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Conserved domains on  [gi|1997968265|ref|WP_206397054|]
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sulfate adenylyltransferase subunit CysD [Micrococcus luteus]

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;
21-311 0e+00

sulfate adenylyltransferase subunit CysD;


:

Pssm-ID: 235375  Cd Length: 301  Bit Score: 554.36  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997968265  21 DALEAEAIHIIREVVAEFERPAMLFSGGKDSVVMLHLAAKAFWPGRIPFPVVHVDTGHNFPEVLEFRDRTVERLGLRLVV 100
Cdd:PRK05253   10 DQLEAESIHILREVAAEFENPVMLYSIGKDSSVMLHLARKAFYPGKLPFPLLHVDTGWKFPEMIEFRDRRAKELGLELIV 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997968265 101 GSVQEYIDRGELRERADG--TRNTLQTTPLLDTIRTNRFDAVFGGGRRDEDKARAKERIISLRDAFGQWDPRNQRPELWN 178
Cdd:PRK05253   90 HSNPEGIARGINPFRHGSakHTNAMKTEGLKQALEKYGFDAAFGGARRDEEKSRAKERIFSFRDEFGQWDPKNQRPELWN 169

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997968265 179 LYNGRHTPGQHVRAFPISNWTELDVWRYIAREGIELPSIYYAHEREVFRRDGMWRAVGEHSRPTEEEEVTTRTVRYRTVG 258
Cdd:PRK05253  170 LYNGRINKGEHIRVFPLSNWTELDIWQYIERENIPIVPLYFAHERPVVERDGMLIMVDDRMPLRPGEVVEERMVRFRTLG 249

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1997968265 259 DMSCTGAVLSAAATVEDVVLEVAASTLTERGATRADDRiSEAAMEDRKKDGYF 311
Cdd:PRK05253  250 CYPCTGAVESEAATLEEIIAEMLVTRTSERGGRAIDDD-QEASMEKRKREGYF 301
 
Name Accession Description Interval E-value
PRK05253 PRK05253
sulfate adenylyltransferase subunit CysD;
21-311 0e+00

sulfate adenylyltransferase subunit CysD;


Pssm-ID: 235375  Cd Length: 301  Bit Score: 554.36  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997968265  21 DALEAEAIHIIREVVAEFERPAMLFSGGKDSVVMLHLAAKAFWPGRIPFPVVHVDTGHNFPEVLEFRDRTVERLGLRLVV 100
Cdd:PRK05253   10 DQLEAESIHILREVAAEFENPVMLYSIGKDSSVMLHLARKAFYPGKLPFPLLHVDTGWKFPEMIEFRDRRAKELGLELIV 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997968265 101 GSVQEYIDRGELRERADG--TRNTLQTTPLLDTIRTNRFDAVFGGGRRDEDKARAKERIISLRDAFGQWDPRNQRPELWN 178
Cdd:PRK05253   90 HSNPEGIARGINPFRHGSakHTNAMKTEGLKQALEKYGFDAAFGGARRDEEKSRAKERIFSFRDEFGQWDPKNQRPELWN 169

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997968265 179 LYNGRHTPGQHVRAFPISNWTELDVWRYIAREGIELPSIYYAHEREVFRRDGMWRAVGEHSRPTEEEEVTTRTVRYRTVG 258
Cdd:PRK05253  170 LYNGRINKGEHIRVFPLSNWTELDIWQYIERENIPIVPLYFAHERPVVERDGMLIMVDDRMPLRPGEVVEERMVRFRTLG 249

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1997968265 259 DMSCTGAVLSAAATVEDVVLEVAASTLTERGATRADDRiSEAAMEDRKKDGYF 311
Cdd:PRK05253  250 CYPCTGAVESEAATLEEIIAEMLVTRTSERGGRAIDDD-QEASMEKRKREGYF 301
CysD TIGR02039
sulfate adenylyltransferase, small subunit; Metabolic assimilation of sulfur from inorganic ...
 21-311 1.48e-155

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: 436.47  E-value: 1.48e-155
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997968265  21 DALEAEAIHIIREVVAEFERPAMLFSGGKDSVVMLHLAAKAFWPGRIPFPVVHVDTGHNFPEVLEFRDRTVERLGLRLVV 100
Cdd:TIGR02039   2 RALESEAIHIIREVAAEFERPVMLYSIGKDSSVLLHLARKAFYPGPLPFPLLHVDTGWKFREMIAFRDHMVAKYGLRLIV 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997968265 101 GSVQEYIDRG--ELRERADGTRNTLQTTPLLDTIRTNRFDAVFGGGRRDEDKARAKERIISLRDAFGQWDPRNQRPELWN 178
Cdd:TIGR02039  82 HSNEEGIADGinPFTEGSALHTDIMKTEALRQALDKNQFDAAFGGARRDEEKSRAKERIFSFRNAFHQWDPKKQRPELWN 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997968265 179 LYNGRHTPGQHVRAFPISNWTELDVWRYIAREGIELPSIYYAHEREVFRRDGMWRAVG-EHSRPTEEEEVTTRTVRYRTV 257
Cdd:TIGR02039 162 LYNGRISKGESVRVFPLSNWTELDIWRYIAAENIPIVPLYFAAKRPVVQRDGMLIMVDdVRMPLAPGEVVKERMVRFRTL 241

