NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1827956745|ref|WP_167399487|]
View 

MULTISPECIES: sulfate adenylyltransferase subunit CysD [Pseudomonas]

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

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
PRK05253 PRK05253
sulfate adenylyltransferase subunit CysD;
16-314 0e+00

sulfate adenylyltransferase subunit CysD;


:

Pssm-ID: 235375  Cd Length: 301  Bit Score: 631.79  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827956745  16 PMLTHLQWLEAESIQIIREVVAECENPVMLYSIGKDSAVMLHLAMKAFAPGKPPFPLLHVDTTWKFREMITFRDQTASRL 95
Cdd:PRK05253    4 YRLTHLDQLEAESIHILREVAAEFENPVMLYSIGKDSSVMLHLARKAFYPGKLPFPLLHVDTGWKFPEMIEFRDRRAKEL 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827956745  96 GLELLVHVNPEGVEKAIDPFTHGSALHTDVWKTQGLKQALDHYGFDAAFGGARRDEEKSRAKERMFSLRSEQHRWDPKQQ 175
Cdd:PRK05253   84 GLELIVHSNPEGIARGINPFRHGSAKHTNAMKTEGLKQALEKYGFDAAFGGARRDEEKSRAKERIFSFRDEFGQWDPKNQ 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827956745 176 RPELWRLYNTRKRKGESLRVFPLSNWTELDIWQYIYLEQIPIVPLYFAKERPVVQRDGTLIMVDDeRLPLRPGETPQMRK 255
Cdd:PRK05253  164 RPELWNLYNGRINKGEHIRVFPLSNWTELDIWQYIERENIPIVPLYFAHERPVVERDGMLIMVDD-RMPLRPGEVVEERM 242

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1827956745 256 VRFRTLGCYPLTGAIDSDADNLPAIISEMLVSRTSERQGRLIDSDSAGSMEKKKQEGYF 314
Cdd:PRK05253  243 VRFRTLGCYPCTGAVESEAATLEEIIAEMLVTRTSERGGRAIDDDQEASMEKRKREGYF 301
 
Name Accession Description Interval E-value
PRK05253 PRK05253
sulfate adenylyltransferase subunit CysD;
16-314 0e+00

sulfate adenylyltransferase subunit CysD;


Pssm-ID: 235375  Cd Length: 301  Bit Score: 631.79  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827956745  16 PMLTHLQWLEAESIQIIREVVAECENPVMLYSIGKDSAVMLHLAMKAFAPGKPPFPLLHVDTTWKFREMITFRDQTASRL 95
Cdd:PRK05253    4 YRLTHLDQLEAESIHILREVAAEFENPVMLYSIGKDSSVMLHLARKAFYPGKLPFPLLHVDTGWKFPEMIEFRDRRAKEL 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827956745  96 GLELLVHVNPEGVEKAIDPFTHGSALHTDVWKTQGLKQALDHYGFDAAFGGARRDEEKSRAKERMFSLRSEQHRWDPKQQ 175
Cdd:PRK05253   84 GLELIVHSNPEGIARGINPFRHGSAKHTNAMKTEGLKQALEKYGFDAAFGGARRDEEKSRAKERIFSFRDEFGQWDPKNQ 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827956745 176 RPELWRLYNTRKRKGESLRVFPLSNWTELDIWQYIYLEQIPIVPLYFAKERPVVQRDGTLIMVDDeRLPLRPGETPQMRK 255
Cdd:PRK05253  164 RPELWNLYNGRINKGEHIRVFPLSNWTELDIWQYIERENIPIVPLYFAHERPVVERDGMLIMVDD-RMPLRPGEVVEERM 242

