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Conserved domains on  [gi|1101081741|gb|OIO41909|]
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phosphoadenosine phosphosulfate reductase [Candidatus Pacearchaeota archaeon CG1_02_35_32]

Protein Classification

phosphoadenosine phosphosulfate reductase( domain architecture ID 11467720)

phosphoadenosine phosphosulfate reductase uses thioredoxin as an electron donor for the reduction of PAPS to phospho-adenosine-phosphate (PAP), contains a C-terminal DUF3440 domain

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
YbdN COG3969
Predicted phosphoadenosine phosphosulfate sulfurtransferase, contains C-terminal DUF3440 ...
 1-397 0e+00

Predicted phosphoadenosine phosphosulfate sulfurtransferase, contains C-terminal DUF3440 domain [General function prediction only];


:

Pssm-ID: 443169 [Multi-domain]  Cd Length: 402  Bit Score: 592.69  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101081741   1 MKK-LGIDVLSAATQRIAWVFDNFPRIYVSFSGGKDSTVMLHLVAKEAIKRNRKIGVLFVDLEGQYKLTIDHIKECFSFY 79
Cdd:COG3969     1 MKKyLDENVYEAAQERIEWIFDEFDRVCVSFSGGKDSGVLLHLAAEVARKNGRKIDVLFIDWEAQYSATIDHVEEMFERY 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101081741  80 STIIEPYWIALPLHLRNAVSNFEPHWICWQPDRKKDWVRDFPPF-AINNENYFSFFHYGMEFEEFVLSFGKWFGQGKLTA 158
Cdd:COG3969    81 EDVVRFYWVCLPLTTRNAVSQFQPEWYCWDPGKKEDWVRPMPEHdVITDPNFFPFYRYGMEFEEFVPAFGRWLSGKHPTA 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101081741 159 CFVGIRTVESLNRWRTIATGKKQTM-ENKCWTTWMGNILYNVYPIYDWRTEDIWTFHAKNpELAYNKLYDRMHQAGLSIY 237
Cdd:COG3969   161 CLVGIRADESLNRYLAIASQRKLRYyKDKPWTTAPFGNAYNAYPLYDWKTEDIWTANAKF-GYDYNRLYDLMYQAGVPLS 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101081741 238 QQRICQPYGDDQRKGLWLFHVIEPETWARVVARVNGANQGALYSQESgnILGRIKISKPEHYNWKEFALFLIDSMPKKTS 317
Cdd:COG3969   240 QMRVCEPFGDEQRKGLWLYHVLEPETWAKLVGRVNGANFGAIYGGTK--ALGYRKISLPEGHTWRSYALFLLDSMPERTA 317

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101081741 318 EHYKNKIFVFLQWWGKKGFKDG-IPDDGPLE----RDTPNWKRICKVLLRNDYWCKGLSFSQQKSHAYEKYLKVMRRRRE 392
Cdd:COG3969   318 EHYRNKIAVSLRWWQKRGGPLDeIPDDQDKDiegtKDIPSWRRICKCILKNDYWCRSLSFGPTKSEIYRRYALREKYKRI 397


                  ....*
gi 1101081741 393 QWEMI 397
Cdd:COG3969   398 LWGIL 402
 
Name Accession Description Interval E-value
YbdN COG3969
Predicted phosphoadenosine phosphosulfate sulfurtransferase, contains C-terminal DUF3440 ...
 1-397 0e+00

Predicted phosphoadenosine phosphosulfate sulfurtransferase, contains C-terminal DUF3440 domain [General function prediction only];


