|
Name |
Accession |
Description |
Interval |
E-value |
| PRK05253 |
PRK05253 |
sulfate adenylyltransferase subunit CysD; |
6-305 |
0e+00 |
|
sulfate adenylyltransferase subunit CysD;
Pssm-ID: 235375 Cd Length: 301 Bit Score: 533.18 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529146338 6 TDTTLSPHLRDLENESIHILREVAGQFDKIGLLFSGGKDSCVVFELARRAFAPATVPFELLHVDTGHNFPEVLDFRDRLV 85
Cdd:PRK05253 1 MDQYRLTHLDQLEAESIHILREVAAEFENPVMLYSIGKDSSVMLHLARKAFYPGKLPFPLLHVDTGWKFPEMIEFRDRRA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529146338 86 EETGARLHVAKVQDWIDRGELQERPDG--TRNPLQTVPLVETIADRGYDAVLGGARRDEERARAKERVFSVRDSFGGWDP 163
Cdd:PRK05253 81 KELGLELIVHSNPEGIARGINPFRHGSakHTNAMKTEGLKQALEKYGFDAAFGGARRDEEKSRAKERIFSFRDEFGQWDP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529146338 164 RRQRPELWSLYNGEKLPGENIRVFPISNWTETDIWEYIGARGIELPSIYFSHDREVFNRDGMWLTPGEWGGPGKDEQLEV 243
Cdd:PRK05253 161 KNQRPELWNLYNGRINKGEHIRVFPLSNWTELDIWQYIERENIPIVPLYFAHERPVVERDGMLIMVDDRMPLRPGEVVEE 240
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 529146338 244 RTVRYRTVGDMSCTGAVESDAASIDAVLAEISTSTLTERGATRADDRlSESAMEDRKKEGYF 305
Cdd:PRK05253 241 RMVRFRTLGCYPCTGAVESEAATLEEIIAEMLVTRTSERGGRAIDDD-QEASMEKRKREGYF 301
|
|
| CysD |
TIGR02039 |
sulfate adenylyltransferase, small subunit; Metabolic assimilation of sulfur from inorganic ... |
14-305 |
6.58e-147 |
|
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: 414.52 E-value: 6.58e-147
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529146338 14 LRDLENESIHILREVAGQFDKIGLLFSGGKDSCVVFELARRAFAPATVPFELLHVDTGHNFPEVLDFRDRLVEETGARLH 93
Cdd:TIGR02039 1 LRALESEAIHIIREVAAEFERPVMLYSIGKDSSVLLHLARKAFYPGPLPFPLLHVDTGWKFREMIAFRDHMVAKYGLRLI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529146338 94 VAKVQDWIDRG--ELQERPDGTRNPLQTVPLVETIADRGYDAVLGGARRDEERARAKERVFSVRDSFGGWDPRRQRPELW 171
Cdd:TIGR02039 81 VHSNEEGIADGinPFTEGSALHTDIMKTEALRQALDKNQFDAAFGGARRDEEKSRAKERIFSFRNAFHQWDPKKQRPELW 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529146338 172 SLYNGEKLPGENIRVFPISNWTETDIWEYIGARGIELPSIYFSHDREVFNRDGMWLTPG-EWGGPGKDEQLEVRTVRYRT 250
Cdd:TIGR02039 161 NLYNGRISKGESVRVFPLSNWTELDIWRYIAAENIPIVPLYFAAKRPVVQRDGMLIMVDdVRMPLAPGEVVKERMVRFRT 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 529146338 251 VGDMSCTGAVESDAASIDAVLAEISTSTLTERgATRADDRLSESAMEDRKKEGYF 305
Cdd:TIGR02039 241 LGCYPLTGAIESDAATVEEIIAETAAARTSER-QGRAIDRDQAASMEDKKREGYF 294
|
|
| Sulfate_adenylyltransferase_2 |
cd23946 |
Sulfate adenylyltransferase subunit 2; Sulfate adenylyltransferase subunits 1 and 2 form ATP ... |
13-224 |
4.44e-84 |
|
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: 252.03 E-value: 4.44e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529146338 13 HLRDLENESIHILREVAGQFDKIGLLFSGGKDSCVVFELARRAFAPATVPFELLHVDTGHNFPEVLDFRDRLVEETGARL 92
Cdd:cd23946 1 HLRQLEAESIHIIREVAAEFSNPVMLYSIGKDSSVMLHLARKAFYPGKPPFPLLHVDTTWKFREMIEFRDRVAKEYGLDL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529146338 93 HVAKVQDWIDRGeLQERPDGTR---NPLQTVPLVETIADRGYDAVLGGARRDEERARAKERVFSVRDSFGGWDPRRQRPE 169