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1827956745 256 VRFRTLGCYPLTGAIDSDADNLPAIISEMLVSRTSERQGRLIDSDSAGSMEKKKQEGYF 314
Cdd:PRK05253  243 VRFRTLGCYPCTGAVESEAATLEEIIAEMLVTRTSERGGRAIDDDQEASMEKRKREGYF 301
CysD TIGR02039
sulfate adenylyltransferase, small subunit; Metabolic assimilation of sulfur from inorganic ...
 21-314 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: 535.86  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827956745  21 LQWLEAESIQIIREVVAECENPVMLYSIGKDSAVMLHLAMKAFAPGKPPFPLLHVDTTWKFREMITFRDQTASRLGLELL 100
Cdd:TIGR02039   1 LRALESEAIHIIREVAAEFERPVMLYSIGKDSSVLLHLARKAFYPGPLPFPLLHVDTGWKFREMIAFRDHMVAKYGLRLI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827956745 101 VHVNPEGVEKAIDPFTHGSALHTDVWKTQGLKQALDHYGFDAAFGGARRDEEKSRAKERMFSLRSEQHRWDPKQQRPELW 180
Cdd:TIGR02039  81 VHSNEEGIADGINPFTEGSALHTDIMKTEALRQALDKNQFDAAFGGARRDEEKSRAKERIFSFRNAFHQWDPKKQRPELW 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827956745 181 RLYNTRKRKGESLRVFPLSNWTELDIWQYIYLEQIPIVPLYFAKERPVVQRDGTLIMVDDERLPLRPGETPQMRKVRFRT 260
Cdd:TIGR02039 161 NLYNGRISKGESVRVFPLSNWTELDIWRYIAAENIPIVPLYFAAKRPVVQRDGMLIMVDDVRMPLAPGEVVKERMVRFRT 240

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1827956745 261 LGCYPLTGAIDSDADNLPAIISEMLVSRTSERQGRLIDSDSAGSMEKKKQEGYF 314
Cdd:TIGR02039 241 LGCYPLTGAIESDAATVEEIIAETAAARTSERQGRAIDRDQAASMEDKKREGYF 294
Sulfate_adenylyltransferase_2 cd23946
Sulfate adenylyltransferase subunit 2; Sulfate adenylyltransferase subunits 1 and 2 form ATP ...
 20-233 5.93e-145

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: 406.88  E-value: 5.93e-145
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827956745  20 HLQWLEAESIQIIREVVAECENPVMLYSIGKDSAVMLHLAMKAFAPGKPPFPLLHVDTTWKFREMITFRDQTASRLGLEL 99
Cdd:cd23946     1 HLRQLEAESIHIIREVAAEFSNPVMLYSIGKDSSVMLHLARKAFYPGKPPFPLLHVDTTWKFREMIEFRDRVAKEYGLDL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827956745 100 LVHVNPEGVEKAIDPFTHGSALHTDVWKTQGLKQALDHYGFDAAFGGARRDEEKSRAKERMFSLRSEQHRWDPKQQRPEL 179
Cdd:cd23946    81 IVHVNPDGVEAGINPFTHGSAKHTDIMKTEGLKQALDKYGFDAAFGGARRDEEKSRAKERVYSFRDSNHRWDPKNQRPEL 160

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1827956745 180 WRLYNTRKRKGESLRVFPLSNWTELDIWQYIYLEQIPIVPLYFAKERPVVQRDG 233
Cdd:cd23946   161 WNQYNGRVKKGESIRVFPLSNWTELDIWQYIYLENIPIVPLYFAAERPVIERDG 214
CysD COG0175
3'-phosphoadenosine 5'-phosphosulfate sulfotransferase (PAPS reductase)/FAD synthetase or ...
 17-312 2.01e-80

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: 243.60  E-value: 2.01e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827956745  17 MLTHL-QWLEAESIQIIREVVAEC-ENPVMLYSIGKDSAVMLHLAMKAfapgKPPFPLLHVDTTWKFREMITFRDQTASR 94
Cdd:COG0175     9 LLEELnAELEAEAIEILREAAAEFgGRVVVSSSGGKDSTVLLHLAAKF----KPPIPVLFLDTGYEFPETYEFRDRLAER 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827956745  95 LGLELLVHVNPEGVEKA-----IDPFTHGSALHTDVWKTQGLKQALDHYGFDAAFGGARRDEEKSRAKERMFSlrseqhr 169
Cdd:COG0175    85 LGLDLIVVRPEDAFAEQlaefgPPLFYRDPRWCCKIRKVEPLKRALAGYDFDAWITGLRRDESPTRAKEPVVE------- 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827956745 170 WDPkqqrpelwrlyntrkrKGESLRVFPLSNWTELDIWQYIYLEQIPIVPLYFakerpvvqrdgtlimvdderlplrpge 249
Cdd:COG0175   158 WDP----------------VGGLIKVNPLADWTELDVWAYIRREDLPYNPLYD--------------------------- 194