Pssm-ID: 443169 [Multi-domain]  Cd Length: 402  Bit Score: 592.69  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101081741   1 MKK-LGIDVLSAATQRIAWVFDNFPRIYVSFSGGKDSTVMLHLVAKEAIKRNRKIGVLFVDLEGQYKLTIDHIKECFSFY 79
Cdd:COG3969     1 MKKyLDENVYEAAQERIEWIFDEFDRVCVSFSGGKDSGVLLHLAAEVARKNGRKIDVLFIDWEAQYSATIDHVEEMFERY 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101081741  80 STIIEPYWIALPLHLRNAVSNFEPHWICWQPDRKKDWVRDFPPF-AINNENYFSFFHYGMEFEEFVLSFGKWFGQGKLTA 158
Cdd:COG3969    81 EDVVRFYWVCLPLTTRNAVSQFQPEWYCWDPGKKEDWVRPMPEHdVITDPNFFPFYRYGMEFEEFVPAFGRWLSGKHPTA 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101081741 159 CFVGIRTVESLNRWRTIATGKKQTM-ENKCWTTWMGNILYNVYPIYDWRTEDIWTFHAKNpELAYNKLYDRMHQAGLSIY 237
Cdd:COG3969   161 CLVGIRADESLNRYLAIASQRKLRYyKDKPWTTAPFGNAYNAYPLYDWKTEDIWTANAKF-GYDYNRLYDLMYQAGVPLS 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101081741 238 QQRICQPYGDDQRKGLWLFHVIEPETWARVVARVNGANQGALYSQESgnILGRIKISKPEHYNWKEFALFLIDSMPKKTS 317
Cdd:COG3969   240 QMRVCEPFGDEQRKGLWLYHVLEPETWAKLVGRVNGANFGAIYGGTK--ALGYRKISLPEGHTWRSYALFLLDSMPERTA 317

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101081741 318 EHYKNKIFVFLQWWGKKGFKDG-IPDDGPLE----RDTPNWKRICKVLLRNDYWCKGLSFSQQKSHAYEKYLKVMRRRRE 392
Cdd:COG3969   318 EHYRNKIAVSLRWWQKRGGPLDeIPDDQDKDiegtKDIPSWRRICKCILKNDYWCRSLSFGPTKSEIYRRYALREKYKRI 397


                  ....*
gi 1101081741 393 QWEMI 397
Cdd:COG3969   398 LWGIL 402
PAPS_reductase-like_YbdN cd23947
uncharacterized phosphoadenosine phosphosulfate reductase-like proteins, similar to ...
 12-240 1.51e-49

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: 166.41  E-value: 1.51e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101081741  12 ATQRIAWVFDNFPRIYVSFSGGKDSTVMLHLVAKEAIKRNRKIGVLFVDLEGQYKLTIDHIKECFSFYSTIIepYWIALP 91
Cdd:cd23947     1 ALERIRKVFEEFDPVIVSFSGGKDSLVLLHLALEALRRLRKDVYVVFIDTGIEFPETIDFVEKLAETLGLDV--EAARPP 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101081741  92 LHLRNAVSNFEPHWICwqpdrkkdwvrdfppfaINNENYFSFFHYGMEFEEFVLSFGKWFGQ--GKLTACFVGIRTVESL 169
Cdd:cd23947    79 LFLEWLTSNFQPQWDP-----------------IWDNPPPPRDYRWCCDELKLEPFTKWLKEkkPEGVLLLVGIRADESL 141

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1101081741 170 NRWRTIATGKKQTMENKcwttWMGNIlYNVYPIYDWRTEDIWTFHAKNPeLAYNKLYDRMHQAGLSIYQQR 240
Cdd:cd23947   142 NRAKRPRVYRKYGWRNS----TLPGQ-IVAYPIKDWSVEDVWLYILRHG-LPYNPLYDLGFDRGGCLVCPR 206
DUF3440 pfam11922
Domain of unknown function (DUF3440); This presumed domain is functionally uncharacterized. ...
 233-376 2.78e-33

Domain of unknown function (DUF3440); This presumed domain is functionally uncharacterized. This domain is found in bacteria. This domain is typically between 53 to 190 amino acids in length. This domain is found associated with pfam01507. This domain has a conserved KND sequence motif.


Pssm-ID: 432190  Cd Length: 181  Bit Score: 122.77  E-value: 2.78e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101081741 233 GLSIYQQRICQPYGDDQRKGLWLFHVIEPETWARVVARVNGANQGALYSQESGniLGRIKISKPEHYNWKEFALFLIDSM 312
Cdd:pfam11922   1 GVPLEQMRVASPFISAAIESLKLYRVIDPDTWGKMIGRVNGVNFAGIYGGTKA--MGWRSIKLPEGHTWKSYMYFLLSTL 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101081741 313 PKKTSEHYKNKIFVFLQWWGKKG--------------------------------FKDGIPDDGPLE--RDTPNWKRICK 358
Cdd:pfam11922  79 PEETRNNYLKKLSVSIKFWREKGgclseetieelkaagipievggksnyttdkrpVRMEYPDDIDIKefKEIPTYKRMCI 158