Cdd:cd23946 81 IVHVNPDGVEAG-INPFTHGSAkhtDIMKTEGLKQALDKYGFDAAFGGARRDEEKSRAKERVYSFRDSNHRWDPKNQRPE 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 529146338 170 LWSLYNGEKLPGENIRVFPISNWTETDIWEYIGARGIELPSIYFSHDREVFNRDG 224
Cdd:cd23946 160 LWNQYNGRVKKGESIRVFPLSNWTELDIWQYIYLENIPIVPLYFAAERPVIERDG 214
|
|
| CysD |
COG0175 |
3'-phosphoadenosine 5'-phosphosulfate sulfotransferase (PAPS reductase)/FAD synthetase or ... |
2-262 |
2.24e-61 |
|
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: 194.68 E-value: 2.24e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529146338 2 TQTVTDTTLSPHL-RDLENESIHILREVAGQF-DKIGLLFSGGKDSCVVFELARRaFAPatvPFELLHVDTGHNFPEVLD 79
Cdd:COG0175 1 PLPATLDDLLEELnAELEAEAIEILREAAAEFgGRVVVSSSGGKDSTVLLHLAAK-FKP---PIPVLFLDTGYEFPETYE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529146338 80 FRDRLVEETGARLHVAKVQDWIDRGELQ-------ERPDGTRNPLQTVPLVETIADRGYDAVLGGARRDEERARAKERVF 152
Cdd:COG0175 77 FRDRLAERLGLDLIVVRPEDAFAEQLAEfgpplfyRDPRWCCKIRKVEPLKRALAGYDFDAWITGLRRDESPTRAKEPVV 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529146338 153 SvrdsfggWDPrrqrpelwslyngeklPGENIRVFPISNWTETDIWEYIGARGIELPSIYFshdrevfnrdgmwltpgew 232
Cdd:COG0175 157 E-------WDP----------------VGGLIKVNPLADWTELDVWAYIRREDLPYNPLYD------------------- 194
|
250 260 270
....*....|....*....|....*....|
gi 529146338 233 ggpgkdeqlevrtVRYRTVGDMSCTGAVES 262
Cdd:COG0175 195 -------------QGYPSIGCAPCTRAVES 211
|
|
| PAPS_reduct |
pfam01507 |
Phosphoadenosine phosphosulfate reductase family; This domain is found in phosphoadenosine ... |
34-259 |
3.83e-44 |
|
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: 148.60 E-value: 3.83e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529146338 34 KIGLLFSGGKDSCVVFELARRAFAPATVpfelLHVDTGHNFPEVLDFRDRLVEETGARLHVAKVQDWIDRGELQERPDGT 113
Cdd:pfam01507 1 ELVVSFSGGKDSLVLLHLASKAFPPGPV----IFIDTGYEFPETYEFVDELEEKYGLNLKVYLPEDSFAEGINPEGIPSS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529146338 114 -----RNPLQTVPLVETIADRGYDAVLGGARRDEERARAKERVFSVRDSFGGwdprrqrpelwslyngeklpgeNIRVFP 188
Cdd:pfam01507 77 lyrrcCRLRKVEPLKRALKELGFDAWFTGLRRDESPSRAKLPIVSIDGDFPK----------------------VIKVFP 134
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 529146338 189 ISNWTETDIWEYIGARGIELPSIYFSHdrevfnrdgmwltpgewggpgkdeqlevrtvrYRTVGDMSCTGA 259
Cdd:pfam01507 135 LLNWTETDVWQYILANNVPYNPLYDQG--------------------------------YRSIGCYPCTGP 173
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PRK05253 |
PRK05253 |
sulfate adenylyltransferase subunit CysD; |
6-305 |
0e+00 |
|
sulfate adenylyltransferase subunit CysD;
Pssm-ID: 235375 Cd Length: 301 Bit Score: 533.18 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529146338 6 TDTTLSPHLRDLENESIHILREVAGQFDKIGLLFSGGKDSCVVFELARRAFAPATVPFELLHVDTGHNFPEVLDFRDRLV 85