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1827956745 250 tpqmrkVRFRTLGCYPLTGAIDSDADnlpaiisemlvsrtsERQGRLIDSDSAgsmekKKQEG 312
Cdd:COG0175   195 ------QGYPSIGCAPCTRAVESGED---------------ERAGRWWDEEKE-----RKECG 231
PAPS_reduct pfam01507
Phosphoadenosine phosphosulfate reductase family; This domain is found in phosphoadenosine ...
 41-269 1.27e-67

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: 208.69  E-value: 1.27e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827956745  41 NPVMLYSIGKDSAVMLHLAMKAFapgkPPFPLLHVDTTWKFREMITFRDQTASRLGLELLVHVNPEGVEKAIDPFTHGSA 120
Cdd:pfam01507   1 ELVVSFSGGKDSLVLLHLASKAF----PPGPVIFIDTGYEFPETYEFVDELEEKYGLNLKVYLPEDSFAEGINPEGIPSS 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827956745 121 L---HTDVWKTQGLKQALDHYGFDAAFGGARRDEEKSRAKERMFSLRSEQHRwdpkqqrpelwrlyntrkrkgeSLRVFP 197
Cdd:pfam01507  77 LyrrCCRLRKVEPLKRALKELGFDAWFTGLRRDESPSRAKLPIVSIDGDFPK----------------------VIKVFP 134

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1827956745 198 LSNWTELDIWQYIYLEQIPIVPLYFAKerpvvqrdgtlimvdderlplrpgetpqmrkvrFRTLGCYPLTGA 269
Cdd:pfam01507 135 LLNWTETDVWQYILANNVPYNPLYDQG---------------------------------YRSIGCYPCTGP 173
 
Name Accession Description Interval E-value
PRK05253 PRK05253
sulfate adenylyltransferase subunit CysD;
16-314 0e+00

sulfate adenylyltransferase subunit CysD;


Pssm-ID: 235375  Cd Length: 301  Bit Score: 631.79  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827956745  16 PMLTHLQWLEAESIQIIREVVAECENPVMLYSIGKDSAVMLHLAMKAFAPGKPPFPLLHVDTTWKFREMITFRDQTASRL 95
Cdd:PRK05253    4 YRLTHLDQLEAESIHILREVAAEFENPVMLYSIGKDSSVMLHLARKAFYPGKLPFPLLHVDTGWKFPEMIEFRDRRAKEL 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827956745  96 GLELLVHVNPEGVEKAIDPFTHGSALHTDVWKTQGLKQALDHYGFDAAFGGARRDEEKSRAKERMFSLRSEQHRWDPKQQ 175
Cdd:PRK05253   84 GLELIVHSNPEGIARGINPFRHGSAKHTNAMKTEGLKQALEKYGFDAAFGGARRDEEKSRAKERIFSFRDEFGQWDPKNQ 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827956745 176 RPELWRLYNTRKRKGESLRVFPLSNWTELDIWQYIYLEQIPIVPLYFAKERPVVQRDGTLIMVDDeRLPLRPGETPQMRK 255
Cdd:PRK05253  164 RPELWNLYNGRINKGEHIRVFPLSNWTELDIWQYIERENIPIVPLYFAHERPVVERDGMLIMVDD-RMPLRPGEVVEERM 242

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1827956745 256 VRFRTLGCYPLTGAIDSDADNLPAIISEMLVSRTSERQGRLIDSDSAGSMEKKKQEGYF 314
Cdd:PRK05253  243 VRFRTLGCYPCTGAVESEAATLEEIIAEMLVTRTSERGGRAIDDDQEASMEKRKREGYF 301
PRK12563 PRK12563
sulfate adenylyltransferase subunit CysD;
14-314 0e+00

sulfate adenylyltransferase subunit CysD;


Pssm-ID: 237138  Cd Length: 312  Bit Score: 604.86  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827956745  14 RYPMLTHLQWLEAESIQIIREVVAECENPVMLYSIGKDSAVMLHLAMKAFAPGKPPFPLLHVDTTWKFREMITFRDQTAS 93
Cdd:PRK12563   12 STSRMGHLDRLEAESIHILREVVAECSKPVMLYSIGKDSVVMLHLAMKAFRPTRPPFPLLHVDTTWKFREMIDFRDRRAK 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827956745  94 RLGLELLVHVNPEGVEKAIDPFTHGSALHTDVWKTQGLKQALDHYGFDAAFGGARRDEEKSRAKERMFSLRSEQHRWDPK 173
Cdd:PRK12563   92 ELGLDLVVHHNPDGIARGIVPFRHGSALHTDVAKTQGLKQALDHHGFDAAIGGARRDEEKSRAKERIFSFRSAFHRWDPK 171