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1997968265 258 GDMSCTGAVLSAAATVEDVVLEVAASTLTERgATRADDRISEAAMEDRKKDGYF 311
Cdd:TIGR02039 242 GCYPLTGAIESDAATVEEIIAETAAARTSER-QGRAIDRDQAASMEDKKREGYF 294
Sulfate_adenylyltransferase_2 cd23946
Sulfate adenylyltransferase subunit 2; Sulfate adenylyltransferase subunits 1 and 2 form ATP ...
 21-230 3.48e-95

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: 280.54  E-value: 3.48e-95
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997968265  21 DALEAEAIHIIREVVAEFERPAMLFSGGKDSVVMLHLAAKAFWPGRIPFPVVHVDTGHNFPEVLEFRDRTVERLGLRLVV 100
Cdd:cd23946     3 RQLEAESIHIIREVAAEFSNPVMLYSIGKDSSVMLHLARKAFYPGKPPFPLLHVDTTWKFREMIEFRDRVAKEYGLDLIV 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997968265 101 GSVQEYIDRGELRERADGTRNT--LQTTPLLDTIRTNRFDAVFGGGRRDEDKARAKERIISLRDAFGQWDPRNQRPELWN 178
Cdd:cd23946    83 HVNPDGVEAGINPFTHGSAKHTdiMKTEGLKQALDKYGFDAAFGGARRDEEKSRAKERVYSFRDSNHRWDPKNQRPELWN 162

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1997968265 179 LYNGRHTPGQHVRAFPISNWTELDVWRYIAREGIELPSIYYAHEREVFRRDG 230
Cdd:cd23946   163 QYNGRVKKGESIRVFPLSNWTELDIWQYIYLENIPIVPLYFAAERPVIERDG 214
CysD COG0175
3'-phosphoadenosine 5'-phosphosulfate sulfotransferase (PAPS reductase)/FAD synthetase or ...
 17-269 3.35e-70

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: 217.41  E-value: 3.35e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997968265  17 PDVQDALEAEAIHIIREVVAEF-ERPAMLFSGGKDSVVMLHLAAKAfwpgRIPFPVVHVDTGHNFPEVLEFRDRTVERLG 95
Cdd:COG0175    11 EELNAELEAEAIEILREAAAEFgGRVVVSSSGGKDSTVLLHLAAKF----KPPIPVLFLDTGYEFPETYEFRDRLAERLG 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997968265  96 LRLVVGSVQEYIDRGEL-------RERADGTRNTLQTTPLLDTIRTNRFDAVFGGGRRDEDKARAKERIISlrdafgqWD 168
Cdd:COG0175    87 LDLIVVRPEDAFAEQLAefgpplfYRDPRWCCKIRKVEPLKRALAGYDFDAWITGLRRDESPTRAKEPVVE-------WD 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997968265 169 PrnqrpelwnlyngrhtPGQHVRAFPISNWTELDVWRYIAREGIELPSIYyaherevfrrdgmwrAVGehsrpteeeevt 248
Cdd:COG0175   160 P----------------VGGLIKVNPLADWTELDVWAYIRREDLPYNPLY---------------DQG------------ 196

                         250       260
                  ....*....|....*....|.
gi 1997968265 249 trtvrYRTVGDMSCTGAVLSA 269
Cdd:COG0175   197 -----YPSIGCAPCTRAVESG 212
PAPS_reduct pfam01507
Phosphoadenosine phosphosulfate reductase family; This domain is found in phosphoadenosine ...
 40-265 3.72e-52

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: 169.40  E-value: 3.72e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997968265  40 RPAMLFSGGKDSVVMLHLAAKAFWPGripfPVVHVDTGHNFPEVLEFRDRTVERLGLRLVVGSVQEYIDRGELRERADGT 119
Cdd:pfam01507   1 ELVVSFSGGKDSLVLLHLASKAFPPG----PVIFIDTGYEFPETYEFVDELEEKYGLNLKVYLPEDSFAEGINPEGIPSS 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997968265 120 -----RNTLQTTPLLDTIRTNRFDAVFGGGRRDEDKARAKERIISLRDAFgqwdprnqrpelwnlyngrhtpGQHVRAFP 194
Cdd:pfam01507  77 lyrrcCRLRKVEPLKRALKELGFDAWFTGLRRDESPSRAKLPIVSIDGDF----------------------PKVIKVFP 134

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1997968265 195 ISNWTELDVWRYIAREGIELPSIYYAHerevfrrdgmwravgehsrpteeeevttrtvrYRTVGDMSCTGA 265
Cdd:pfam01507 135 LLNWTETDVWQYILANNVPYNPLYDQG--------------------------------YRSIGCYPCTGP 173
 
