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Conserved domains on  [gi|655374700|ref|WP_028780229|]
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MULTISPECIES: sulfate adenylyltransferase subunit CysD [Shewanella]

Protein Classification

sulfate adenylyltransferase subunit CysD( domain architecture ID 10012282)

sulfate adenylyltransferase subunit CysD (subunit 2) is the small subunit that with CysN, forms the ATP sulfurylase (ATPS) that catalyzes the conversion of ATP and sulfate to diphosphate and adenylyl sulfate

CATH:  3.40.50.620
EC:  2.7.7.4
Gene Symbol:  cysD
Gene Ontology:  GO:0005524|GO:0004781|GO:0009336|GO:0070814
PubMed:  12676676|16387658|2185135|2828368
SCOP:  4003838

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PRK05253 PRK05253
sulfate adenylyltransferase subunit CysD;
1-302 0e+00

sulfate adenylyltransferase subunit CysD;


:

Pssm-ID: 235375  Cd Length: 301  Bit Score: 649.51  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655374700   1 MSGPVLSHLEQLEAESIQIFREVAAEFDNPVMLYSIGKDSSVLLHLARKAFYPGKIPFPLLHVDTDWKFREMIRFRDQAA 80
Cdd:PRK05253   1 MDQYRLTHLDQLEAESIHILREVAAEFENPVMLYSIGKDSSVMLHLARKAFYPGKLPFPLLHVDTGWKFPEMIEFRDRRA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655374700  81 EKYGFELLVHKNPQGLAMGMNPFTFGSAKHTDVMKTEGLKQALDKYGFDAAFGGARRDEEKSRAKERVYSFRDRHHRWDP 160
Cdd:PRK05253  81 KELGLELIVHSNPEGIARGINPFRHGSAKHTNAMKTEGLKQALEKYGFDAAFGGARRDEEKSRAKERIFSFRDEFGQWDP 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655374700 161 KNQRPELWHTYNGQVNKGESIRVFPLSNWTELDIWQYIYQENIDIVPLYFAEQRPVVERDGSLIMVDDeRMPLNEGEVPE 240
Cdd:PRK05253 161 KNQRPELWNLYNGRINKGEHIRVFPLSNWTELDIWQYIERENIPIVPLYFAHERPVVERDGMLIMVDD-RMPLRPGEVVE 239

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 655374700 241 YRRVRFRTLGCYPLTGAIESSAATLAEIIEEMLLSRSSERQGRVIDRDSSGSMEKKKREGYF 302
Cdd:PRK05253 240 ERMVRFRTLGCYPCTGAVESEAATLEEIIAEMLVTRTSERGGRAIDDDQEASMEKRKREGYF 301
 
Name Accession Description Interval E-value
PRK05253 PRK05253
sulfate adenylyltransferase subunit CysD;
1-302 0e+00

sulfate adenylyltransferase subunit CysD;


Pssm-ID: 235375  Cd Length: 301  Bit Score: 649.51  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655374700   1 MSGPVLSHLEQLEAESIQIFREVAAEFDNPVMLYSIGKDSSVLLHLARKAFYPGKIPFPLLHVDTDWKFREMIRFRDQAA 80
Cdd:PRK05253   1 MDQYRLTHLDQLEAESIHILREVAAEFENPVMLYSIGKDSSVMLHLARKAFYPGKLPFPLLHVDTGWKFPEMIEFRDRRA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655374700  81 EKYGFELLVHKNPQGLAMGMNPFTFGSAKHTDVMKTEGLKQALDKYGFDAAFGGARRDEEKSRAKERVYSFRDRHHRWDP 160
Cdd:PRK05253  81 KELGLELIVHSNPEGIARGINPFRHGSAKHTNAMKTEGLKQALEKYGFDAAFGGARRDEEKSRAKERIFSFRDEFGQWDP 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655374700 161 KNQRPELWHTYNGQVNKGESIRVFPLSNWTELDIWQYIYQENIDIVPLYFAEQRPVVERDGSLIMVDDeRMPLNEGEVPE 240
Cdd:PRK05253 161 KNQRPELWNLYNGRINKGEHIRVFPLSNWTELDIWQYIERENIPIVPLYFAHERPVVERDGMLIMVDD-RMPLRPGEVVE 239