Cdd:PRK05253 1 MDQYRLTHLDQLEAESIHILREVAAEFENPVMLYSIGKDSSVMLHLARKAFYPGKLPFPLLHVDTGWKFPEMIEFRDRRA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529146338 86 EETGARLHVAKVQDWIDRGELQERPDG--TRNPLQTVPLVETIADRGYDAVLGGARRDEERARAKERVFSVRDSFGGWDP 163
Cdd:PRK05253 81 KELGLELIVHSNPEGIARGINPFRHGSakHTNAMKTEGLKQALEKYGFDAAFGGARRDEEKSRAKERIFSFRDEFGQWDP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529146338 164 RRQRPELWSLYNGEKLPGENIRVFPISNWTETDIWEYIGARGIELPSIYFSHDREVFNRDGMWLTPGEWGGPGKDEQLEV 243
Cdd:PRK05253 161 KNQRPELWNLYNGRINKGEHIRVFPLSNWTELDIWQYIERENIPIVPLYFAHERPVVERDGMLIMVDDRMPLRPGEVVEE 240
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 529146338 244 RTVRYRTVGDMSCTGAVESDAASIDAVLAEISTSTLTERGATRADDRlSESAMEDRKKEGYF 305
Cdd:PRK05253 241 RMVRFRTLGCYPCTGAVESEAATLEEIIAEMLVTRTSERGGRAIDDD-QEASMEKRKREGYF 301
|
|
| CysD |
TIGR02039 |
sulfate adenylyltransferase, small subunit; Metabolic assimilation of sulfur from inorganic ... |
14-305 |
6.58e-147 |
|
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: 414.52 E-value: 6.58e-147
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529146338 14 LRDLENESIHILREVAGQFDKIGLLFSGGKDSCVVFELARRAFAPATVPFELLHVDTGHNFPEVLDFRDRLVEETGARLH 93
Cdd:TIGR02039 1 LRALESEAIHIIREVAAEFERPVMLYSIGKDSSVLLHLARKAFYPGPLPFPLLHVDTGWKFREMIAFRDHMVAKYGLRLI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529146338 94 VAKVQDWIDRG--ELQERPDGTRNPLQTVPLVETIADRGYDAVLGGARRDEERARAKERVFSVRDSFGGWDPRRQRPELW 171
Cdd:TIGR02039 81 VHSNEEGIADGinPFTEGSALHTDIMKTEALRQALDKNQFDAAFGGARRDEEKSRAKERIFSFRNAFHQWDPKKQRPELW 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529146338 172 SLYNGEKLPGENIRVFPISNWTETDIWEYIGARGIELPSIYFSHDREVFNRDGMWLTPG-EWGGPGKDEQLEVRTVRYRT 250
Cdd:TIGR02039 161 NLYNGRISKGESVRVFPLSNWTELDIWRYIAAENIPIVPLYFAAKRPVVQRDGMLIMVDdVRMPLAPGEVVKERMVRFRT 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 529146338 251 VGDMSCTGAVESDAASIDAVLAEISTSTLTERgATRADDRLSESAMEDRKKEGYF 305
Cdd:TIGR02039 241 LGCYPLTGAIESDAATVEEIIAETAAARTSER-QGRAIDRDQAASMEDKKREGYF 294
|
|
| PRK12563 |
PRK12563 |
sulfate adenylyltransferase subunit CysD; |
7-305 |
7.09e-124 |
|
sulfate adenylyltransferase subunit CysD;
Pssm-ID: 237138 Cd Length: 312 Bit Score: 356.79 E-value: 7.09e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529146338 7 DTTLSPHLRDLENESIHILREVAGQFDKIGLLFSGGKDSCVVFELARRAFAPATVPFELLHVDTGHNFPEVLDFRDRLVE 86
Cdd:PRK12563 12 STSRMGHLDRLEAESIHILREVVAECSKPVMLYSIGKDSVVMLHLAMKAFRPTRPPFPLLHVDTTWKFREMIDFRDRRAK 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529146338 87 ETGARLHVAKVQDWIDRG--ELQERPDGTRNPLQTVPLVETIADRGYDAVLGGARRDEERARAKERVFSVRDSFGGWDPR 164
Cdd:PRK12563 92 ELGLDLVVHHNPDGIARGivPFRHGSALHTDVAKTQGLKQALDHHGFDAAIGGARRDEEKSRAKERIFSFRSAFHRWDPK 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529146338 165 RQRPELWSLYNGEKLPGENIRVFPISNWTETDIWEYIGARGIELPSIYFSHDREVFNRDGMW---------LTPGewggp 235
Cdd:PRK12563 172 AQRPELWSLYNARLRRGESLRVFPLSNWTELDVWQYIAREKIPLVPLYFAKRRPVVERDGLLimvddertpLRPG----- 246
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529146338 236 gkdEQLEVRTVRYRTVGDMSCTGAVESDAASIDAVLAEISTSTLTERGAtRADDRLSESAMEDRKKEGYF 305