Name Accession Description Interval E-value
PRK05253 PRK05253
sulfate adenylyltransferase subunit CysD;
21-311 0e+00

sulfate adenylyltransferase subunit CysD;


Pssm-ID: 235375  Cd Length: 301  Bit Score: 554.36  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997968265  21 DALEAEAIHIIREVVAEFERPAMLFSGGKDSVVMLHLAAKAFWPGRIPFPVVHVDTGHNFPEVLEFRDRTVERLGLRLVV 100
Cdd:PRK05253   10 DQLEAESIHILREVAAEFENPVMLYSIGKDSSVMLHLARKAFYPGKLPFPLLHVDTGWKFPEMIEFRDRRAKELGLELIV 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997968265 101 GSVQEYIDRGELRERADG--TRNTLQTTPLLDTIRTNRFDAVFGGGRRDEDKARAKERIISLRDAFGQWDPRNQRPELWN 178
Cdd:PRK05253   90 HSNPEGIARGINPFRHGSakHTNAMKTEGLKQALEKYGFDAAFGGARRDEEKSRAKERIFSFRDEFGQWDPKNQRPELWN 169

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997968265 179 LYNGRHTPGQHVRAFPISNWTELDVWRYIAREGIELPSIYYAHEREVFRRDGMWRAVGEHSRPTEEEEVTTRTVRYRTVG 258
Cdd:PRK05253  170 LYNGRINKGEHIRVFPLSNWTELDIWQYIERENIPIVPLYFAHERPVVERDGMLIMVDDRMPLRPGEVVEERMVRFRTLG 249

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1997968265 259 DMSCTGAVLSAAATVEDVVLEVAASTLTERGATRADDRiSEAAMEDRKKDGYF 311
Cdd:PRK05253  250 CYPCTGAVESEAATLEEIIAEMLVTRTSERGGRAIDDD-QEASMEKRKREGYF 301
CysD TIGR02039
sulfate adenylyltransferase, small subunit; Metabolic assimilation of sulfur from inorganic ...
 21-311 1.48e-155

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: 436.47  E-value: 1.48e-155
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997968265  21 DALEAEAIHIIREVVAEFERPAMLFSGGKDSVVMLHLAAKAFWPGRIPFPVVHVDTGHNFPEVLEFRDRTVERLGLRLVV 100
Cdd:TIGR02039   2 RALESEAIHIIREVAAEFERPVMLYSIGKDSSVLLHLARKAFYPGPLPFPLLHVDTGWKFREMIAFRDHMVAKYGLRLIV 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997968265 101 GSVQEYIDRG--ELRERADGTRNTLQTTPLLDTIRTNRFDAVFGGGRRDEDKARAKERIISLRDAFGQWDPRNQRPELWN 178
Cdd:TIGR02039  82 HSNEEGIADGinPFTEGSALHTDIMKTEALRQALDKNQFDAAFGGARRDEEKSRAKERIFSFRNAFHQWDPKKQRPELWN 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997968265 179 LYNGRHTPGQHVRAFPISNWTELDVWRYIAREGIELPSIYYAHEREVFRRDGMWRAVG-EHSRPTEEEEVTTRTVRYRTV 257
Cdd:TIGR02039 162 LYNGRISKGESVRVFPLSNWTELDIWRYIAAENIPIVPLYFAAKRPVVQRDGMLIMVDdVRMPLAPGEVVKERMVRFRTL 241

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1997968265 258 GDMSCTGAVLSAAATVEDVVLEVAASTLTERgATRADDRISEAAMEDRKKDGYF 311
Cdd:TIGR02039 242 GCYPLTGAIESDAATVEEIIAETAAARTSER-QGRAIDRDQAASMEDKKREGYF 294
PRK12563 PRK12563
sulfate adenylyltransferase subunit CysD;
13-311 2.22e-130

sulfate adenylyltransferase subunit CysD;


Pssm-ID: 237138  Cd Length: 312  Bit Score: 373.35  E-value: 2.22e-130
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997968265  13 SPAGPDVQDALEAEAIHIIREVVAEFERPAMLFSGGKDSVVMLHLAAKAFWPGRIPFPVVHVDTGHNFPEVLEFRDRTVE 92
Cdd:PRK12563   12 STSRMGHLDRLEAESIHILREVVAECSKPVMLYSIGKDSVVMLHLAMKAFRPTRPPFPLLHVDTTWKFREMIDFRDRRAK 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997968265  93 RLGLRLVVGSVQEYIDRG--ELRERADGTRNTLQTTPLLDTIRTNRFDAVFGGGRRDEDKARAKERIISLRDAFGQWDPR 170
Cdd:PRK12563   92 ELGLDLVVHHNPDGIARGivPFRHGSALHTDVAKTQGLKQALDHHGFDAAIGGARRDEEKSRAKERIFSFRSAFHRWDPK 171