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 655374700 241 YRRVRFRTLGCYPLTGAIESSAATLAEIIEEMLLSRSSERQGRVIDRDSSGSMEKKKREGYF 302
Cdd:PRK05253 240 ERMVRFRTLGCYPCTGAVESEAATLEEIIAEMLVTRTSERGGRAIDDDQEASMEKRKREGYF 301
CysD TIGR02039
sulfate adenylyltransferase, small subunit; Metabolic assimilation of sulfur from inorganic ...
 9-302 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 655374700    9 LEQLEAESIQIFREVAAEFDNPVMLYSIGKDSSVLLHLARKAFYPGKIPFPLLHVDTDWKFREMIRFRDQAAEKYGFELL 88
Cdd:TIGR02039   1 LRALESEAIHIIREVAAEFERPVMLYSIGKDSSVLLHLARKAFYPGPLPFPLLHVDTGWKFREMIAFRDHMVAKYGLRLI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655374700   89 VHKNPQGLAMGMNPFTFGSAKHTDVMKTEGLKQALDKYGFDAAFGGARRDEEKSRAKERVYSFRDRHHRWDPKNQRPELW 168
Cdd:TIGR02039  81 VHSNEEGIADGINPFTEGSALHTDIMKTEALRQALDKNQFDAAFGGARRDEEKSRAKERIFSFRNAFHQWDPKKQRPELW 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655374700  169 HTYNGQVNKGESIRVFPLSNWTELDIWQYIYQENIDIVPLYFAEQRPVVERDGSLIMVDDERMPLNEGEVPEYRRVRFRT 248
Cdd:TIGR02039 161 NLYNGRISKGESVRVFPLSNWTELDIWRYIAAENIPIVPLYFAAKRPVVQRDGMLIMVDDVRMPLAPGEVVKERMVRFRT 240

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....
gi 655374700  249 LGCYPLTGAIESSAATLAEIIEEMLLSRSSERQGRVIDRDSSGSMEKKKREGYF 302
Cdd:TIGR02039 241 LGCYPLTGAIESDAATVEEIIAETAAARTSERQGRAIDRDQAASMEDKKREGYF 294
Sulfate_adenylyltransferase_2 cd23946
Sulfate adenylyltransferase subunit 2; Sulfate adenylyltransferase subunits 1 and 2 form ATP ...
 8-221 4.65e-154

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: 429.23  E-value: 4.65e-154
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655374700   8 HLEQLEAESIQIFREVAAEFDNPVMLYSIGKDSSVLLHLARKAFYPGKIPFPLLHVDTDWKFREMIRFRDQAAEKYGFEL 87
Cdd:cd23946    1 HLRQLEAESIHIIREVAAEFSNPVMLYSIGKDSSVMLHLARKAFYPGKPPFPLLHVDTTWKFREMIEFRDRVAKEYGLDL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655374700  88 LVHKNPQGLAMGMNPFTFGSAKHTDVMKTEGLKQALDKYGFDAAFGGARRDEEKSRAKERVYSFRDRHHRWDPKNQRPEL 167
Cdd:cd23946   81 IVHVNPDGVEAGINPFTHGSAKHTDIMKTEGLKQALDKYGFDAAFGGARRDEEKSRAKERVYSFRDSNHRWDPKNQRPEL 160

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 655374700 168 WHTYNGQVNKGESIRVFPLSNWTELDIWQYIYQENIDIVPLYFAEQRPVVERDG 221
Cdd:cd23946  161 WNQYNGRVKKGESIRVFPLSNWTELDIWQYIYLENIPIVPLYFAAERPVIERDG 214
CysD COG0175
3'-phosphoadenosine 5'-phosphosulfate sulfotransferase (PAPS reductase)/FAD synthetase or ...
 5-300 1.06e-83

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: 251.69  E-value: 1.06e-83
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655374700   5 VLSHLEQ-LEAESIQIFREVAAEF-DNPVMLYSIGKDSSVLLHLARKAfypgKIPFPLLHVDTDWKFREMIRFRDQAAEK 82
Cdd:COG0175    9 LLEELNAeLEAEAIEILREAAAEFgGRVVVSSSGGKDSTVLLHLAAKF----KPPIPVLFLDTGYEFPETYEFRDRLAER 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655374700  83 YGFELLVHKNPQGLAM-----GMNPFTFGSAKHTDVMKTEGLKQALDKYGFDAAFGGARRDEEKSRAKERVYSfrdrhhr 157
Cdd:COG0175   85 LGLDLIVVRPEDAFAEqlaefGPPLFYRDPRWCCKIRKVEPLKRALAGYDFDAWITGLRRDESPTRAKEPVVE------- 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655374700 158 WDPknqrpelwhtyngqvnKGESIRVFPLSNWTELDIWQYIYQENIDIVPLYFaeqrpvverdgslimvddermplnege 237
Cdd:COG0175  158 WDP----------------VGGLIKVNPLADWTELDVWAYIRREDLPYNPLYD--------------------------- 194