Cdd:PRK12563 247 ---ETPQQRKVRFRTLGCYPLTGAVESDADTVEKIIQEMAVTRISERQG-RMIDQDSAASMEKKKKEGYF 312
|
|
| Sulfate_adenylyltransferase_2 |
cd23946 |
Sulfate adenylyltransferase subunit 2; Sulfate adenylyltransferase subunits 1 and 2 form ATP ... |
13-224 |
4.44e-84 |
|
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: 252.03 E-value: 4.44e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529146338 13 HLRDLENESIHILREVAGQFDKIGLLFSGGKDSCVVFELARRAFAPATVPFELLHVDTGHNFPEVLDFRDRLVEETGARL 92
Cdd:cd23946 1 HLRQLEAESIHIIREVAAEFSNPVMLYSIGKDSSVMLHLARKAFYPGKPPFPLLHVDTTWKFREMIEFRDRVAKEYGLDL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529146338 93 HVAKVQDWIDRGeLQERPDGTR---NPLQTVPLVETIADRGYDAVLGGARRDEERARAKERVFSVRDSFGGWDPRRQRPE 169
Cdd:cd23946 81 IVHVNPDGVEAG-INPFTHGSAkhtDIMKTEGLKQALDKYGFDAAFGGARRDEEKSRAKERVYSFRDSNHRWDPKNQRPE 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 529146338 170 LWSLYNGEKLPGENIRVFPISNWTETDIWEYIGARGIELPSIYFSHDREVFNRDG 224
Cdd:cd23946 160 LWNQYNGRVKKGESIRVFPLSNWTELDIWQYIYLENIPIVPLYFAAERPVIERDG 214
|
|
| CysD |
COG0175 |
3'-phosphoadenosine 5'-phosphosulfate sulfotransferase (PAPS reductase)/FAD synthetase or ... |
2-262 |
2.24e-61 |
|
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: 194.68 E-value: 2.24e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529146338 2 TQTVTDTTLSPHL-RDLENESIHILREVAGQF-DKIGLLFSGGKDSCVVFELARRaFAPatvPFELLHVDTGHNFPEVLD 79
Cdd:COG0175 1 PLPATLDDLLEELnAELEAEAIEILREAAAEFgGRVVVSSSGGKDSTVLLHLAAK-FKP---PIPVLFLDTGYEFPETYE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529146338 80 FRDRLVEETGARLHVAKVQDWIDRGELQ-------ERPDGTRNPLQTVPLVETIADRGYDAVLGGARRDEERARAKERVF 152
Cdd:COG0175 77 FRDRLAERLGLDLIVVRPEDAFAEQLAEfgpplfyRDPRWCCKIRKVEPLKRALAGYDFDAWITGLRRDESPTRAKEPVV 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529146338 153 SvrdsfggWDPrrqrpelwslyngeklPGENIRVFPISNWTETDIWEYIGARGIELPSIYFshdrevfnrdgmwltpgew 232
Cdd:COG0175 157 E-------WDP----------------VGGLIKVNPLADWTELDVWAYIRREDLPYNPLYD------------------- 194
|
250 260 270
....*....|....*....|....*....|
gi 529146338 233 ggpgkdeqlevrtVRYRTVGDMSCTGAVES 262
Cdd:COG0175 195 -------------QGYPSIGCAPCTRAVES 211
|
|
| PAPS_reduct |
pfam01507 |
Phosphoadenosine phosphosulfate reductase family; This domain is found in phosphoadenosine ... |
34-259 |
3.83e-44 |
|
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: 148.60 E-value: 3.83e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529146338 34 KIGLLFSGGKDSCVVFELARRAFAPATVpfelLHVDTGHNFPEVLDFRDRLVEETGARLHVAKVQDWIDRGELQERPDGT 113
Cdd:pfam01507 1 ELVVSFSGGKDSLVLLHLASKAFPPGPV----IFIDTGYEFPETYEFVDELEEKYGLNLKVYLPEDSFAEGINPEGIPSS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529146338 114 -----RNPLQTVPLVETIADRGYDAVLGGARRDEERARAKERVFSVRDSFGGwdprrqrpelwslyngeklpgeNIRVFP 188
Cdd:pfam01507 77 lyrrcCRLRKVEPLKRALKELGFDAWFTGLRRDESPSRAKLPIVSIDGDFPK----------------------VIKVFP 134