                         170
                  ....*....|....*...
gi 1101081741 359 VLLRNDYWCKGLSFSQQK 376
Cdd:pfam11922 159 CILKNDHTCKYMGFGPTK 176
PRK13795 PRK13795
hypothetical protein; Provisional
 22-228 1.55e-07

hypothetical protein; Provisional


Pssm-ID: 237510 [Multi-domain]  Cd Length: 636  Bit Score: 53.46  E-value: 1.55e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101081741  22 NFPrIYVSFSGGKDSTVMLHLVAKEAikrnRKIGVLFVDLEGQYKLTIDHIKECFSFYST--II----EPYWialplhlr 95
Cdd:PRK13795  243 NLP-VSVSFSGGKDSLVVLDLAREAL----KDFKAFFNNTGLEFPETVENVKEVAEEYGIelIEadagDAFW-------- 309

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101081741  96 NAVSNFEPhwicwqPDRKKDW---VRDFPPF--AINNEnyfsffhygmefeefvlsfgkwFGQGKLTacFVGIRTVESLN 170
Cdd:PRK13795  310 RAVEKFGP------PARDYRWcckVCKLGPItrAIKEN----------------------FPKGCLT--FVGQRKYESFS 359

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1101081741 171 RWRTIATGKkqtmeNKcwttWMGNILyNVYPIYDWRTEDIWTF-HAKNpeLAYNKLYDR 228
Cdd:PRK13795  360 RAKSPRVWR-----NP----WVPNQI-GASPIQDWTALEVWLYiFWRK--LPYNPLYER 406
lysidine_TilS_N TIGR02432
tRNA(Ile)-lysidine synthetase, N-terminal domain; The only examples in which the wobble ...
 25-60 2.44e-04

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: 41.85  E-value: 2.44e-04
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 1101081741  25 RIYVSFSGGKDSTVMLHLVAKEAIKRNRKIGVLFVD 60
Cdd:TIGR02432   1 RILVAVSGGVDSMALLHLLLKLQPKIKIKLIAAHVD 36
 
Name Accession Description Interval E-value
YbdN COG3969
Predicted phosphoadenosine phosphosulfate sulfurtransferase, contains C-terminal DUF3440 ...
 1-397 0e+00

Predicted phosphoadenosine phosphosulfate sulfurtransferase, contains C-terminal DUF3440 domain [General function prediction only];


Pssm-ID: 443169 [Multi-domain]  Cd Length: 402  Bit Score: 592.69  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101081741   1 MKK-LGIDVLSAATQRIAWVFDNFPRIYVSFSGGKDSTVMLHLVAKEAIKRNRKIGVLFVDLEGQYKLTIDHIKECFSFY 79
Cdd:COG3969     1 MKKyLDENVYEAAQERIEWIFDEFDRVCVSFSGGKDSGVLLHLAAEVARKNGRKIDVLFIDWEAQYSATIDHVEEMFERY 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101081741  80 STIIEPYWIALPLHLRNAVSNFEPHWICWQPDRKKDWVRDFPPF-AINNENYFSFFHYGMEFEEFVLSFGKWFGQGKLTA 158
Cdd:COG3969    81 EDVVRFYWVCLPLTTRNAVSQFQPEWYCWDPGKKEDWVRPMPEHdVITDPNFFPFYRYGMEFEEFVPAFGRWLSGKHPTA 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101081741 159 CFVGIRTVESLNRWRTIATGKKQTM-ENKCWTTWMGNILYNVYPIYDWRTEDIWTFHAKNpELAYNKLYDRMHQAGLSIY 237
Cdd:COG3969   161 CLVGIRADESLNRYLAIASQRKLRYyKDKPWTTAPFGNAYNAYPLYDWKTEDIWTANAKF-GYDYNRLYDLMYQAGVPLS 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101081741 238 QQRICQPYGDDQRKGLWLFHVIEPETWARVVARVNGANQGALYSQESgnILGRIKISKPEHYNWKEFALFLIDSMPKKTS 317
Cdd:COG3969   240 QMRVCEPFGDEQRKGLWLYHVLEPETWAKLVGRVNGANFGAIYGGTK--ALGYRKISLPEGHTWRSYALFLLDSMPERTA 317

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101081741 318 EHYKNKIFVFLQWWGKKGFKDG-IPDDGPLE----RDTPNWKRICKVLLRNDYWCKGLSFSQQKSHAYEKYLKVMRRRRE 392
Cdd:COG3969   318 EHYRNKIAVSLRWWQKRGGPLDeIPDDQDKDiegtKDIPSWRRICKCILKNDYWCRSLSFGPTKSEIYRRYALREKYKRI 397