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 655374700 238 vpeyrrVRFRTLGCYPLTGAIESsaatlAEIieemllsrssERQGRVIDRDSSgsmekKKREG 300
Cdd:COG0175  195 ------QGYPSIGCAPCTRAVES-----GED----------ERAGRWWDEEKE-----RKECG 231
PAPS_reduct pfam01507
Phosphoadenosine phosphosulfate reductase family; This domain is found in phosphoadenosine ...
 29-257 3.11e-70

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: 215.24  E-value: 3.11e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655374700   29 NPVMLYSIGKDSSVLLHLARKAFYPGkipfPLLHVDTDWKFREMIRFRDQAAEKYGFELLVHKNPQGLAMGMNPFTFGSA 108
Cdd:pfam01507   1 ELVVSFSGGKDSLVLLHLASKAFPPG----PVIFIDTGYEFPETYEFVDELEEKYGLNLKVYLPEDSFAEGINPEGIPSS 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655374700  109 ---KHTDVMKTEGLKQALDKYGFDAAFGGARRDEEKSRAKERVYSFRDRHHRwdpknqrpelwhtyngqvnkgeSIRVFP 185
Cdd:pfam01507  77 lyrRCCRLRKVEPLKRALKELGFDAWFTGLRRDESPSRAKLPIVSIDGDFPK----------------------VIKVFP 134

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 655374700  186 LSNWTELDIWQYIYQENIDIVPLYFAEqrpvverdgslimvddermplnegevpeyrrvrFRTLGCYPLTGA 257
Cdd:pfam01507 135 LLNWTETDVWQYILANNVPYNPLYDQG---------------------------------YRSIGCYPCTGP 173
 
Name Accession Description Interval E-value
PRK05253 PRK05253
sulfate adenylyltransferase subunit CysD;
1-302 0e+00

sulfate adenylyltransferase subunit CysD;


Pssm-ID: 235375  Cd Length: 301  Bit Score: 649.51  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655374700   1 MSGPVLSHLEQLEAESIQIFREVAAEFDNPVMLYSIGKDSSVLLHLARKAFYPGKIPFPLLHVDTDWKFREMIRFRDQAA 80
Cdd:PRK05253   1 MDQYRLTHLDQLEAESIHILREVAAEFENPVMLYSIGKDSSVMLHLARKAFYPGKLPFPLLHVDTGWKFPEMIEFRDRRA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655374700  81 EKYGFELLVHKNPQGLAMGMNPFTFGSAKHTDVMKTEGLKQALDKYGFDAAFGGARRDEEKSRAKERVYSFRDRHHRWDP 160
Cdd:PRK05253  81 KELGLELIVHSNPEGIARGINPFRHGSAKHTNAMKTEGLKQALEKYGFDAAFGGARRDEEKSRAKERIFSFRDEFGQWDP 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655374700 161 KNQRPELWHTYNGQVNKGESIRVFPLSNWTELDIWQYIYQENIDIVPLYFAEQRPVVERDGSLIMVDDeRMPLNEGEVPE 240
Cdd:PRK05253 161 KNQRPELWNLYNGRINKGEHIRVFPLSNWTELDIWQYIERENIPIVPLYFAHERPVVERDGMLIMVDD-RMPLRPGEVVE 239