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 529146338 189 ISNWTETDIWEYIGARGIELPSIYFSHdrevfnrdgmwltpgewggpgkdeqlevrtvrYRTVGDMSCTGA 259
Cdd:pfam01507 135 LLNWTETDVWQYILANNVPYNPLYDQG--------------------------------YRSIGCYPCTGP 173
|
|
| PAPS_reductase-like_YbdN |
cd23947 |
uncharacterized phosphoadenosine phosphosulfate reductase-like proteins, similar to ... |
21-219 |
1.01e-21 |
|
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: 90.53 E-value: 1.01e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529146338 21 SIHILREVAGQFDKIGLLFSGGKDSCVVFELARRAFAPATVPFELLHVDTGHNFPEVLDFRDRLVEETGARLHVAKV--- 97
Cdd:cd23947 1 ALERIRKVFEEFDPVIVSFSGGKDSLVLLHLALEALRRLRKDVYVVFIDTGIEFPETIDFVEKLAETLGLDVEAARPplf 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529146338 98 QDWIDRGELQERPDGTRNPLQTVP---------------LVETIADRGYdAVLGGARRDEERARAKErvfsvrdsfggwd 162
Cdd:cd23947 81 LEWLTSNFQPQWDPIWDNPPPPRDyrwccdelklepftkWLKEKKPEGV-LLLVGIRADESLNRAKR------------- 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 529146338 163 PRRQRPELWSlyngEKLPGENIRVFPISNWTETDIWEYIGARGIELPSIYF-SHDREV 219
Cdd:cd23947 147 PRVYRKYGWR----NSTLPGQIVAYPIKDWSVEDVWLYILRHGLPYNPLYDlGFDRGG 200
|
|
| PRK13795 |
PRK13795 |
hypothetical protein; Provisional |
11-229 |
7.64e-16 |
|
hypothetical protein; Provisional
Pssm-ID: 237510 [Multi-domain] Cd Length: 636 Bit Score: 77.73 E-value: 7.64e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529146338 11 SPHLRDLENESIHILREVAGQFDK-IGLLFSGGKDSCVVFELARRAFapatVPFELLHVDTGHNFPEVLDFRDRLVEETG 89
Cdd:PRK13795 221 RKHLEEKEKEAVNFIRGVAEKYNLpVSVSFSGGKDSLVVLDLAREAL----KDFKAFFNNTGLEFPETVENVKEVAEEYG 296
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529146338 90 ARLHVAKVQDWIDR---------------------GelqerpdgtrnplqtvPLVETIADRGYDAVLG--GARRDEERAR 146
Cdd:PRK13795 297 IELIEADAGDAFWRavekfgppardyrwcckvcklG----------------PITRAIKENFPKGCLTfvGQRKYESFSR 360
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529146338 147 AK-ERVfsvrdsfggWdprrQRPelWslyngekLPGEnIRVFPISNWTETDIWEYIGARGIELPSIYfshDREvFNRDGM 225
Cdd:PRK13795 361 AKsPRV---------W----RNP--W-------VPNQ-IGASPIQDWTALEVWLYIFWRKLPYNPLY---ERG-FDRIGC 413
|
....
gi 529146338 226 WLTP 229
Cdd:PRK13795 414 WLCP 417
|
|
| PAPS_reductase |
cd23945 |
Phosphoadenylyl-sulfate reductase (thioredoxin); Phosphoadenosine phosphosulfate (PAPS) ... |
24-206 |
5.84e-15 |
|
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: 71.47 E-value: 5.84e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529146338 24 ILREVAGQFDKIGLLFSGGKDSCVVFELARRAFAPATVPFellhVDTGHNFPEVLDFRDRLVEETGARLHVAK-----VQ 98
Cdd:cd23945 5 LLWAAEEFGPKLVFATSFGAEDAVILDLLSKVRPDIPVVF----LDTGYLFPETYDLIDEVEARYGLNIEVYFpegteAE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529146338 99 DWIDRGELQERPDGTRNPLQTVPLVETI----ADRGYDAVLGGARRDEERARAKERVFsvrdsfgGWDPRRQRpelwsly 174
Cdd:cd23945 81 EEALEGGLNEFYLEDEERYDCCRKRKPFplalALLGVKAWITGRRRDQSPTRANLPIV-------EVDEEGGL------- 146
|
170 180 190
....*....|....*....|....*....|..
