thioredoxin); This enzyme, involved in the assimilation of ... |
33-211 |
2.13e-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: 67.89 E-value: 2.13e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490868236 33 VMLYSIGKDSAVMLHLALKAFYPAKLPFpllhVDTGWKFKDMITFRDNMAKTHGFDLIVHQNKE-----GVEAGINPFDH 107
Cdd:TIGR00434 17 VYSTSFGIQGAVLLDLVSKISPDIPVIF----LDTGYHFPETYELIDELTERYPLNIKVYKPDLslaeqAAKYGDKLWEQ 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490868236 108 GSSKYTDIMKTQGLKQALDKYGFDAAFGGARRDEEKSRAKERVYSFRDskhrwdpknqrpelwnlyngkvnKGESIRVFP 187
Cdd:TIGR00434 93 DPNKYDYLRKVEPMHRALKELHASAWFTGLRRDQGPSRANLSILNIDE-----------------------KFGILKVLP 149
|
170 180
....*....|....*....|....
gi 490868236 188 LSNWTELDIWQYIYLESIPLVPLY 211
Cdd:TIGR00434 150 LIDWTWKDVYQYIDAHNLPYNPLH 173
|
|
| PAPS_reductase |
TIGR02057 |
phosphoadenosine phosphosulfate reductase, thioredoxin dependent; Requiring thioredoxin as an ... |
33-211 |
1.89e-10 |
|
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: 59.85 E-value: 1.89e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490868236 33 VMLYSIGKDSAVMLHLALKAFYPaklPFPLLHVDTGWKFKDMITFRDNMAKTHGFDLIVH-----QNKEGVEAGINPF-- 105
Cdd:TIGR02057 29 VQTSAFGIQALVTLHLLSSISEP---MIPVIFIDTLYHFPQTLTLKDELTKKYYQTLNLYkydgcESEADFEAKYGKLlw 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490868236 106 DHGSSKYTDIMKTQGLKQALDKYGFDAAFGGARRDEEKSRAKERVYSFrdskhrwDPKNQRpelwnlyngkvnkgesIRV 185
Cdd:TIGR02057 106 QKDIEKYDYIAKVEPMQRALKELNASAWFTGRRRDQGSARANLPVIEI-------DEQNGI----------------LKV 162
|
170 180
....*....|....*....|....*.
gi 490868236 186 FPLSNWTELDIWQYIYLESIPLVPLY 211
Cdd:TIGR02057 163 NPLIDWTFEQVYQYLDAHNVPYNPLL 188
|
|
| FAD_synthase |
cd23948 |
FAD synthase; FAD synthase (FMN:ATP adenylyl transferase (FMNAT); FAD pyrophosphorylase; ... |
17-211 |
3.49e-10 |
|
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: 57.92 E-value: 3.49e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490868236 17 ESIHIIREVAAEFENP-VML-YSIGKDSAVMLHL---ALKAFYPAKL-PFPLLHVDTGWKFKDMITFRDNMAKTHGFDLI 90
Cdd:cd23948 4 SALEVIEEALDKYGPEeIAIsFNGGKDCTVLLHLlraALKRKYPSPLtPLKALYIKSPDPFPEVEEFVEDTAKRYNLDLI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490868236 91 VHqnkegveaginpfdHGSskytdiMKtQGLKQALDKYG-FDAAFGGARRDEEKSrakERVYSFRDSKHRWdpknqrPEL 169
Cdd:cd23948 84 TI--------------DGP------MK-EGLEELLKEHPiIKAVFMGTRRTDPHG---ENLKPFSPTDPGW------PQF 133
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 490868236 170 wnlyngkvnkgesIRVFPLSNWTELDIWQYIYLESIPLVPLY 211
Cdd:cd23948 134 -------------MRVNPILDWSYHDVWEFLRTLNLPYCSLY 162
|
|
| PRK08557 |
PRK08557 |
hypothetical protein; Provisional |
4-211 |
1.25e-09 |
|
hypothetical protein; Provisional
Pssm-ID: 181465 [Multi-domain] Cd Length: 417 Bit Score: 58.61 E-value: 1.25e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490868236 4 NEERLthlKQLEAESIHIIREVAAEFENPVML----YSIGKDSAVMLHLALKAFYPAKLPFpllhVDTGWKFKDMITFRD 79
Cdd:PRK08557 155 NKERI---EKLEENSLSILKDYIEKYKNKGYAinasFSGGKDSSVSTLLAKEVIPDLEVIF----IDTGLEYPETINYVK 227
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490868236 80 NMAKTHGFDLIV--------HQNKEGVEAGINPFdhgsskYTDIMKTQGLKQALDK-YGFDAAF--GGARRDEEKSRAK- 147
Cdd:PRK08557 228 DFAKKYDLNLDTldgdnfweNLEKEGIPTKDNRW------CNSACKLMPLKEYLKKkYGNKKVLtiDGSRKYESFTRANl 301
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 490868236 148 --ERVYSFRDskhrwdpkNQrpelwnlyngkvnkgesIRVFPLSNWTELDIWQYIYLESIPLVPLY 211
Cdd:PRK08557 302 dyERKSGFID--------FQ-----------------TNVFPILDWNSLDIWSYIYLNDILYNPLY 342
|
|
| PRK08576 |
PRK08576 |
hypothetical protein; Provisional |
1-240 |
9.06e-07 |
|
hypothetical protein; Provisional
Pssm-ID: 236300 [Multi-domain] Cd Length: 438 Bit Score: 49.69 E-value: 9.06e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490868236 1 MSLNEERLTHLKQLEAESIHIIREVaaEFENPVMLYSIGKDSAVMLHLALKAFYPAKLpfplLHVDTGWKFKDMITFRDN 80
Cdd:PRK08576 208 EKLIEANREVLEAFEKASIKFLRKF--EEWTVIVPWSGGKDSTAALLLAKKAFGDVTA----VYVDTGYEMPLTDEYVEK 281
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490868236 81 MAKTHGFDLIvhqnKEGVEAGINPFDHG----SSKYTDIMKTQGLKQALDKYGFDAAFGGARRDEEKSRAKervysfrds 156
Cdd:PRK08576 282 VAEKLGVDLI----RAGVDVPMPIEKYGmpthSNRWCTKLKVEALEEAIRELEDGLLVVGDRDGESARRRL--------- 348
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490868236 157 khrwdpknqRPELwnlYNGKVNKGESIRVFPLSNWTELDIWQYIYLESIPLVPLY--------------LAA-ERPVVER 221
Cdd:PRK08576 349 ---------RPPV---VERKTNFGKILVVMPIKFWSGAMVQLYILMNGLELNPLYykgfyrlgcyicpsLRSwEIELLKR 416
|
250
....*....|....*....
gi 490868236 222 SGTLIMVDDERmPLKEGEV 240
Cdd:PRK08576 417 LPVLPLILKKR-PLYKFLV 434
|
|
| AANH-like |
cd01986 |
adenine nucleotide alpha hydrolase (AANH)-like proteins; This group of adenine nucleotide ... |
32-105 |
1.28e-06 |
|
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: 45.52 E-value: 1.28e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 490868236 32 PVMLYSIGKDSAVMLHLALKAFYpaKLPFPLLHVDTGWKFK-DMITFRDNMAKTHGFDLIVHQNKEGVEAGINPF 105
Cdd:cd01986 1 VVVGYSGGKDSSVALHLASRLGR--KAEVAVVHIDHGIGFKeEAESVASIARRSILKKLAEKGARAIATGVLRPL 73
|
|
| |