                  ....*
gi 1101081741 393 QWEMI 397
Cdd:COG3969   398 LWGIL 402
PAPS_reductase-like_YbdN cd23947
uncharacterized phosphoadenosine phosphosulfate reductase-like proteins, similar to ...
 12-240 1.51e-49

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: 166.41  E-value: 1.51e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101081741  12 ATQRIAWVFDNFPRIYVSFSGGKDSTVMLHLVAKEAIKRNRKIGVLFVDLEGQYKLTIDHIKECFSFYSTIIepYWIALP 91
Cdd:cd23947     1 ALERIRKVFEEFDPVIVSFSGGKDSLVLLHLALEALRRLRKDVYVVFIDTGIEFPETIDFVEKLAETLGLDV--EAARPP 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101081741  92 LHLRNAVSNFEPHWICwqpdrkkdwvrdfppfaINNENYFSFFHYGMEFEEFVLSFGKWFGQ--GKLTACFVGIRTVESL 169
Cdd:cd23947    79 LFLEWLTSNFQPQWDP-----------------IWDNPPPPRDYRWCCDELKLEPFTKWLKEkkPEGVLLLVGIRADESL 141

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1101081741 170 NRWRTIATGKKQTMENKcwttWMGNIlYNVYPIYDWRTEDIWTFHAKNPeLAYNKLYDRMHQAGLSIYQQR 240
Cdd:cd23947   142 NRAKRPRVYRKYGWRNS----TLPGQ-IVAYPIKDWSVEDVWLYILRHG-LPYNPLYDLGFDRGGCLVCPR 206
DUF3440 pfam11922
Domain of unknown function (DUF3440); This presumed domain is functionally uncharacterized. ...
 233-376 2.78e-33

Domain of unknown function (DUF3440); This presumed domain is functionally uncharacterized. This domain is found in bacteria. This domain is typically between 53 to 190 amino acids in length. This domain is found associated with pfam01507. This domain has a conserved KND sequence motif.


Pssm-ID: 432190  Cd Length: 181  Bit Score: 122.77  E-value: 2.78e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101081741 233 GLSIYQQRICQPYGDDQRKGLWLFHVIEPETWARVVARVNGANQGALYSQESGniLGRIKISKPEHYNWKEFALFLIDSM 312
Cdd:pfam11922   1 GVPLEQMRVASPFISAAIESLKLYRVIDPDTWGKMIGRVNGVNFAGIYGGTKA--MGWRSIKLPEGHTWKSYMYFLLSTL 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101081741 313 PKKTSEHYKNKIFVFLQWWGKKG--------------------------------FKDGIPDDGPLE--RDTPNWKRICK 358
Cdd:pfam11922  79 PEETRNNYLKKLSVSIKFWREKGgclseetieelkaagipievggksnyttdkrpVRMEYPDDIDIKefKEIPTYKRMCI 158

                         170
                  ....*....|....*...
gi 1101081741 359 VLLRNDYWCKGLSFSQQK 376
Cdd:pfam11922 159 CILKNDHTCKYMGFGPTK 176
CysD COG0175
3'-phosphoadenosine 5'-phosphosulfate sulfotransferase (PAPS reductase)/FAD synthetase or ...
 1-228 3.57e-12

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: 65.64  E-value: 3.57e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101081741   1 MKKLGIDVLSAATQRIAWVFDNFP-RIYVSFSGGKDSTVMLHLVAkeaiKRNRKIGVLFVD--LEgqYKLTIDHIKEcfs 77
Cdd:COG0175    10 LEELNAELEAEAIEILREAAAEFGgRVVVSSSGGKDSTVLLHLAA----KFKPPIPVLFLDtgYE--FPETYEFRDR--- 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101081741  78 fystIIEpywiALPLHLRNAvsnfephwicwQPDRKKDWVRDfppfainnenyfsffHYGMEFEEF----------VLSF 147
Cdd:COG0175    81 ----LAE----RLGLDLIVV-----------RPEDAFAEQLA---------------EFGPPLFYRdprwcckirkVEPL 126

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101081741 148 GKWFGQGKLTACFVGIRTVESLNRwrtiatgkkqTMENKCWTTWMGNILyNVYPIYDWRTEDIWTFHAKNpELAYNKLYD 227
Cdd:COG0175   127 KRALAGYDFDAWITGLRRDESPTR----------AKEPVVEWDPVGGLI-KVNPLADWTELDVWAYIRRE-DLPYNPLYD 194


                  .
gi 1101081741 228 R 228
Cdd:COG0175   195 Q 195
PAPS_reduct pfam01507
Phosphoadenosine phosphosulfate reductase family; This domain is found in phosphoadenosine ...
 25-228 6.47e-12

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: 63.47  E-value: 6.47e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101081741  25 RIYVSFSGGKDSTVMLHLvakeAIKRNRKIGVLFVDLEGQYKLTIDHIKECFSFYSTIIEpywIALPLHlrNAVSNFEPH 104
Cdd:pfam01507   1 ELVVSFSGGKDSLVLLHL----ASKAFPPGPVIFIDTGYEFPETYEFVDELEEKYGLNLK---VYLPED--SFAEGINPE 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101081741 105 WICWQPDRKKDWVRDFPPF--AINNENYfsffhygmefeefvlsfgkwfgqgklTACFVGIRTVESLNRwrtiatgKKQT 182
Cdd:pfam01507  72 GIPSSLYRRCCRLRKVEPLkrALKELGF--------------------------DAWFTGLRRDESPSR-------AKLP 118

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1101081741 183 MENKcwTTWMGNiLYNVYPIYDWRTEDIWTFHAKNpELAYNKLYDR 228
Cdd:pfam01507 119 IVSI--DGDFPK-VIKVFPLLNWTETDVWQYILAN-NVPYNPLYDQ 160
PRK13795 PRK13795
hypothetical protein; Provisional
 22-228 1.55e-07

hypothetical protein; Provisional


Pssm-ID: 237510 [Multi-domain]  Cd Length: 636  Bit Score: 53.46  E-value: 1.55e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101081741  22 NFPrIYVSFSGGKDSTVMLHLVAKEAikrnRKIGVLFVDLEGQYKLTIDHIKECFSFYST--II----EPYWialplhlr 95
Cdd:PRK13795  243 NLP-VSVSFSGGKDSLVVLDLAREAL----KDFKAFFNNTGLEFPETVENVKEVAEEYGIelIEadagDAFW-------- 309

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101081741  96 NAVSNFEPhwicwqPDRKKDW---VRDFPPF--AINNEnyfsffhygmefeefvlsfgkwFGQGKLTacFVGIRTVESLN 170
Cdd:PRK13795  310 RAVEKFGP------PARDYRWcckVCKLGPItrAIKEN----------------------FPKGCLT--FVGQRKYESFS 359

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1101081741 171 RWRTIATGKkqtmeNKcwttWMGNILyNVYPIYDWRTEDIWTF-HAKNpeLAYNKLYDR 228
Cdd:PRK13795  360 RAKSPRVWR-----NP----WVPNQI-GASPIQDWTALEVWLYiFWRK--LPYNPLYER 406
TilS COG0037
tRNA(Ile)-lysidine synthase TilS/MesJ [Translation, ribosomal structure and biogenesis]; tRNA ...
 25-60 1.45e-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: 49.06  E-value: 1.45e-06
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 1101081741  25 RIYVSFSGGKDSTVMLHLVAKEAIKRNRKIGVLFVD 60
Cdd:COG0037    17 RILVAVSGGKDSLALLHLLAKLRRRLGFELVAVHVD 52
PRK08557 PRK08557
hypothetical protein; Provisional
 26-228 7.36e-06

hypothetical protein; Provisional


Pssm-ID: 181465 [Multi-domain]  Cd Length: 417  Bit Score: 47.83  E-value: 7.36e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101081741  26 IYVSFSGGKDSTVMLhLVAKEAIKrnrKIGVLFVDLEGQYKLTIDHIKECFSFYStiiepywiaLPLHL---RNAVSNFE 102
Cdd:PRK08557  184 INASFSGGKDSSVST-LLAKEVIP---DLEVIFIDTGLEYPETINYVKDFAKKYD---------LNLDTldgDNFWENLE 250

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101081741 103 PHWICWQPDRKKDWVRDFPPFainnENYFsffhygmefeefvlsfgKWFGQGKLTACFVGIRTVESLNRWRTIATGKKQT 182
Cdd:PRK08557  251 KEGIPTKDNRWCNSACKLMPL----KEYL-----------------KKKYGNKKVLTIDGSRKYESFTRANLDYERKSGF 309

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1101081741 183 MENKCwttwmgnilyNVYPIYDWRTEDIWTFHAKNpELAYNKLYDR 228
Cdd:PRK08557  310 IDFQT----------NVFPILDWNSLDIWSYIYLN-DILYNPLYDK 344
FAD_synthase cd23948
FAD synthase; FAD synthase (FMN:ATP adenylyl transferase (FMNAT); FAD pyrophosphorylase; ...
 19-228 9.93e-06

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: 45.59  E-value: 9.93e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101081741  19 VFDNFP--RIYVSFSGGKDSTVMLHLVAkEAIKRNR-----KIGVLFVDLEGQYKLTIDHIKECFSFYstiiepywiALP 91
Cdd:cd23948    12 ALDKYGpeEIAISFNGGKDCTVLLHLLR-AALKRKYpspltPLKALYIKSPDPFPEVEEFVEDTAKRY---------NLD 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101081741  92 LhlrnavsnfephwicwqpdrkkdwvrdfppfainnenyfsfFHYGMEFEEFVLSFGKWFGQGKltACFVGIRtveslnr 171
Cdd:cd23948    82 L-----------------------------------------ITIDGPMKEGLEELLKEHPIIK--AVFMGTR------- 111

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101081741 172 wRTIATGKKQTMENKC---WTTWMgnilyNVYPIYDWRTEDIWTFHaKNPELAYNKLYDR 228
Cdd:cd23948   112 -RTDPHGENLKPFSPTdpgWPQFM-----RVNPILDWSYHDVWEFL-RTLNLPYCSLYDQ 164
PRK02090 PRK02090
phosphoadenylyl-sulfate reductase;
11-228 1.27e-05

phosphoadenylyl-sulfate reductase;


Pssm-ID: 234997  Cd Length: 241  Bit Score: 45.98  E-value: 1.27e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101081741  11 AATQRIAWVFDNFPR--IYVSFSGGKDStVMLHLVAKEaikrNRKIGVLFVD---LEGQyklTIDHIKECFSFYSTIIEP 85
Cdd:PRK02090   27 SAQERLAWALENFGGrlALVSSFGAEDA-VLLHLVAQV----DPDIPVIFLDtgyLFPE---TYRFIDELTERLLLNLKV 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101081741  86 YwialplhlrnavsnfephwicwQPDRKKDWvrdfppfainnenyfsffhygmefeEFVLSFGKWFGQGKLT-ACfVGIR 164
Cdd:PRK02090   99 Y----------------------RPDASAAE-------------------------QEARYGGLWEQSVEDRdEC-CRIR 130

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1101081741 165 TVESLNR-------WrtiATGKKQ----TMENKCWTTWMGNIlYNVYPIYDWRTEDIWTFHAKNpELAYNKLYDR 228
Cdd:PRK02090  131 KVEPLNRalagldaW---ITGLRReqsgTRANLPVLEIDGGR-FKINPLADWTNEDVWAYLKEH-DLPYHPLVDQ 200
PRK13794 PRK13794
hypothetical protein; Provisional
 28-229 2.71e-05

hypothetical protein; Provisional


Pssm-ID: 237509 [Multi-domain]  Cd Length: 479  Bit Score: 46.20  E-value: 2.71e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101081741  28 VSFSGGKDSTVMLhLVAKEAIKRNrkIGVLFVDLEGQYKLTIDHIKECFSFYSTII-----EPYWIALPLHLRNAVSNfe 102
Cdd:PRK13794  252 VAYSGGKDSLATL-LLALKALGIN--FPVLFNDTGLEFPETLENVEDVEKHYGLEIirtksEEFWEKLEEYGPPARDN-- 326

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101081741 103 pHWIC----WQPDRKkdwvrdfppfaINNENYfsffhygmefEEFVLSfgkwfgqgkltacFVGIRTVESLNR------W 172
Cdd:PRK13794  327 -RWCSevckLEPLGK-----------LIDEKY----------EGECLS-------------FVGQRKYESFNRskkpriW 371

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1101081741 173 RTiATGKKQTmenkcwttwmgnilyNVYPIYDWRTEDIWTFHAKNpELAYNKLY----DRM 229
Cdd:PRK13794  372 RN-PYIKKQI---------------LAAPILHWTAMHVWIYLFRE-KAPYNKLYeqgfDRI 415
PAPS_reductase cd23945
Phosphoadenylyl-sulfate reductase (thioredoxin); Phosphoadenosine phosphosulfate (PAPS) ...
 12-228 4.72e-05

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: 43.74  E-value: 4.72e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101081741  12 ATQRIAWVFDNF-PRIYVSFSGGKDSTVMLHLVAKEaikrNRKIGVLFVDlegqyklTIDHIKECFSFYSTIIEPYwial 90
Cdd:cd23945     1 PLEILLWAAEEFgPKLVFATSFGAEDAVILDLLSKV----RPDIPVVFLD-------TGYLFPETYDLIDEVEARY---- 65

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101081741  91 plhlrnavsNFEPHwicwqpdrkkdwVRdFPPfAINNENYFsFFHYGMEFEEFVLsfgkwfgqGKLTACFvgIRTVESLN 170
Cdd:cd23945    66 ---------GLNIE------------VY-FPE-GTEAEEEA-LEGGLNEFYLEDE--------ERYDCCR--KRKPFPLA 111

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1101081741 171 R----WRTIATG--KKQTME----NKCWTTWMGNIL-YNvyPIYDWRTEDIWTFHAKNpELAYNKLYDR 228
Cdd:cd23945   112 LallgVKAWITGrrRDQSPTranlPIVEVDEEGGLVkIN--PLADWTWEDVWAYIREH-DLPYNPLHDQ 177
TilS_N cd01992
N-terminal domain of tRNA(Ile)-lysidine synthase and similar proteins; tRNA(Ile)-lysidine ...
 25-60 6.66e-05

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: 43.35  E-value: 6.66e-05
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 1101081741  25 RIYVSFSGGKDSTVMLHLVAKEAIKRNRKIGVLFVD 60
Cdd:cd01992     1 KILVAVSGGPDSMALLHLLKELRPKLGLKLVAVHVD 36
lysidine_TilS_N TIGR02432
tRNA(Ile)-lysidine synthetase, N-terminal domain; The only examples in which the wobble ...
 25-60 2.44e-04

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: 41.85  E-value: 2.44e-04
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 1101081741  25 RIYVSFSGGKDSTVMLHLVAKEAIKRNRKIGVLFVD 60
Cdd:TIGR02432   1 RILVAVSGGVDSMALLHLLLKLQPKIKIKLIAAHVD 36
AANH-like cd01986
adenine nucleotide alpha hydrolase (AANH)-like proteins; This group of adenine nucleotide ...
 28-74 3.74e-04

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: 38.59  E-value: 3.74e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 1101081741  28 VSFSGGKDSTVMLHLVAKEAikRNRKIGVLFVDLEGQYKLTIDHIKE 74
Cdd:cd01986     3 VGYSGGKDSSVALHLASRLG--RKAEVAVVHIDHGIGFKEEAESVAS 47
ATP_bind_3 pfam01171
PP-loop family; This family of proteins belongs to the PP-loop superfamily.
 28-60 4.18e-04

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


Pssm-ID: 426097 [Multi-domain]  Cd Length: 178  Bit Score: 40.69  E-value: 4.18e-04
                          10        20        30
                  ....*....|....*....|....*....|...
gi 1101081741  28 VSFSGGKDSTVMLHLVAKEAIKRNRKIGVLFVD 60
Cdd:pfam01171   1 VAVSGGPDSMALLYLLAKLKIKLGIELTAAHVN 33
PRK05253 PRK05253
sulfate adenylyltransferase subunit CysD;
30-45 1.26e-03

sulfate adenylyltransferase subunit CysD;


Pssm-ID: 235375  Cd Length: 301  Bit Score: 40.51  E-value: 1.26e-03
                          10
                  ....*....|....*.
gi 1101081741  30 FSGGKDSTVMLHLVAK 45
Cdd:PRK05253   34 YSIGKDSSVMLHLARK 49
CTU1-like cd01713
cytoplasmic tRNA 2-thiolation protein 1 and similar proteins; This subfamily includes human ...
 25-78 3.74e-03

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: 38.34  E-value: 3.74e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1101081741  25 RIYVSFSGGKDSTVMLHLVAK-----------------EAIKRNRKIGVLFV-DLEGQY--KLTIDHIKECFSF 78
Cdd:cd01713    20 RVAVGLSGGKDSTVLLYVLKElnkrhdygveliavtidEGIKGYRDDSLEAArKLAEEYgiPLEIVSFEDEFGF 93
 
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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