gi 529146338 175 ngeklpgenIRVFPISNWTETDIWEYIGARGI 206
Cdd:cd23945 147 ---------VKINPLADWTWEDVWAYIREHDL 169
|
|
| FAD_synthase |
cd23948 |
FAD synthase; FAD synthase (FMN:ATP adenylyl transferase (FMNAT); FAD pyrophosphorylase; ... |
19-209 |
1.26e-13 |
|
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: 67.93 E-value: 1.26e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529146338 19 NESIHILREVAGQF--DKIGLLFSGGKDSCVVFELARRA----FAPATVPFELLHVDTGHNFPEVLDFRDRLVEETGARL 92
Cdd:cd23948 3 KSALEVIEEALDKYgpEEIAISFNGGKDCTVLLHLLRAAlkrkYPSPLTPLKALYIKSPDPFPEVEEFVEDTAKRYNLDL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529146338 93 HVakvqdwIDRGELqerpDGTRNPLQTVPLVEtiadrgydAVLGGARRDEERARaKERVFSVRDSfgGWdprrqrPELws 172
Cdd:cd23948 83 IT------IDGPMK----EGLEELLKEHPIIK--------AVFMGTRRTDPHGE-NLKPFSPTDP--GW------PQF-- 133
|
170 180 190
....*....|....*....|....*....|....*..
gi 529146338 173 lyngeklpgenIRVFPISNWTETDIWEYIgaRGIELP 209
Cdd:cd23948 134 -----------MRVNPILDWSYHDVWEFL--RTLNLP 157
|
|
| PRK08557 |
PRK08557 |
hypothetical protein; Provisional |
14-229 |
1.50e-09 |
|
hypothetical protein; Provisional
Pssm-ID: 181465 [Multi-domain] Cd Length: 417 Bit Score: 58.23 E-value: 1.50e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529146338 14 LRDLENESIHILREVAGQFDK----IGLLFSGGKDSCVVFELARRAFAPATVPFellhVDTGHNFPEVLDFRDRLVEETG 89
Cdd:PRK08557 159 IEKLEENSLSILKDYIEKYKNkgyaINASFSGGKDSSVSTLLAKEVIPDLEVIF----IDTGLEYPETINYVKDFAKKYD 234
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529146338 90 ARLHVAKVQDWIDrgELQERPDGTRN------PLQTVPLVETIADR-GYDAVL--GGARRDEERARAK---ERVFSVRDS 157
Cdd:PRK08557 235 LNLDTLDGDNFWE--NLEKEGIPTKDnrwcnsACKLMPLKEYLKKKyGNKKVLtiDGSRKYESFTRANldyERKSGFIDF 312
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 529146338 158 fggwdprrqrpelwslyngeklpgeNIRVFPISNWTETDIWEYIGARGIELPSIYfshdREVFNRDGMWLTP 229
Cdd:PRK08557 313 -------------------------QTNVFPILDWNSLDIWSYIYLNDILYNPLY----DKGFERIGCYLCP 355
|
|
| PRK08576 |
PRK08576 |
hypothetical protein; Provisional |
14-232 |
6.75e-09 |
|
hypothetical protein; Provisional
Pssm-ID: 236300 [Multi-domain] Cd Length: 438 Bit Score: 56.24 E-value: 6.75e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529146338 14 LRDLENESIHILREVAGqfDKIGLLFSGGKDSCVVFELARRAFAPATVpfelLHVDTGHNFPEvldfRDRLVEETGARLH 93
Cdd:PRK08576 218 LEAFEKASIKFLRKFEE--WTVIVPWSGGKDSTAALLLAKKAFGDVTA----VYVDTGYEMPL----TDEYVEKVAEKLG 287
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529146338 94 VAKVQDWIDRGELQER---PDG-----TRNPLQTvpLVETIADRGyDAVLGGARRDEERARakervfsvrdsfggwdpRR 165
Cdd:PRK08576 288 VDLIRAGVDVPMPIEKygmPTHsnrwcTKLKVEA--LEEAIRELE-DGLLVVGDRDGESAR-----------------RR 347
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 529146338 166 QRPelwSLYNGEKLPGENIRVFPISNWTETDIWEYIGARGIELPSIYFshdrEVFNRDGMWLTPG--EW 232
Cdd:PRK08576 348 LRP---PVVERKTNFGKILVVMPIKFWSGAMVQLYILMNGLELNPLYY----KGFYRLGCYICPSlrSW 409
|
|
| cysH |
TIGR00434 |
phosophoadenylyl-sulfate reductase (thioredoxin); This enzyme, involved in the assimilation of ... |
64-239 |
8.77e-09 |
|