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 655374700 241 YRRVRFRTLGCYPLTGAIESSAATLAEIIEEMLLSRSSERQGRVIDRDSSGSMEKKKREGYF 302
Cdd:PRK05253 240 ERMVRFRTLGCYPCTGAVESEAATLEEIIAEMLVTRTSERGGRAIDDDQEASMEKRKREGYF 301
CysD TIGR02039
sulfate adenylyltransferase, small subunit; Metabolic assimilation of sulfur from inorganic ...
 9-302 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 655374700    9 LEQLEAESIQIFREVAAEFDNPVMLYSIGKDSSVLLHLARKAFYPGKIPFPLLHVDTDWKFREMIRFRDQAAEKYGFELL 88
Cdd:TIGR02039   1 LRALESEAIHIIREVAAEFERPVMLYSIGKDSSVLLHLARKAFYPGPLPFPLLHVDTGWKFREMIAFRDHMVAKYGLRLI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655374700   89 VHKNPQGLAMGMNPFTFGSAKHTDVMKTEGLKQALDKYGFDAAFGGARRDEEKSRAKERVYSFRDRHHRWDPKNQRPELW 168
Cdd:TIGR02039  81 VHSNEEGIADGINPFTEGSALHTDIMKTEALRQALDKNQFDAAFGGARRDEEKSRAKERIFSFRNAFHQWDPKKQRPELW 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655374700  169 HTYNGQVNKGESIRVFPLSNWTELDIWQYIYQENIDIVPLYFAEQRPVVERDGSLIMVDDERMPLNEGEVPEYRRVRFRT 248
Cdd:TIGR02039 161 NLYNGRISKGESVRVFPLSNWTELDIWRYIAAENIPIVPLYFAAKRPVVQRDGMLIMVDDVRMPLAPGEVVKERMVRFRT 240

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....
gi 655374700  249 LGCYPLTGAIESSAATLAEIIEEMLLSRSSERQGRVIDRDSSGSMEKKKREGYF 302
Cdd:TIGR02039 241 LGCYPLTGAIESDAATVEEIIAETAAARTSERQGRAIDRDQAASMEDKKREGYF 294
PRK12563 PRK12563
sulfate adenylyltransferase subunit CysD;
4-302 0e+00

sulfate adenylyltransferase subunit CysD;


Pssm-ID: 237138  Cd Length: 312  Bit Score: 552.47  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655374700   4 PVLSHLEQLEAESIQIFREVAAEFDNPVMLYSIGKDSSVLLHLARKAFYPGKIPFPLLHVDTDWKFREMIRFRDQAAEKY 83
Cdd:PRK12563  14 SRMGHLDRLEAESIHILREVVAECSKPVMLYSIGKDSVVMLHLAMKAFRPTRPPFPLLHVDTTWKFREMIDFRDRRAKEL 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655374700  84 GFELLVHKNPQGLAMGMNPFTFGSAKHTDVMKTEGLKQALDKYGFDAAFGGARRDEEKSRAKERVYSFRDRHHRWDPKNQ 163
Cdd:PRK12563  94 GLDLVVHHNPDGIARGIVPFRHGSALHTDVAKTQGLKQALDHHGFDAAIGGARRDEEKSRAKERIFSFRSAFHRWDPKAQ 173

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655374700 164 RPELWHTYNGQVNKGESIRVFPLSNWTELDIWQYIYQENIDIVPLYFAEQRPVVERDGSLIMVDDERMPLNEGEVPEYRR 243
Cdd:PRK12563 174 RPELWSLYNARLRRGESLRVFPLSNWTELDVWQYIAREKIPLVPLYFAKRRPVVERDGLLIMVDDERTPLRPGETPQQRK 253

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 655374700 244 VRFRTLGCYPLTGAIESSAATLAEIIEEMLLSRSSERQGRVIDRDSSGSMEKKKREGYF 302
Cdd:PRK12563 254 VRFRTLGCYPLTGAVESDADTVEKIIQEMAVTRISERQGRMIDQDSAASMEKKKKEGYF 312
Sulfate_adenylyltransferase_2 cd23946
Sulfate adenylyltransferase subunit 2; Sulfate adenylyltransferase subunits 1 and 2 form ATP ...
 8-221 4.65e-154

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: 429.23  E-value: 4.65e-154
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655374700   8 HLEQLEAESIQIFREVAAEFDNPVMLYSIGKDSSVLLHLARKAFYPGKIPFPLLHVDTDWKFREMIRFRDQAAEKYGFEL 87
Cdd:cd23946    1 HLRQLEAESIHIIREVAAEFSNPVMLYSIGKDSSVMLHLARKAFYPGKPPFPLLHVDTTWKFREMIEFRDRVAKEYGLDL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655374700  88 LVHKNPQGLAMGMNPFTFGSAKHTDVMKTEGLKQALDKYGFDAAFGGARRDEEKSRAKERVYSFRDRHHRWDPKNQRPEL 167
Cdd:cd23946   81 IVHVNPDGVEAGINPFTHGSAKHTDIMKTEGLKQALDKYGFDAAFGGARRDEEKSRAKERVYSFRDSNHRWDPKNQRPEL 160