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827956745 174 QQRPELWRLYNTRKRKGESLRVFPLSNWTELDIWQYIYLEQIPIVPLYFAKERPVVQRDGTLIMVDDERLPLRPGETPQM 253
Cdd:PRK12563  172 AQRPELWSLYNARLRRGESLRVFPLSNWTELDVWQYIAREKIPLVPLYFAKRRPVVERDGLLIMVDDERTPLRPGETPQQ 251

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1827956745 254 RKVRFRTLGCYPLTGAIDSDADNLPAIISEMLVSRTSERQGRLIDSDSAGSMEKKKQEGYF 314
Cdd:PRK12563  252 RKVRFRTLGCYPLTGAVESDADTVEKIIQEMAVTRISERQGRMIDQDSAASMEKKKKEGYF 312
CysD TIGR02039
sulfate adenylyltransferase, small subunit; Metabolic assimilation of sulfur from inorganic ...
 21-314 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: 535.86  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827956745  21 LQWLEAESIQIIREVVAECENPVMLYSIGKDSAVMLHLAMKAFAPGKPPFPLLHVDTTWKFREMITFRDQTASRLGLELL 100
Cdd:TIGR02039   1 LRALESEAIHIIREVAAEFERPVMLYSIGKDSSVLLHLARKAFYPGPLPFPLLHVDTGWKFREMIAFRDHMVAKYGLRLI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827956745 101 VHVNPEGVEKAIDPFTHGSALHTDVWKTQGLKQALDHYGFDAAFGGARRDEEKSRAKERMFSLRSEQHRWDPKQQRPELW 180
Cdd:TIGR02039  81 VHSNEEGIADGINPFTEGSALHTDIMKTEALRQALDKNQFDAAFGGARRDEEKSRAKERIFSFRNAFHQWDPKKQRPELW 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827956745 181 RLYNTRKRKGESLRVFPLSNWTELDIWQYIYLEQIPIVPLYFAKERPVVQRDGTLIMVDDERLPLRPGETPQMRKVRFRT 260
Cdd:TIGR02039 161 NLYNGRISKGESVRVFPLSNWTELDIWRYIAAENIPIVPLYFAAKRPVVQRDGMLIMVDDVRMPLAPGEVVKERMVRFRT 240

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1827956745 261 LGCYPLTGAIDSDADNLPAIISEMLVSRTSERQGRLIDSDSAGSMEKKKQEGYF 314
Cdd:TIGR02039 241 LGCYPLTGAIESDAATVEEIIAETAAARTSERQGRAIDRDQAASMEDKKREGYF 294
Sulfate_adenylyltransferase_2 cd23946
Sulfate adenylyltransferase subunit 2; Sulfate adenylyltransferase subunits 1 and 2 form ATP ...
 20-233 5.93e-145

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: 406.88  E-value: 5.93e-145
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827956745  20 HLQWLEAESIQIIREVVAECENPVMLYSIGKDSAVMLHLAMKAFAPGKPPFPLLHVDTTWKFREMITFRDQTASRLGLEL 99
Cdd:cd23946     1 HLRQLEAESIHIIREVAAEFSNPVMLYSIGKDSSVMLHLARKAFYPGKPPFPLLHVDTTWKFREMIEFRDRVAKEYGLDL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827956745 100 LVHVNPEGVEKAIDPFTHGSALHTDVWKTQGLKQALDHYGFDAAFGGARRDEEKSRAKERMFSLRSEQHRWDPKQQRPEL 179
Cdd:cd23946    81 IVHVNPDGVEAGINPFTHGSAKHTDIMKTEGLKQALDKYGFDAAFGGARRDEEKSRAKERVYSFRDSNHRWDPKNQRPEL 160