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: 54.79 E-value: 8.77e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529146338 64 ELLHVDTGHNFPEVLDFRDRLVEETGARLHVAKVQDWIDR------GELQERPDGTRNPLQTV-PLVETIADRGYDAVLG 136
Cdd:TIGR00434 41 PVIFLDTGYHFPETYELIDELTERYPLNIKVYKPDLSLAEqaakygDKLWEQDPNKYDYLRKVePMHRALKELHASAWFT 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529146338 137 GARRDEERARAKERVFSVRDSFGgwdprrqrpelwslyngeklpgeNIRVFPISNWTETDIWEYIGARGIE--------L 208
Cdd:TIGR00434 121 GLRRDQGPSRANLSILNIDEKFG-----------------------ILKVLPLIDWTWKDVYQYIDAHNLPynplhdqgY 177
|
170 180 190
....*....|....*....|....*....|..
gi 529146338 209 PSIYFSH-DREVFnrDGMWLTPGEWGGPGKDE 239
Cdd:TIGR00434 178 PSIGDYHsTRPVK--EGEDERAGRWKGKAKTE 207
|
|
| PRK02090 |
PRK02090 |
phosphoadenylyl-sulfate reductase; |
10-206 |
2.02e-08 |
|
phosphoadenylyl-sulfate reductase;
Pssm-ID: 234997 Cd Length: 241 Bit Score: 54.07 E-value: 2.02e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529146338 10 LSPHLRDLEneSIHILREVAGQF-DKIGLLFSGGKDSCVVFELARRAFAPATVPFellhVDTGHNFPEVLDFRDRLVE-- 86
Cdd:PRK02090 19 LNAELEGAS--AQERLAWALENFgGRLALVSSFGAEDAVLLHLVAQVDPDIPVIF----LDTGYLFPETYRFIDELTErl 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529146338 87 ----------ETGARLHVAKVQDWIDRGELQERPDGTR--NPLQTvplvetiADRGYDAVLGGARRDEERARAKERVFSv 154
Cdd:PRK02090 93 llnlkvyrpdASAAEQEARYGGLWEQSVEDRDECCRIRkvEPLNR-------ALAGLDAWITGLRREQSGTRANLPVLE- 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 529146338 155 rdsfggWDPRRqrpelwslyngeklpgenIRVFPISNWTETDIWEYIGARGI 206
Cdd:PRK02090 165 ------IDGGR------------------FKINPLADWTNEDVWAYLKEHDL 192
|
|
| PAPS_reductase |
TIGR02057 |
phosphoadenosine phosphosulfate reductase, thioredoxin dependent; Requiring thioredoxin as an ... |
62-206 |
2.11e-08 |
|
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: 53.68 E-value: 2.11e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529146338 62 PFELLHVDTGHNFPEVLDFRDRLVEETGARLHVAKVQDWIDR-------GELQERPDGTRnpLQTVPLVETiADRGYD-- 132
Cdd:TIGR02057 52 MIPVIFIDTLYHFPQTLTLKDELTKKYYQTLNLYKYDGCESEadfeakyGKLLWQKDIEK--YDYIAKVEP-MQRALKel 128
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 529146338 133 ---AVLGGARRDEERARAKERVFSVRDSFGgwdprrqrpelwslyngeklpgeNIRVFPISNWTETDIWEYIGARGI 206
Cdd:TIGR02057 129 nasAWFTGRRRDQGSARANLPVIEIDEQNG-----------------------ILKVNPLIDWTFEQVYQYLDAHNV 182
|
|
| PRK13794 |
PRK13794 |
hypothetical protein; Provisional |
14-201 |
6.71e-08 |
|
hypothetical protein; Provisional
Pssm-ID: 237509 [Multi-domain] Cd Length: 479 Bit Score: 53.52 E-value: 6.71e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529146338 14 LRDLENESIHILREVAGQFDK-IGLLFSGGKDSCVVFELARRAFApatVPFELLHVDTGHNFPEVLDFRDRLVEETGARL 92
Cdd:PRK13794 228 LDKYERNSIGFIRNTAEKINKpVTVAYSGGKDSLATLLLALKALG---INFPVLFNDTGLEFPETLENVEDVEKHYGLEI 304
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529146338 93 HVAKVQDWIDRGELQERPdgTRN------PLQTVPLVETIADRGYDAVLG--GARRDEERARAKervfsvrdsfggwdpr 164
Cdd:PRK13794 305 IRTKSEEFWEKLEEYGPP--ARDnrwcseVCKLEPLGKLIDEKYEGECLSfvGQRKYESFNRSK---------------- 366
|
170 180 190
....*....|....*....|....*....|....*..
gi 529146338 165 rqRPELWSLYNGEKlpgeNIRVFPISNWTETDIWEYI 201
Cdd:PRK13794 367 --KPRIWRNPYIKK----QILAAPILHWTAMHVWIYL 397
|
|
| TilS |
COG0037 |
tRNA(Ile)-lysidine synthase TilS/MesJ [Translation, ribosomal structure and biogenesis]; tRNA ... |
33-94 |
2.79e-04 |
|
tRNA(Ile)-lysidine synthase TilS/MesJ [Translation, ribosomal structure and biogenesis]; tRNA(Ile)-lysidine synthase TilS/MesJ is part of the Pathway/BioSystem: tRNA modification
Pssm-ID: 439807 [Multi-domain] Cd Length: 235 Bit Score: 41.36 E-value: 2.79e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 529146338 33 DKIGLLFSGGKDSCVVFELARRAFAPATVPFELLHVDtgHNFPEVLDFRDRLVEETGARLHV 94
Cdd:COG0037 16 DRILVAVSGGKDSLALLHLLAKLRRRLGFELVAVHVD--HGLREESDEDAEFVAELCEELGI 75
|
|
| TtcA-like |
cd24138 |
tRNA-cytidine(32) 2-sulfurtransferase and similar proteins; tRNA-cytidine(32) ... |
33-110 |
6.74e-04 |
|
tRNA-cytidine(32) 2-sulfurtransferase and similar proteins; tRNA-cytidine(32) 2-sulfurtransferase, also called two-thiocytidine biosynthesis protein A or tRNA 2-thiocytidine biosynthesis protein TtcA, catalyzes the ATP-dependent 2-thiolation of cytidine in position 32 of tRNA, to form 2-thiocytidine (s(2)C32). TtcA belongs to the adenine nucleotide alpha hydrolase superfamily (AANH) that includes N-type ATP PPases and ATP sulfurylases. It forms an alpha/beta/alpha fold which binds to the adenosine group. This domain has a strongly conserved motif SGGKD at the N-terminus.
Pssm-ID: 467514 [Multi-domain] Cd Length: 187 Bit Score: 39.95 E-value: 6.74e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529146338 33 DKIGLLFSGGKDS----CVVFELARRAFapatVPFEL--LHVDTG-HNFPEVLDFRDRLVEETGARLHVAkvqDWIDRGE 105
Cdd:cd24138 9 DRILVGLSGGKDSltllHLLEELKRRAP----IKFELvaVTVDPGyPGYRPPREELAEILEELGEILEDE---ESEIIII 81
|
....*
gi 529146338 106 LQERP 110
Cdd:cd24138 82 EKERE 86
|
|
| AANH-like |
cd01986 |
adenine nucleotide alpha hydrolase (AANH)-like proteins; This group of adenine nucleotide ... |
37-88 |
1.68e-03 |
|
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: 36.66 E-value: 1.68e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 529146338 37 LLFSGGKDSCVVFELARRAFAPAtvPFELLHVDTGHNFPEVLDFRDRLVEET 88
Cdd:cd01986 3 VGYSGGKDSSVALHLASRLGRKA--EVAVVHIDHGIGFKEEAESVASIARRS 52
|
|
| |