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997968265 171 NQRPELWNLYNGRHTPGQHVRAFPISNWTELDVWRYIAREGIELPSIYYAHEREVFRRDGMWRAVG-EHSRPTEEEEVTT 249
Cdd:PRK12563  172 AQRPELWSLYNARLRRGESLRVFPLSNWTELDVWQYIAREKIPLVPLYFAKRRPVVERDGLLIMVDdERTPLRPGETPQQ 251

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1997968265 250 RTVRYRTVGDMSCTGAVLSAAATVEDVVLEVAASTLTERGAtRADDRISEAAMEDRKKDGYF 311
Cdd:PRK12563  252 RKVRFRTLGCYPLTGAVESDADTVEKIIQEMAVTRISERQG-RMIDQDSAASMEKKKKEGYF 312
Sulfate_adenylyltransferase_2 cd23946
Sulfate adenylyltransferase subunit 2; Sulfate adenylyltransferase subunits 1 and 2 form ATP ...
 21-230 3.48e-95

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: 280.54  E-value: 3.48e-95
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997968265  21 DALEAEAIHIIREVVAEFERPAMLFSGGKDSVVMLHLAAKAFWPGRIPFPVVHVDTGHNFPEVLEFRDRTVERLGLRLVV 100
Cdd:cd23946     3 RQLEAESIHIIREVAAEFSNPVMLYSIGKDSSVMLHLARKAFYPGKPPFPLLHVDTTWKFREMIEFRDRVAKEYGLDLIV 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997968265 101 GSVQEYIDRGELRERADGTRNT--LQTTPLLDTIRTNRFDAVFGGGRRDEDKARAKERIISLRDAFGQWDPRNQRPELWN 178
Cdd:cd23946    83 HVNPDGVEAGINPFTHGSAKHTdiMKTEGLKQALDKYGFDAAFGGARRDEEKSRAKERVYSFRDSNHRWDPKNQRPELWN 162

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1997968265 179 LYNGRHTPGQHVRAFPISNWTELDVWRYIAREGIELPSIYYAHEREVFRRDG 230
Cdd:cd23946   163 QYNGRVKKGESIRVFPLSNWTELDIWQYIYLENIPIVPLYFAAERPVIERDG 214
CysD COG0175
3'-phosphoadenosine 5'-phosphosulfate sulfotransferase (PAPS reductase)/FAD synthetase or ...
 17-269 3.35e-70

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: 217.41  E-value: 3.35e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997968265  17 PDVQDALEAEAIHIIREVVAEF-ERPAMLFSGGKDSVVMLHLAAKAfwpgRIPFPVVHVDTGHNFPEVLEFRDRTVERLG 95
Cdd:COG0175    11 EELNAELEAEAIEILREAAAEFgGRVVVSSSGGKDSTVLLHLAAKF----KPPIPVLFLDTGYEFPETYEFRDRLAERLG 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997968265  96 LRLVVGSVQEYIDRGEL-------RERADGTRNTLQTTPLLDTIRTNRFDAVFGGGRRDEDKARAKERIISlrdafgqWD 168
Cdd:COG0175    87 LDLIVVRPEDAFAEQLAefgpplfYRDPRWCCKIRKVEPLKRALAGYDFDAWITGLRRDESPTRAKEPVVE-------WD 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997968265 169 PrnqrpelwnlyngrhtPGQHVRAFPISNWTELDVWRYIAREGIELPSIYyaherevfrrdgmwrAVGehsrpteeeevt 248
Cdd:COG0175   160 P----------------VGGLIKVNPLADWTELDVWAYIRREDLPYNPLY---------------DQG------------ 196

                         250       260
                  ....*....|....*....|.
gi 1997968265 249 trtvrYRTVGDMSCTGAVLSA 269
Cdd:COG0175   197 -----YPSIGCAPCTRAVESG 212
PAPS_reduct pfam01507
Phosphoadenosine phosphosulfate reductase family; This domain is found in phosphoadenosine ...
 40-265 3.72e-52

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: 169.40  E-value: 3.72e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997968265  40 RPAMLFSGGKDSVVMLHLAAKAFWPGripfPVVHVDTGHNFPEVLEFRDRTVERLGLRLVVGSVQEYIDRGELRERADGT 119
Cdd:pfam01507   1 ELVVSFSGGKDSLVLLHLASKAFPPG----PVIFIDTGYEFPETYEFVDELEEKYGLNLKVYLPEDSFAEGINPEGIPSS 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997968265 120 -----RNTLQTTPLLDTIRTNRFDAVFGGGRRDEDKARAKERIISLRDAFgqwdprnqrpelwnlyngrhtpGQHVRAFP 194
Cdd:pfam01507  77 lyrrcCRLRKVEPLKRALKELGFDAWFTGLRRDESPSRAKLPIVSIDGDF----------------------PKVIKVFP 134

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1997968265 195 ISNWTELDVWRYIAREGIELPSIYYAHerevfrrdgmwravgehsrpteeeevttrtvrYRTVGDMSCTGA 265
Cdd:pfam01507 135 LLNWTETDVWQYILANNVPYNPLYDQG--------------------------------YRSIGCYPCTGP 173
PAPS_reductase-like_YbdN cd23947
uncharacterized phosphoadenosine phosphosulfate reductase-like proteins, similar to ...
 27-225 6.11e-27

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: 104.78  E-value: 6.11e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997968265  27 AIHIIREVVAEFERPAMLFSGGKDSVVMLHLAAKAFWPGRIPFPVVHVDTGHNFPEVLEFRDRTVERLGLRLVvgsVQEY 106
Cdd:cd23947     1 ALERIRKVFEEFDPVIVSFSGGKDSLVLLHLALEALRRLRKDVYVVFIDTGIEFPETIDFVEKLAETLGLDVE---AARP 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997968265 107 IDRGELRERADGTRNTLQTTPLL---------DTIRTNRFD-----------AVFGGGRRDEDKARAKeriislrdafgq 166
Cdd:cd23947    78 PLFLEWLTSNFQPQWDPIWDNPPpprdyrwccDELKLEPFTkwlkekkpegvLLLVGIRADESLNRAK------------ 145

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1997968265 167 wdprnqRPELWNLYNGRHT--PGQHVrAFPISNWTELDVWRYIAREGIELPSIYY-AHEREV 225
Cdd:cd23947   146 ------RPRVYRKYGWRNStlPGQIV-AYPIKDWSVEDVWLYILRHGLPYNPLYDlGFDRGG 200
PAPS_reductase cd23945
Phosphoadenylyl-sulfate reductase (thioredoxin); Phosphoadenosine phosphosulfate (PAPS) ...
 30-212 9.48e-21

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: 87.65  E-value: 9.48e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997968265  30 IIREVVAEFERPAMLFSGGKDSVVMLHLAAKAfwpgRIPFPVVHVDTGHNFPEVLEFRDRTVERLGLRLVV-----GSVQ 104
Cdd:cd23945     5 LLWAAEEFGPKLVFATSFGAEDAVILDLLSKV----RPDIPVVFLDTGYLFPETYDLIDEVEARYGLNIEVyfpegTEAE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997968265 105 EYIDRGELRERADGTRNT------LQTTPLLdtIRTNRFDAVFGGGRRDEDKARAKERIISLRDAFGQWDprnqrpelWN 178
Cdd:cd23945    81 EEALEGGLNEFYLEDEERydccrkRKPFPLA--LALLGVKAWITGRRRDQSPTRANLPIVEVDEEGGLVK--------IN 150

                         170       180       190
                  ....*....|....*....|....*....|....
gi 1997968265 179 lyngrhtpgqhvrafPISNWTELDVWRYIAREGI 212
Cdd:cd23945   151 ---------------PLADWTWEDVWAYIREHDL 169
PRK13795 PRK13795
hypothetical protein; Provisional
 11-211 2.31e-20

hypothetical protein; Provisional


Pssm-ID: 237510 [Multi-domain]  Cd Length: 636  Bit Score: 91.21  E-value: 2.31e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997968265  11 TVSPAGPDVQDALEA----------EAIHIIREVVAEFERP-AMLFSGGKDSVVMLHLAAKAFwpgrIPFPVVHVDTGHN 79
Cdd:PRK13795  205 RLPPGRATLEDAIEAnrkhleekekEAVNFIRGVAEKYNLPvSVSFSGGKDSLVVLDLAREAL----KDFKAFFNNTGLE 280

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997968265  80 FPEVLEFRDRTVERLGLRLVVGSVQEYIDR--GELRERADGTR---NTLQTTPLLDTIRTNRFDAV--FGGGRRDEDKAR 152
Cdd:PRK13795  281 FPETVENVKEVAEEYGIELIEADAGDAFWRavEKFGPPARDYRwccKVCKLGPITRAIKENFPKGCltFVGQRKYESFSR 360

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997968265 153 AK-ERIislrdafgqWdpRNQrpelWnlyngrhTPGQhVRAFPISNWTELDVWRYIAREG 211
Cdd:PRK13795  361 AKsPRV---------W--RNP----W-------VPNQ-IGASPIQDWTALEVWLYIFWRK 397
PRK13794 PRK13794
hypothetical protein; Provisional
 15-210 5.86e-19

hypothetical protein; Provisional


Pssm-ID: 237509 [Multi-domain]  Cd Length: 479  Bit Score: 86.65  E-value: 5.86e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997968265  15 AGPDVQDALEAEAIHIIREVVAEFERPAML-FSGGKDSVVMLHLAAKAFwpgRIPFPVVHVDTGHNFPEVLEFRDRTVER 93
Cdd:PRK13794  223 ANKNVLDKYERNSIGFIRNTAEKINKPVTVaYSGGKDSLATLLLALKAL---GINFPVLFNDTGLEFPETLENVEDVEKH 299

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997968265  94 LGLRLVVGSVQEYIDRgeLRERADGTRN------TLQTTPLLDTIRTNRFDAV--FGGGRRDEDKARAKERIIslrdafg 165
Cdd:PRK13794  300 YGLEIIRTKSEEFWEK--LEEYGPPARDnrwcseVCKLEPLGKLIDEKYEGEClsFVGQRKYESFNRSKKPRI------- 370

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1997968265 166 qwdprnqrpelwnlYNGRHTPGQhVRAFPISNWTELDVWRYIARE 210
Cdd:PRK13794  371 --------------WRNPYIKKQ-ILAAPILHWTAMHVWIYLFRE 400
FAD_synthase cd23948
FAD synthase; FAD synthase (FMN:ATP adenylyl transferase (FMNAT); FAD pyrophosphorylase; ...
 26-212 5.62e-17

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: 77.18  E-value: 5.62e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997968265  26 EAIHIIREVVAEFERPAMLFS--GGKDSVVMLHLAAKAFW----PGRIPFPVVHVDTGHNFPEVLEFRDRTVERLGLRLV 99
Cdd:cd23948     4 SALEVIEEALDKYGPEEIAISfnGGKDCTVLLHLLRAALKrkypSPLTPLKALYIKSPDPFPEVEEFVEDTAKRYNLDLI 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997968265 100 VGSvqeyidrGELREradGTRNTLQTTPLLdtirtnrfDAVFGGGRRDedkarakeriislrdafgqwDP--RNQRPELW 177
Cdd:cd23948    84 TID-------GPMKE---GLEELLKEHPII--------KAVFMGTRRT--------------------DPhgENLKPFSP 125

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1997968265 178 NlyngrhTPG--QHVRAFPISNWTELDVWRYIAREGI 212
Cdd:cd23948   126 T------DPGwpQFMRVNPILDWSYHDVWEFLRTLNL 156
PRK02090 PRK02090
phosphoadenylyl-sulfate reductase;
24-212 2.39e-15

phosphoadenylyl-sulfate reductase;


Pssm-ID: 234997  Cd Length: 241  Bit Score: 74.10  E-value: 2.39e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997968265  24 EAEAIHIIREVVAEF-ERPAMLFSGGKDSVVMLHLAAKAfwpgRIPFPVVHVDTGHNFPEVLEFRDRTVERLGLRLVV-- 100
Cdd:PRK02090   25 GASAQERLAWALENFgGRLALVSSFGAEDAVLLHLVAQV----DPDIPVIFLDTGYLFPETYRFIDELTERLLLNLKVyr 100

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997968265 101 ---GSVQEYIDRG-------ELRERADGTRntlQTTPLldtirtNR----FDAVFGGGRRDEDKARAKERIIslrdafgQ 166
Cdd:PRK02090  101 pdaSAAEQEARYGglweqsvEDRDECCRIR---KVEPL------NRalagLDAWITGLRREQSGTRANLPVL-------E 164

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1997968265 167 WDprnqrpelwnlyNGRhtpgqhVRAFPISNWTELDVWRYIAREGI 212
Cdd:PRK02090  165 ID------------GGR------FKINPLADWTNEDVWAYLKEHDL 192
cysH TIGR00434
phosophoadenylyl-sulfate reductase (thioredoxin); This enzyme, involved in the assimilation of ...
 46-212 1.29e-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: 62.88  E-value: 1.29e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997968265  46 SGGKDSVVMLHLAAKAfwpgRIPFPVVHVDTGHNFPEVLEFRDRTVERLGLRLVVGSVQEYIDR------GELRERADGT 119
Cdd:TIGR00434  21 SFGIQGAVLLDLVSKI----SPDIPVIFLDTGYHFPETYELIDELTERYPLNIKVYKPDLSLAEqaakygDKLWEQDPNK 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997968265 120 RNTL-QTTPLLDTIRTNRFDAVFGGGRRDEDKARAKERIISLRDAFGQwdprnqrpelwnlyngrhtpgqhVRAFPISNW 198
Cdd:TIGR00434  97 YDYLrKVEPMHRALKELHASAWFTGLRRDQGPSRANLSILNIDEKFGI-----------------------LKVLPLIDW 153

                         170
                  ....*....|....
gi 1997968265 199 TELDVWRYIAREGI 212
Cdd:TIGR00434 154 TWKDVYQYIDAHNL 167
PRK08576 PRK08576
hypothetical protein; Provisional
 14-220 4.93e-08

hypothetical protein; Provisional


Pssm-ID: 236300 [Multi-domain]  Cd Length: 438  Bit Score: 53.93  E-value: 4.93e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997968265  14 PAGPDVQDALEAEaihiiREVVAEFERPAMLF-------------SGGKDSVVMLHLAAKAFwpGRIPfpVVHVDTGHNF 80
Cdd:PRK08576  202 PEEVSLEKLIEAN-----REVLEAFEKASIKFlrkfeewtvivpwSGGKDSTAALLLAKKAF--GDVT--AVYVDTGYEM 272

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997968265  81 PEVLEFRDRTVERLGLRLVVGSVQE--YIDRGELRERADGTRNTLQTTPLLDTIRTNRFDAVFGGGRRDEDKARakerii 158
Cdd:PRK08576  273 PLTDEYVEKVAEKLGVDLIRAGVDVpmPIEKYGMPTHSNRWCTKLKVEALEEAIRELEDGLLVVGDRDGESARR------ 346

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1997968265 159 SLRdafgqwDPRNQRPELWnlyngrhtpGQHVRAFPISNWTELDVWRYIAREGIELPSIYYA 220
Cdd:PRK08576  347 RLR------PPVVERKTNF---------GKILVVMPIKFWSGAMVQLYILMNGLELNPLYYK 393
PRK08557 PRK08557
hypothetical protein; Provisional
 21-218 1.93e-07

hypothetical protein; Provisional


Pssm-ID: 181465 [Multi-domain]  Cd Length: 417  Bit Score: 52.06  E-value: 1.93e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997968265  21 DALEAEAIHIIREVVAEFERPAML----FSGGKDSVVMLHLAAKAfwpgrIP-FPVVHVDTGHNFPEVLEFRDRTVERLG 95
Cdd:PRK08557  160 EKLEENSLSILKDYIEKYKNKGYAinasFSGGKDSSVSTLLAKEV-----IPdLEVIFIDTGLEYPETINYVKDFAKKYD 234

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997968265  96 LRLVV---GSVQEYIDRGELRERADGTRNTL-QTTPL---LDTIRTNRFDAVFGGGRRDEDKARAK---ERIISLRDafg 165
Cdd:PRK08557  235 LNLDTldgDNFWENLEKEGIPTKDNRWCNSAcKLMPLkeyLKKKYGNKKVLTIDGSRKYESFTRANldyERKSGFID--- 311

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1997968265 166 qwdprNQrpelwnlyngrhtpgqhVRAFPISNWTELDVWRYIAREGIELPSIY 218
Cdd:PRK08557  312 -----FQ-----------------TNVFPILDWNSLDIWSYIYLNDILYNPLY 342
AANH-like cd01986
adenine nucleotide alpha hydrolase (AANH)-like proteins; This group of adenine nucleotide ...
 44-93 2.28e-07

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: 47.45  E-value: 2.28e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 1997968265  44 LFSGGKDSVVMLHLAAKAFWPgrIPFPVVHVDTGHNFPEVLEFRDRTVER 93
Cdd:cd01986     4 GYSGGKDSSVALHLASRLGRK--AEVAVVHIDHGIGFKEEAESVASIARR 51
TilS COG0037
tRNA(Ile)-lysidine synthase TilS/MesJ [Translation, ribosomal structure and biogenesis]; tRNA ...
 45-106 1.23e-06

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: 48.68  E-value: 1.23e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1997968265  45 FSGGKDSVVMLHLAAKAFWPGRIPFPVVHVDtgHNFPEVLEFRDRTV----ERLGLRLVVGSVQEY 106
Cdd:COG0037    22 VSGGKDSLALLHLLAKLRRRLGFELVAVHVD--HGLREESDEDAEFVaelcEELGIPLHVVRVDVP 85
AANH_WbpG-like cd01996
Rhizobium leguminosarum WbpG protein and similar proteins; This subfamily includes Rhizobium ...
 45-99 4.44e-04

Rhizobium leguminosarum WbpG protein and similar proteins; This subfamily includes Rhizobium leguminosarum WbpG and Campylobacter jejuni PseA proteins. They belong to the of adenine nucleotide alpha hydrolase (AANH) superfamily that also includes N-type ATP PPases and ATP sulfurylases. It forms an alpha/beta/alpha fold which binds to adenosine group. This subfamily of proteins is predicted to bind ATP. This domain has a strongly conserved motif SGGKD at the N-terminus.


Pssm-ID: 467500 [Multi-domain]  Cd Length: 158  Bit Score: 40.05  E-value: 4.44e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1997968265  45 FSGGKDSVVMLHLAAKAFwpGRIPFpVVHVDTGHNFPEVLEFRDRTVERLGLRLV 99
Cdd:cd01996    12 VSGGKDSTYAAHKAKEKY--GLRPL-LVTVDAGWNSPEAVKNIEKLVRALGVDLI 63
ATP_bind_3 pfam01171
PP-loop family; This family of proteins belongs to the PP-loop superfamily.
 45-111 8.22e-04

PP-loop family; This family of proteins belongs to the PP-loop superfamily.


Pssm-ID: 426097 [Multi-domain]  Cd Length: 178  Bit Score: 39.53  E-value: 8.22e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1997968265  45 FSGGKDSVVMLHLAAKAFWPGRIPFPVVHVDtgHNFPEVLEFRDRTVE----RLGLRLVVGSVQEYIDRGE 111
Cdd:pfam01171   3 VSGGPDSMALLYLLAKLKIKLGIELTAAHVN--HGLREESDREAEHVQalcrQLGIPLEILRVDVAKKSGE 71
CTU1-like cd01713
cytoplasmic tRNA 2-thiolation protein 1 and similar proteins; This subfamily includes human ...
 39-122 9.39e-04

cytoplasmic tRNA 2-thiolation protein 1 and similar proteins; This subfamily includes human cytoplasmic tRNA 2-thiolation protein 1, also called cytosolic thiouridylase subunit 1 (CTU1), ATP-binding domain-containing protein 3 (ATPBD3), cancer-associated gene protein, or cytoplasmic tRNA adenylyltransferase 1. CTU1 plays a central role in 2-thiolation of mcm(5)S(2)U at tRNA wobble positions of tRNA(Lys), tRNA(Glu) and tRNA(Gln). It directly binds tRNAs and probably acts by catalyzing adenylation of tRNAs, an intermediate required for 2-thiolation. The CTU1-like subfamily belongs to the nucleotide alpha hydrolase (AANH) superfamily that includes N-type ATP PPases and ATP sulfurylases. It forms an alpha/beta/alpha fold which binds to the adenosine group.


Pssm-ID: 467486  Cd Length: 208  Bit Score: 39.88  E-value: 9.39e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997968265  39 ERPAMLFSGGKDSVVMLHLAAKAF--WPGRIPFPVVHVDTGHNF--PEVLEFRDRTVERLGLRLVVGSVQEYIDRG--EL 112
Cdd:cd01713    19 DRVAVGLSGGKDSTVLLYVLKELNkrHDYGVELIAVTIDEGIKGyrDDSLEAARKLAEEYGIPLEIVSFEDEFGFTldEL 98

                          90
                  ....*....|
gi 1997968265 113 RERADGTRNT 122
Cdd:cd01713    99 IVGKGGKKNA 108
lysidine_TilS_N TIGR02432
tRNA(Ile)-lysidine synthetase, N-terminal domain; The only examples in which the wobble ...
 45-79 1.20e-03

tRNA(Ile)-lysidine synthetase, N-terminal domain; The only examples in which the wobble position of a tRNA must discriminate between G and A of mRNA are AUA (Ile) vs. AUG (Met) and UGA (stop) vs. UGG (Trp). In all bacteria, the wobble position of the tRNA(Ile) recognizing AUA is lysidine, a lysine derivative of cytidine. This family describes a protein domain found, apparently, in all bacteria in a single copy. Eukaryotic sequences appear to be organellar. The domain archictecture of this protein family is variable; some, including characterized proteins of E. coli and B. subtilis known to be tRNA(Ile)-lysidine synthetase, include a conserved 50-residue domain that many other members lack. This protein belongs to the ATP-binding PP-loop family ( pfam01171). It appears in the literature and protein databases as TilS, YacA, and putative cell cycle protein MesJ (a misnomer). [Protein synthesis, tRNA and rRNA base modification]


Pssm-ID: 274129 [Multi-domain]  Cd Length: 189  Bit Score: 39.15  E-value: 1.20e-03
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 1997968265  45 FSGGKDSVVMLHLAAKAFWPGRIPFPVVHVDtgHN 79
Cdd:TIGR02432   6 VSGGVDSMALLHLLLKLQPKIKIKLIAAHVD--HG 38
TtcA-like cd24138
tRNA-cytidine(32) 2-sulfurtransferase and similar proteins; tRNA-cytidine(32) ...
 45-95 3.05e-03

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: 38.02  E-value: 3.05e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1997968265  45 FSGGKDSVVMLHLAakAFWPGRIPFPV----VHVDTG-HNFPEVLEFRDRTVERLG 95
Cdd:cd24138    15 LSGGKDSLTLLHLL--EELKRRAPIKFelvaVTVDPGyPGYRPPREELAEILEELG 68
TilS_N cd01992
N-terminal domain of tRNA(Ile)-lysidine synthase and similar proteins; tRNA(Ile)-lysidine ...
 45-80 6.78e-03

N-terminal domain of tRNA(Ile)-lysidine synthase and similar proteins; tRNA(Ile)-lysidine synthase (EC 6.3.4.19), also called tRNA(Ile)-2-lysyl-cytidine synthase or tRNA(Ile)-lysidine synthetase, catalyzes the ligation of lysine onto the cytidine present at position 34 of the AUA codon-specific tRNA(Ile) that contains the anticodon CAU, in an ATP-dependent manner. Cytidine is converted to lysidine, thus changing the amino acid specificity of the tRNA from methionine to isoleucine. This subfamily belongs to the adenine nucleotide alpha hydrolase superfamily that also includes N-type ATP PPases and ATP sulfurylases. It forms an alpha/beta/alpha fold which binds to adenosine group. This domain has a strongly conserved motif SGGXD at the N-terminus.


Pssm-ID: 467496 [Multi-domain]  Cd Length: 185  Bit Score: 36.80  E-value: 6.78e-03
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 1997968265  45 FSGGKDSVVMLHLAAKAFWPGRIPFPVVHVDtgHNF 80
Cdd:cd01992     6 VSGGPDSMALLHLLKELRPKLGLKLVAVHVD--HGL 39
 
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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