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1827956745 180 WRLYNTRKRKGESLRVFPLSNWTELDIWQYIYLEQIPIVPLYFAKERPVVQRDG 233
Cdd:cd23946   161 WNQYNGRVKKGESIRVFPLSNWTELDIWQYIYLENIPIVPLYFAAERPVIERDG 214
CysD COG0175
3'-phosphoadenosine 5'-phosphosulfate sulfotransferase (PAPS reductase)/FAD synthetase or ...
 17-312 2.01e-80

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: 243.60  E-value: 2.01e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827956745  17 MLTHL-QWLEAESIQIIREVVAEC-ENPVMLYSIGKDSAVMLHLAMKAfapgKPPFPLLHVDTTWKFREMITFRDQTASR 94
Cdd:COG0175     9 LLEELnAELEAEAIEILREAAAEFgGRVVVSSSGGKDSTVLLHLAAKF----KPPIPVLFLDTGYEFPETYEFRDRLAER 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827956745  95 LGLELLVHVNPEGVEKA-----IDPFTHGSALHTDVWKTQGLKQALDHYGFDAAFGGARRDEEKSRAKERMFSlrseqhr 169
Cdd:COG0175    85 LGLDLIVVRPEDAFAEQlaefgPPLFYRDPRWCCKIRKVEPLKRALAGYDFDAWITGLRRDESPTRAKEPVVE------- 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827956745 170 WDPkqqrpelwrlyntrkrKGESLRVFPLSNWTELDIWQYIYLEQIPIVPLYFakerpvvqrdgtlimvdderlplrpge 249
Cdd:COG0175   158 WDP----------------VGGLIKVNPLADWTELDVWAYIRREDLPYNPLYD--------------------------- 194

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1827956745 250 tpqmrkVRFRTLGCYPLTGAIDSDADnlpaiisemlvsrtsERQGRLIDSDSAgsmekKKQEG 312
Cdd:COG0175   195 ------QGYPSIGCAPCTRAVESGED---------------ERAGRWWDEEKE-----RKECG 231
PAPS_reduct pfam01507
Phosphoadenosine phosphosulfate reductase family; This domain is found in phosphoadenosine ...
 41-269 1.27e-67

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: 208.69  E-value: 1.27e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827956745  41 NPVMLYSIGKDSAVMLHLAMKAFapgkPPFPLLHVDTTWKFREMITFRDQTASRLGLELLVHVNPEGVEKAIDPFTHGSA 120
Cdd:pfam01507   1 ELVVSFSGGKDSLVLLHLASKAF----PPGPVIFIDTGYEFPETYEFVDELEEKYGLNLKVYLPEDSFAEGINPEGIPSS 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827956745 121 L---HTDVWKTQGLKQALDHYGFDAAFGGARRDEEKSRAKERMFSLRSEQHRwdpkqqrpelwrlyntrkrkgeSLRVFP 197
Cdd:pfam01507  77 LyrrCCRLRKVEPLKRALKELGFDAWFTGLRRDESPSRAKLPIVSIDGDFPK----------------------VIKVFP 134

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1827956745 198 LSNWTELDIWQYIYLEQIPIVPLYFAKerpvvqrdgtlimvdderlplrpgetpqmrkvrFRTLGCYPLTGA 269
Cdd:pfam01507 135 LLNWTETDVWQYILANNVPYNPLYDQG---------------------------------YRSIGCYPCTGP 173
PAPS_reductase-like_YbdN cd23947
uncharacterized phosphoadenosine phosphosulfate reductase-like proteins, similar to ...
 32-221 7.83e-19

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: 82.82  E-value: 7.83e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827956745  32 IREVVAECENPVMLYSIGKDSAVMLHLAMKAFAPGKPPFPLLHVDTTWKFREMITFRDQTASRLGLELLVHVNPEGVEKA 111
Cdd:cd23947     5 IRKVFEEFDPVIVSFSGGKDSLVLLHLALEALRRLRKDVYVVFIDTGIEFPETIDFVEKLAETLGLDVEAARPPLFLEWL 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827956745 112 IDPFTHGSALH-------------TDVWKTQGLKQAL-DHYGFDAAFG-GARRDEEKSRAKErmfslrseqhrwdPKQQR 176
Cdd:cd23947    85 TSNFQPQWDPIwdnpppprdyrwcCDELKLEPFTKWLkEKKPEGVLLLvGIRADESLNRAKR-------------PRVYR 151