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 655374700 168 WHTYNGQVNKGESIRVFPLSNWTELDIWQYIYQENIDIVPLYFAEQRPVVERDG 221
Cdd:cd23946  161 WNQYNGRVKKGESIRVFPLSNWTELDIWQYIYLENIPIVPLYFAAERPVIERDG 214
CysD COG0175
3'-phosphoadenosine 5'-phosphosulfate sulfotransferase (PAPS reductase)/FAD synthetase or ...
 5-300 1.06e-83

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: 251.69  E-value: 1.06e-83
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655374700   5 VLSHLEQ-LEAESIQIFREVAAEF-DNPVMLYSIGKDSSVLLHLARKAfypgKIPFPLLHVDTDWKFREMIRFRDQAAEK 82
Cdd:COG0175    9 LLEELNAeLEAEAIEILREAAAEFgGRVVVSSSGGKDSTVLLHLAAKF----KPPIPVLFLDTGYEFPETYEFRDRLAER 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655374700  83 YGFELLVHKNPQGLAM-----GMNPFTFGSAKHTDVMKTEGLKQALDKYGFDAAFGGARRDEEKSRAKERVYSfrdrhhr 157
Cdd:COG0175   85 LGLDLIVVRPEDAFAEqlaefGPPLFYRDPRWCCKIRKVEPLKRALAGYDFDAWITGLRRDESPTRAKEPVVE------- 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655374700 158 WDPknqrpelwhtyngqvnKGESIRVFPLSNWTELDIWQYIYQENIDIVPLYFaeqrpvverdgslimvddermplnege 237
Cdd:COG0175  158 WDP----------------VGGLIKVNPLADWTELDVWAYIRREDLPYNPLYD--------------------------- 194

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 655374700 238 vpeyrrVRFRTLGCYPLTGAIESsaatlAEIieemllsrssERQGRVIDRDSSgsmekKKREG 300
Cdd:COG0175  195 ------QGYPSIGCAPCTRAVES-----GED----------ERAGRWWDEEKE-----RKECG 231
PAPS_reduct pfam01507
Phosphoadenosine phosphosulfate reductase family; This domain is found in phosphoadenosine ...
 29-257 3.11e-70

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: 215.24  E-value: 3.11e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655374700   29 NPVMLYSIGKDSSVLLHLARKAFYPGkipfPLLHVDTDWKFREMIRFRDQAAEKYGFELLVHKNPQGLAMGMNPFTFGSA 108
Cdd:pfam01507   1 ELVVSFSGGKDSLVLLHLASKAFPPG----PVIFIDTGYEFPETYEFVDELEEKYGLNLKVYLPEDSFAEGINPEGIPSS 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655374700  109 ---KHTDVMKTEGLKQALDKYGFDAAFGGARRDEEKSRAKERVYSFRDRHHRwdpknqrpelwhtyngqvnkgeSIRVFP 185
Cdd:pfam01507  77 lyrRCCRLRKVEPLKRALKELGFDAWFTGLRRDESPSRAKLPIVSIDGDFPK----------------------VIKVFP 134

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 655374700  186 LSNWTELDIWQYIYQENIDIVPLYFAEqrpvverdgslimvddermplnegevpeyrrvrFRTLGCYPLTGA 257
Cdd:pfam01507 135 LLNWTETDVWQYILANNVPYNPLYDQG---------------------------------YRSIGCYPCTGP 173
PAPS_reductase-like_YbdN cd23947
uncharacterized phosphoadenosine phosphosulfate reductase-like proteins, similar to ...
 21-209 1.32e-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: 95.53  E-value: 1.32e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655374700  21 REVAAEFDNPVMLYSIGKDSSVLLHLARKAFYPGKIPFPLLHVDTDWKFREMIRFRDQAAEKYGFELLVHKNP------- 93
Cdd:cd23947    6 RKVFEEFDPVIVSFSGGKDSLVLLHLALEALRRLRKDVYVVFIDTGIEFPETIDFVEKLAETLGLDVEAARPPlflewlt 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655374700  94 ------QGLAMGMNPFTFGSAKHTDVMKTEGLKQAL-DKYGFDAAFG-GARRDEEKSRAKeRVYsfrdRHHRWDPKNQRP 165
Cdd:cd23947   86 snfqpqWDPIWDNPPPPRDYRWCCDELKLEPFTKWLkEKKPEGVLLLvGIRADESLNRAK-RPR----VYRKYGWRNSTL 160