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1827956745 177 PELWRlyntRKRKGESLRVFPLSNWTELDIWQYIYLEQIPIVPLY 221
Cdd:cd23947   152 KYGWR----NSTLPGQIVAYPIKDWSVEDVWLYILRHGLPYNPLY 192
PRK13795 PRK13795
hypothetical protein; Provisional
 19-221 5.80e-16

hypothetical protein; Provisional


Pssm-ID: 237510 [Multi-domain]  Cd Length: 636  Bit Score: 78.11  E-value: 5.80e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827956745  19 THLQWLEAESIQIIREVVAECENPVML-YSIGKDSAVMLHLAMKAFapgkPPFPLLHVDTTWKFREMITFRDQTASRLGL 97
Cdd:PRK13795  222 KHLEEKEKEAVNFIRGVAEKYNLPVSVsFSGGKDSLVVLDLAREAL----KDFKAFFNNTGLEFPETVENVKEVAEEYGI 297

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827956745  98 ELLvhvnpegVEKAIDPFthgsalhtdvWktqglkQALDHYG---------------------FDAAFG-------GARR 149
Cdd:PRK13795  298 ELI-------EADAGDAF----------W------RAVEKFGppardyrwcckvcklgpitraIKENFPkgcltfvGQRK 354

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1827956745 150 DEEKSRAKermfSLRSEQHRWDPKQqrpelwrlyntrkrkgesLRVFPLSNWTELDIWQYIYLEQIPIVPLY 221
Cdd:PRK13795  355 YESFSRAK----SPRVWRNPWVPNQ------------------IGASPIQDWTALEVWLYIFWRKLPYNPLY 404
PAPS_reductase cd23945
Phosphoadenylyl-sulfate reductase (thioredoxin); Phosphoadenosine phosphosulfate (PAPS) ...
 29-222 2.86e-13

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: 66.85  E-value: 2.86e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827956745  29 IQIIREVVAECENPVMLYSIGKDSAVMLHLAMKAfapgKPPFPLLHVDTTWKFREMITFRDQTASRLGLELLVhVNPEGV 108
Cdd:cd23945     3 EILLWAAEEFGPKLVFATSFGAEDAVILDLLSKV----RPDIPVVFLDTGYLFPETYDLIDEVEARYGLNIEV-YFPEGT 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827956745 109 E--------KAIDPFTHGSALHTDVWKTQGLKQALDHYGFDAAFGGARRDEEKSRAKERMFSlrseqhrWDPKQQRpelw 180
Cdd:cd23945    78 EaeeealegGLNEFYLEDEERYDCCRKRKPFPLALALLGVKAWITGRRRDQSPTRANLPIVE-------VDEEGGL---- 146

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1827956745 181 rlyntrkrkgesLRVFPLSNWTELDIWQYIYLEQIPIVPLYF 222
Cdd:cd23945   147 ------------VKINPLADWTWEDVWAYIREHDLPYNPLHD 176
PRK02090 PRK02090
phosphoadenylyl-sulfate reductase;
25-221 3.58e-12

phosphoadenylyl-sulfate reductase;


Pssm-ID: 234997  Cd Length: 241  Bit Score: 64.86  E-value: 3.58e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827956745  25 EAESIQIIREVVAEC-ENPVMLYSIGKDSAVMLHLAMKAfapgKPPFPLLHVDTTWKFREMITFRDQTASRLGLELLVhV 103
Cdd:PRK02090   25 GASAQERLAWALENFgGRLALVSSFGAEDAVLLHLVAQV----DPDIPVIFLDTGYLFPETYRFIDELTERLLLNLKV-Y 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827956745 104 NPEgvEKAIDPFthgsALHTDVW--------------KTQGLKQALDhyGFDAAFGGARRDEEKSRAKERMFSlrseqhr 169
Cdd:PRK02090  100 RPD--ASAAEQE----ARYGGLWeqsvedrdeccrirKVEPLNRALA--GLDAWITGLRREQSGTRANLPVLE------- 164

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1827956745 170 WDPKQqrpelwrlyntrkrkgesLRVFPLSNWTELDIWQYIYLEQIPIVPLY 221
Cdd:PRK02090  165 IDGGR------------------FKINPLADWTNEDVWAYLKEHDLPYHPLV 198
PAPS_reductase TIGR02057
phosphoadenosine phosphosulfate reductase, thioredoxin dependent; Requiring thioredoxin as an ...
 43-221 8.40e-12

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: 63.70  E-value: 8.40e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827956745  43 VMLYSIGKDSAVMLHLAMKAFapgKPPFPLLHVDTTWKFREMITFRDQTASRLGLELLVHVnPEGVEKAIDpFT--HGSA 120
Cdd:TIGR02057  29 VQTSAFGIQALVTLHLLSSIS---EPMIPVIFIDTLYHFPQTLTLKDELTKKYYQTLNLYK-YDGCESEAD-FEakYGKL 103

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827956745 121 L-------HTDVWKTQGLKQALDHYGFDAAFGGARRDEEKSRAKERMFSLRSeqhrwdpkqqrpelwrlyntrkrKGESL 193
Cdd:TIGR02057 104 LwqkdiekYDYIAKVEPMQRALKELNASAWFTGRRRDQGSARANLPVIEIDE-----------------------QNGIL 160

                         170       180
                  ....*....|....*....|....*...
gi 1827956745 194 RVFPLSNWTELDIWQYIYLEQIPIVPLY 221
Cdd:TIGR02057 161 KVNPLIDWTFEQVYQYLDAHNVPYNPLL 188
PRK13794 PRK13794
hypothetical protein; Provisional
 25-221 1.08e-11

hypothetical protein; Provisional


Pssm-ID: 237509 [Multi-domain]  Cd Length: 479  Bit Score: 65.07  E-value: 1.08e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827956745  25 EAESIQIIREVVAECENPVML-YSIGKDSAVMLHLAMKAFaPGKppFPLLHVDTTWKFREMITFRDQTASRLGLELLVHV 103
Cdd:PRK13794  232 ERNSIGFIRNTAEKINKPVTVaYSGGKDSLATLLLALKAL-GIN--FPVLFNDTGLEFPETLENVEDVEKHYGLEIIRTK 308

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827956745 104 NP---EGVEK----AIDpfthgSALHTDVWKTQGLKQALDH-YGFDA-AFGGARRDEEKSRAKermfslrseqhrwdpkq 174
Cdd:PRK13794  309 SEefwEKLEEygppARD-----NRWCSEVCKLEPLGKLIDEkYEGEClSFVGQRKYESFNRSK----------------- 366

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1827956745 175 qRPELWRLYNTRKRkgesLRVFPLSNWTELDIWQYIYLEQIPIVPLY 221
Cdd:PRK13794  367 -KPRIWRNPYIKKQ----ILAAPILHWTAMHVWIYLFREKAPYNKLY 408
FAD_synthase cd23948
FAD synthase; FAD synthase (FMN:ATP adenylyl transferase (FMNAT); FAD pyrophosphorylase; ...
 27-221 3.05e-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: 61.00  E-value: 3.05e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827956745  27 ESIQIIREVVAecenpvmLYSI---------GKDSAVMLHLAM----KAFAPGKPPFPLLHVDTTWKFREMITFRDQTAS 93
Cdd:cd23948     4 SALEVIEEALD-------KYGPeeiaisfngGKDCTVLLHLLRaalkRKYPSPLTPLKALYIKSPDPFPEVEEFVEDTAK 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827956745  94 RLGLELLVHvnpEGVEKaidpfthgsalhtdvwktQGLKQALDHYG-FDAAFGGARRDEEKSRakermfSLRSEQ---HR 169
Cdd:cd23948    77 RYNLDLITI---DGPMK------------------EGLEELLKEHPiIKAVFMGTRRTDPHGE------NLKPFSptdPG 129