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 655374700 166 ELWHTYngqvnkgesirvFPLSNWTELDIWQYIYQENIDIVPLY 209
Cdd:cd23947  161 PGQIVA------------YPIKDWSVEDVWLYILRHGLPYNPLY 192
PAPS_reductase cd23945
Phosphoadenylyl-sulfate reductase (thioredoxin); Phosphoadenosine phosphosulfate (PAPS) ...
 17-210 2.95e-17

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: 78.02  E-value: 2.95e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655374700  17 IQIFREVAAEFDNPVMLYSIGKDSSVLLHLARKAFYPgkipFPLLHVDTDWKFREMIRFRDQAAEKYGFELLVHKNPQGL 96
Cdd:cd23945    3 EILLWAAEEFGPKLVFATSFGAEDAVILDLLSKVRPD----IPVVFLDTGYLFPETYDLIDEVEARYGLNIEVYFPEGTE 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655374700  97 AM------GMNPF-TFGSAKHTDVMKTEGLKQALDKYGFDAAFGGARRDEEKSRAKERVYSfrdrhhrWDPKNQRpelwh 169
Cdd:cd23945   79 AEeealegGLNEFyLEDEERYDCCRKRKPFPLALALLGVKAWITGRRRDQSPTRANLPIVE-------VDEEGGL----- 146

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 655374700 170 tyngqvnkgesIRVFPLSNWTELDIWQYIYQENIDIVPLYF 210
Cdd:cd23945  147 -----------VKINPLADWTWEDVWAYIREHDLPYNPLHD 176
PRK13795 PRK13795
hypothetical protein; Provisional
 7-209 2.11e-15

hypothetical protein; Provisional


Pssm-ID: 237510 [Multi-domain]  Cd Length: 636  Bit Score: 76.19  E-value: 2.11e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655374700   7 SHLEQLEAESIQIFREVAAEFDNPVML-YSIGKDSSVLLHLARKAFypGKipFPLLHVDTDWKFREMIRFRDQAAEKYGF 85
Cdd:PRK13795 222 KHLEEKEKEAVNFIRGVAEKYNLPVSVsFSGGKDSLVVLDLAREAL--KD--FKAFFNNTGLEFPETVENVKEVAEEYGI 297

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655374700  86 ELLVhknpqglAMGMNPF-----TFG-SAKH----TDVMKTEGLKQALDKYGFDA--AFGGARRDEEKSRAKervysfrd 153
Cdd:PRK13795 298 ELIE-------ADAGDAFwraveKFGpPARDyrwcCKVCKLGPITRAIKENFPKGclTFVGQRKYESFSRAK-------- 362

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 655374700 154 rhhrwdpknqRPELWHTY--NGQVNkgesirVFPLSNWTELDIWQYIYQENIDIVPLY 209
Cdd:PRK13795 363 ----------SPRVWRNPwvPNQIG------ASPIQDWTALEVWLYIFWRKLPYNPLY 404
PRK02090 PRK02090
phosphoadenylyl-sulfate reductase;
8-209 9.25e-13

phosphoadenylyl-sulfate reductase;


Pssm-ID: 234997  Cd Length: 241  Bit Score: 66.40  E-value: 9.25e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655374700   8 HLEQLEAEsiQIFREVAAEF-DNPVMLYSIGKDSSVLLHLARKAfypgKIPFPLLHVDTDWKFREMIRFRDQAAEKYGFE 86
Cdd:PRK02090  22 ELEGASAQ--ERLAWALENFgGRLALVSSFGAEDAVLLHLVAQV----DPDIPVIFLDTGYLFPETYRFIDELTERLLLN 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655374700  87 LLV-HKNPQGLAM-----GMNpftFGSAKHTD----VMKTEGLKQALDkyGFDAAFGGARRDEEKSRAKERVYSfrdrhh 156
Cdd:PRK02090  96 LKVyRPDASAAEQearygGLW---EQSVEDRDeccrIRKVEPLNRALA--GLDAWITGLRREQSGTRANLPVLE------ 164

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 655374700 157 rWDpknqrpelwhtyngqvnkGESIRVFPLSNWTELDIWQYIYQENIDIVPLY 209
Cdd:PRK02090 165 -ID------------------GGRFKINPLADWTNEDVWAYLKEHDLPYHPLV 198
PRK13794 PRK13794
hypothetical protein; Provisional
 9-209 8.73e-12

hypothetical protein; Provisional


Pssm-ID: 237509 [Multi-domain]  Cd Length: 479  Bit Score: 65.07  E-value: 8.73e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655374700   9 LEQLEAESIQIFREVAAEFDNPVML-YSIGKDSSVLLHLARKAFypgKIPFPLLHVDTDWKFREMIRFRDQAAEKYGFEL 87
Cdd:PRK13794 228 LDKYERNSIGFIRNTAEKINKPVTVaYSGGKDSLATLLLALKAL---GINFPVLFNDTGLEFPETLENVEDVEKHYGLEI 304

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655374700  88 LVHKNpqglamgmNPFTFGSAKH----------TDVMKTEGLKQALD-KYGFDA-AFGGARRDEEKSRAKervysfrdrh 155
Cdd:PRK13794 305 IRTKS--------EEFWEKLEEYgppardnrwcSEVCKLEPLGKLIDeKYEGEClSFVGQRKYESFNRSK---------- 366

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 655374700 156 hrwdpknqRPELWHtyNGQVNKgeSIRVFPLSNWTELDIWQYIYQENIDIVPLY 209
Cdd:PRK13794 367 --------KPRIWR--NPYIKK--QILAAPILHWTAMHVWIYLFREKAPYNKLY 408
cysH TIGR00434
phosophoadenylyl-sulfate reductase (thioredoxin); This enzyme, involved in the assimilation of ...
 31-209 1.01e-11

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: 63.27  E-value: 1.01e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655374700   31 VMLYSIGKDSSVLLHLARKAfyPGKIPFPLLhvDTDWKFREMIRFRDQAAEKYGFELLVHKNPQGLA-----MGMNPFTF 105
Cdd:TIGR00434  17 VYSTSFGIQGAVLLDLVSKI--SPDIPVIFL--DTGYHFPETYELIDELTERYPLNIKVYKPDLSLAeqaakYGDKLWEQ 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655374700  106 GSAKHTDVMKTEGLKQALDKYGFDAAFGGARRDEEKSRAKERVYSFRDrhhrwdpknqrpelwhtyngqvnKGESIRVFP 185
Cdd:TIGR00434  93 DPNKYDYLRKVEPMHRALKELHASAWFTGLRRDQGPSRANLSILNIDE-----------------------KFGILKVLP 149

                         170       180
                  ....*....|....*....|....
gi 655374700  186 LSNWTELDIWQYIYQENIDIVPLY 209
Cdd:TIGR00434 150 LIDWTWKDVYQYIDAHNLPYNPLH 173
FAD_synthase cd23948
FAD synthase; FAD synthase (FMN:ATP adenylyl transferase (FMNAT); FAD pyrophosphorylase; ...
 37-209 1.07e-11

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: 62.15  E-value: 1.07e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655374700  37 GKDSSVLLHLAR----KAFYPGKIPFPLLHVDTDWKFREMIRFRDQAAEKYGFELLVHKNPqglamgmnpftfgsakhtd 112
Cdd:cd23948   28 GKDCTVLLHLLRaalkRKYPSPLTPLKALYIKSPDPFPEVEEFVEDTAKRYNLDLITIDGP------------------- 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655374700 113 vMKtEGLKQALDKYG-FDAAFGGARRDeeksrakervysfrdrhhrwDP--KNQRPELWhTYNG--QVnkgesIRVFPLS 187
Cdd:cd23948   89 -MK-EGLEELLKEHPiIKAVFMGTRRT--------------------DPhgENLKPFSP-TDPGwpQF-----MRVNPIL 140

                        170       180
                 ....*....|....*....|..
gi 655374700 188 NWTELDIWQYIYQENIDIVPLY 209
Cdd:cd23948  141 DWSYHDVWEFLRTLNLPYCSLY 162
PAPS_reductase TIGR02057
phosphoadenosine phosphosulfate reductase, thioredoxin dependent; Requiring thioredoxin as an ...
 31-209 1.47e-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: 62.93  E-value: 1.47e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655374700   31 VMLYSIGKDSSVLLHLARKAFYPgkiPFPLLHVDTDWKFREMIRFRDQAAEKYGFELLVHKNPQGLAMGMNPFTFGSA-- 108
Cdd:TIGR02057  29 VQTSAFGIQALVTLHLLSSISEP---MIPVIFIDTLYHFPQTLTLKDELTKKYYQTLNLYKYDGCESEADFEAKYGKLlw 105

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655374700  109 -----KHTDVMKTEGLKQALDKYGFDAAFGGARRDEEKSRAKERVYSFRDRhhrwdpknqrpelwhtyNGQvnkgesIRV 183
Cdd:TIGR02057 106 qkdieKYDYIAKVEPMQRALKELNASAWFTGRRRDQGSARANLPVIEIDEQ-----------------NGI------LKV 162

                         170       180
                  ....*....|....*....|....*.
gi 655374700  184 FPLSNWTELDIWQYIYQENIDIVPLY 209
Cdd:TIGR02057 163 NPLIDWTFEQVYQYLDAHNVPYNPLL 188
AANH-like cd01986
adenine nucleotide alpha hydrolase (AANH)-like proteins; This group of adenine nucleotide ...
 30-99 2.49e-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: 50.14  E-value: 2.49e-08
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655374700  30 PVMLYSIGKDSSVLLHLARKAFYpgKIPFPLLHVDTDWKFREMIRFRDQAAEKYGFELLVHKNPQGLAMG 99
Cdd:cd01986    1 VVVGYSGGKDSSVALHLASRLGR--KAEVAVVHIDHGIGFKEEAESVASIARRSILKKLAEKGARAIATG 68
PRK08557 PRK08557
hypothetical protein; Provisional
 9-209 3.03e-07

hypothetical protein; Provisional


Pssm-ID: 181465 [Multi-domain]  Cd Length: 417  Bit Score: 51.29  E-value: 3.03e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655374700   9 LEQLEAESIQIFREVAAEFDNPVML----YSIGKDSSVLLHLARKAfypgkIP-FPLLHVDTDWKFREMIRFRDQAAEKY 83
Cdd:PRK08557 159 IEKLEENSLSILKDYIEKYKNKGYAinasFSGGKDSSVSTLLAKEV-----IPdLEVIFIDTGLEYPETINYVKDFAKKY 233

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655374700  84 GFELLVHK--------NPQGLAMGMNPFTfgsakhTDVMKTEGLKQALDK-YGFDAAF--GGARRDEEKSRAK---ERVY 149
Cdd:PRK08557 234 DLNLDTLDgdnfwenlEKEGIPTKDNRWC------NSACKLMPLKEYLKKkYGNKKVLtiDGSRKYESFTRANldyERKS 307

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 655374700 150 SFRDrhhrwdpkNQrpelwhtyngqvnkgesIRVFPLSNWTELDIWQYIYQENIDIVPLY 209
Cdd:PRK08557 308 GFID--------FQ-----------------TNVFPILDWNSLDIWSYIYLNDILYNPLY 342
PRK08576 PRK08576
hypothetical protein; Provisional
 7-211 1.06e-06

hypothetical protein; Provisional


Pssm-ID: 236300 [Multi-domain]  Cd Length: 438  Bit Score: 49.69  E-value: 1.06e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655374700   7 SHLEQLEAESIQIFREVaaEFDNPVMLYSIGKDSSVLLHLARKAFypGKIPfpLLHVDTDWKFREMIRFRDQAAEKYGFE 86
Cdd:PRK08576 216 EVLEAFEKASIKFLRKF--EEWTVIVPWSGGKDSTAALLLAKKAF--GDVT--AVYVDTGYEMPLTDEYVEKVAEKLGVD 289

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655374700  87 LLVhknpQGLAMGMNPFTFGSAKHTD----VMKTEGLKQALDKYGFDAAFGGARRDEEKSRAKervysfrdrhhrwdpkn 162
Cdd:PRK08576 290 LIR----AGVDVPMPIEKYGMPTHSNrwctKLKVEALEEAIRELEDGLLVVGDRDGESARRRL----------------- 348

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 655374700 163 qRPELWHTYNgqvNKGESIRVFPLSNWTELDIWQYIYQENIDIVPLYFA 211
Cdd:PRK08576 349 -RPPVVERKT---NFGKILVVMPIKFWSGAMVQLYILMNGLELNPLYYK 393
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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