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1827956745 170 WdpkqqrPELwrlyntrkrkgesLRVFPLSNWTELDIWQYIYLEQIPIVPLY 221
Cdd:cd23948   130 W------PQF-------------MRVNPILDWSYHDVWEFLRTLNLPYCSLY 162
cysH TIGR00434
phosophoadenylyl-sulfate reductase (thioredoxin); This enzyme, involved in the assimilation of ...
 43-221 9.54e-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: 60.57  E-value: 9.54e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827956745  43 VMLYSIGKDSAVMLHLAMKAfapgKPPFPLLHVDTTWKFREMITFRDQTASRLGLELLVHVNPE-----GVEKAIDPFTH 117
Cdd:TIGR00434  17 VYSTSFGIQGAVLLDLVSKI----SPDIPVIFLDTGYHFPETYELIDELTERYPLNIKVYKPDLslaeqAAKYGDKLWEQ 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827956745 118 GSALHTDVWKTQGLKQALDHYGFDAAFGGARRDEEKSRAKERMFSLrseqhrwdpkqqrpelwrlyntrKRKGESLRVFP 197
Cdd:TIGR00434  93 DPNKYDYLRKVEPMHRALKELHASAWFTGLRRDQGPSRANLSILNI-----------------------DEKFGILKVLP 149

                         170       180
                  ....*....|....*....|....
gi 1827956745 198 LSNWTELDIWQYIYLEQIPIVPLY 221
Cdd:TIGR00434 150 LIDWTWKDVYQYIDAHNLPYNPLH 173
PRK08557 PRK08557
hypothetical protein; Provisional
 24-221 8.72e-08

hypothetical protein; Provisional


Pssm-ID: 181465 [Multi-domain]  Cd Length: 417  Bit Score: 53.22  E-value: 8.72e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827956745  24 LEAESIQIIREVVAECENPVML----YSIGKDSAVMLHLAMKAFapgkPPFPLLHVDTTWKFREMITFRDQTASRLGLEL 99
Cdd:PRK08557  162 LEENSLSILKDYIEKYKNKGYAinasFSGGKDSSVSTLLAKEVI----PDLEVIFIDTGLEYPETINYVKDFAKKYDLNL 237

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827956745 100 LV--------HVNPEGVEkaidpfTHGSALHTDVWKTQGLKQALD-HYGFDAAF--GGARRDEEKSRAK---ERMFSLRS 165
Cdd:PRK08557  238 DTldgdnfweNLEKEGIP------TKDNRWCNSACKLMPLKEYLKkKYGNKKVLtiDGSRKYESFTRANldyERKSGFID 311

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1827956745 166 EQhrwdpkqqrpelwrlyntrkrkgesLRVFPLSNWTELDIWQYIYLEQIPIVPLY 221
Cdd:PRK08557  312 FQ-------------------------TNVFPILDWNSLDIWSYIYLNDILYNPLY 342
PRK08576 PRK08576
hypothetical protein; Provisional
 24-243 4.86e-06

hypothetical protein; Provisional


Pssm-ID: 236300 [Multi-domain]  Cd Length: 438  Bit Score: 47.77  E-value: 4.86e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827956745  24 LEAESIQIIREVvaECENPVMLYSIGKDSAVMLHLAMKAFAPGKPpfplLHVDTTWKFREMITFRDQTASRLGLELLVhv 103
Cdd:PRK08576  221 FEKASIKFLRKF--EEWTVIVPWSGGKDSTAALLLAKKAFGDVTA----VYVDTGYEMPLTDEYVEKVAEKLGVDLIR-- 292

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827956745 104 npEGVEKAIDPFTHGSALHTDVW----KTQGLKQALDHYGFDAAFGGARRDEEKSRakermfSLRSeqhrwdPKQQRPEL 179
Cdd:PRK08576  293 --AGVDVPMPIEKYGMPTHSNRWctklKVEALEEAIRELEDGLLVVGDRDGESARR------RLRP------PVVERKTN 358

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1827956745 180 WrlyntrkrkGESLRVFPLSNWTELDIWQYIYLEQIPIVPLYFAK---------------ERPVVQRDGTLIMVDDERL 243
Cdd:PRK08576  359 F---------GKILVVMPIKFWSGAMVQLYILMNGLELNPLYYKGfyrlgcyicpslrswEIELLKRLPVLPLILKKRP 428
AANH-like cd01986
adenine nucleotide alpha hydrolase (AANH)-like proteins; This group of adenine nucleotide ...
 42-103 1.33e-05

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: 42.44  E-value: 1.33e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1827956745  42 PVMLYSIGKDSAVMLHLAMKAFapGKPPFPLLHVDTTWKFREMITF-----RDQTASRLGLELLVHV 103
Cdd:cd01986     1 VVVGYSGGKDSSVALHLASRLG--RKAEVAVVHIDHGIGFKEEAESvasiaRRSILKKLAEKGARAI 65
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH