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Conserved domains on  [gi|1002166899|ref|YP_009230341|]
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phosphoadenosine phosphosulfate reductase [Acidianus tailed spindle virus]

Protein Classification

adenine nucleotide alpha hydrolase family protein( domain architecture ID 188)

AANH (adenine nucleotide alpha hydrolase) family protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
AANH_superfamily super family cl00292
Adenine nucleotide alpha hydrolase (AANH) superfamily; The adenine nucleotide alpha hydrolase ...
 8-179 7.07e-29

Adenine nucleotide alpha hydrolase (AANH) superfamily; The adenine nucleotide alpha hydrolase (AANH) superfamily includes N-type ATP PPases, ATP sulfurylases, universal stress response proteins (USPs), and electron transfer flavoproteins (ETFs). The domain forms an alpha/beta/alpha fold which binds to adenosine nucleotide.


The actual alignment was detected with superfamily member cd23947:

Pssm-ID: 469708 [Multi-domain]  Cd Length: 206  Bit Score: 108.63  E-value: 7.07e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002166899   8 EEAKKILLGFKEIYVMFSGGRDSLVALHLTHSIYPEKTK---ALFINTGIATPGLLDYVEGVTKELGIELTII------- 77
Cdd:cd23947     3 ERIRKVFEEFDPVIVSFSGGKDSLVLLHLALEALRRLRKdvyVVFIDTGIEFPETIDFVEKLAETLGLDVEAArpplfle 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002166899  78 --GSKYNYFELVNKIG-FPTLTKRWCKRYLKLEPLQDFVKDKKD--IILITGVRKSESwmKSRASKLYYNEKIGALS--- 149
Cdd:cd23947    83 wlTSNFQPQWDPIWDNpPPPRDYRWCCDELKLEPFTKWLKEKKPegVLLLVGIRADES--LNRAKRPRVYRKYGWRNstl 160

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1002166899 150 -----YAIVYDFTEQDVEEYIKANGLKKNYLYDIY 179
Cdd:cd23947   161 pgqivAYPIKDWSVEDVWLYILRHGLPYNPLYDLG 195
 
Name Accession Description Interval E-value
PAPS_reductase-like_YbdN cd23947
uncharacterized phosphoadenosine phosphosulfate reductase-like proteins, similar to ...
 8-179 7.07e-29

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: 108.63  E-value: 7.07e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002166899   8 EEAKKILLGFKEIYVMFSGGRDSLVALHLTHSIYPEKTK---ALFINTGIATPGLLDYVEGVTKELGIELTII------- 77
Cdd:cd23947     3 ERIRKVFEEFDPVIVSFSGGKDSLVLLHLALEALRRLRKdvyVVFIDTGIEFPETIDFVEKLAETLGLDVEAArpplfle 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002166899  78 --GSKYNYFELVNKIG-FPTLTKRWCKRYLKLEPLQDFVKDKKD--IILITGVRKSESwmKSRASKLYYNEKIGALS--- 149
Cdd:cd23947    83 wlTSNFQPQWDPIWDNpPPPRDYRWCCDELKLEPFTKWLKEKKPegVLLLVGIRADES--LNRAKRPRVYRKYGWRNstl 160

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1002166899 150 -----YAIVYDFTEQDVEEYIKANGLKKNYLYDIY 179
Cdd:cd23947   161 pgqivAYPIKDWSVEDVWLYILRHGLPYNPLYDLG 195
CysD COG0175
3'-phosphoadenosine 5'-phosphosulfate sulfotransferase (PAPS reductase)/FAD synthetase or ...
 18-177 2.01e-28

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: 108.01  E-value: 2.01e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002166899  18 KEIYVMFSGGRDSLVALHLTHSIYPeKTKALFINTGIATPGLLDYVEGVTKELGIELTIIGSKYNYFELVNKIGFPTLTK 97
Cdd:COG0175    34 GRVVVSSSGGKDSTVLLHLAAKFKP-PIPVLFLDTGYEFPETYEFRDRLAERLGLDLIVVRPEDAFAEQLAEFGPPLFYR 112

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002166899  98 --RWCKRYLKLEPLQDFVKDKKDIILITGVRKSESwmKSRASKLY--YNEKIGALSYAIVYDFTEQDVEEYIKANGLKKN 173
Cdd:COG0175   113 dpRWCCKIRKVEPLKRALAGYDFDAWITGLRRDES--PTRAKEPVveWDPVGGLIKVNPLADWTELDVWAYIRREDLPYN 190


                  ....
gi 1002166899 174 YLYD 177
Cdd:COG0175   191 PLYD 194
PAPS_reduct pfam01507
Phosphoadenosine phosphosulfate reductase family; This domain is found in phosphoadenosine ...
 19-189 9.35e-23

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: 91.59  E-value: 9.35e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002166899  19 EIYVMFSGGRDSLVALHLTHSIYPEKTkALFINTGIATPGLLDYVEGVTKELGIELTIIGSKYNYFELVNKIGFPTLTKR 98
Cdd:pfam01507   1 ELVVSFSGGKDSLVLLHLASKAFPPGP-VIFIDTGYEFPETYEFVDELEEKYGLNLKVYLPEDSFAEGINPEGIPSSLYR 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002166899  99 WCKRYLKLEPLQDFVKDKKDIILITGVRKSESwmKSRASKLYYNE--------KIGALSyaivyDFTEQDVEEYIKANGL 170
Cdd:pfam01507  80 RCCRLRKVEPLKRALKELGFDAWFTGLRRDES--PSRAKLPIVSIdgdfpkviKVFPLL-----NWTETDVWQYILANNV 152

                         170       180
                  ....*....|....*....|...
gi 1002166899 171 KKNYLYDiygKAYD---CW-CSA 189
Cdd:pfam01507 153 PYNPLYD---QGYRsigCYpCTG 172
PRK13795 PRK13795
hypothetical protein; Provisional
 20-219 2.16e-22

hypothetical protein; Provisional


Pssm-ID: 237510 [Multi-domain]  Cd Length: 636  Bit Score: 95.83  E-value: 2.16e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002166899  20 IYVMFSGGRDSLVALHLTHSIYPeKTKALFINTGIATPGLLDYVEGVTKELGIELTIIGSKYNYFELVNKIGFPTLTKRW 99
Cdd:PRK13795  246 VSVSFSGGKDSLVVLDLAREALK-DFKAFFNNTGLEFPETVENVKEVAEEYGIELIEADAGDAFWRAVEKFGPPARDYRW 324

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002166899 100 CKRYLKLEPLQDFVKD--KKDIILITGVRKSESWMKSRASKLYYNEKI-GALSYAIVYDFTEQDVEEYIKANGLKKNYLY 176
Cdd:PRK13795  325 CCKVCKLGPITRAIKEnfPKGCLTFVGQRKYESFSRAKSPRVWRNPWVpNQIGASPIQDWTALEVWLYIFWRKLPYNPLY 404

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1002166899 177 DiygKAYD---CW-CSAYKTpADFAVLALKNPEFFQKFveaEAKLRK 219
Cdd:PRK13795  405 E---RGFDrigCWlCPSSSL-AEFERLKELHPELYEKW---EAFLLK 444
 
Name Accession Description Interval E-value
PAPS_reductase-like_YbdN cd23947
uncharacterized phosphoadenosine phosphosulfate reductase-like proteins, similar to ...
 8-179 7.07e-29

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: 108.63  E-value: 7.07e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002166899   8 EEAKKILLGFKEIYVMFSGGRDSLVALHLTHSIYPEKTK---ALFINTGIATPGLLDYVEGVTKELGIELTII------- 77
Cdd:cd23947     3 ERIRKVFEEFDPVIVSFSGGKDSLVLLHLALEALRRLRKdvyVVFIDTGIEFPETIDFVEKLAETLGLDVEAArpplfle 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002166899  78 --GSKYNYFELVNKIG-FPTLTKRWCKRYLKLEPLQDFVKDKKD--IILITGVRKSESwmKSRASKLYYNEKIGALS--- 149
Cdd:cd23947    83 wlTSNFQPQWDPIWDNpPPPRDYRWCCDELKLEPFTKWLKEKKPegVLLLVGIRADES--LNRAKRPRVYRKYGWRNstl 160

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1002166899 150 -----YAIVYDFTEQDVEEYIKANGLKKNYLYDIY 179
Cdd:cd23947   161 pgqivAYPIKDWSVEDVWLYILRHGLPYNPLYDLG 195
CysD COG0175
3'-phosphoadenosine 5'-phosphosulfate sulfotransferase (PAPS reductase)/FAD synthetase or ...
 18-177 2.01e-28

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: 108.01  E-value: 2.01e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002166899  18 KEIYVMFSGGRDSLVALHLTHSIYPeKTKALFINTGIATPGLLDYVEGVTKELGIELTIIGSKYNYFELVNKIGFPTLTK 97
Cdd:COG0175    34 GRVVVSSSGGKDSTVLLHLAAKFKP-PIPVLFLDTGYEFPETYEFRDRLAERLGLDLIVVRPEDAFAEQLAEFGPPLFYR 112

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002166899  98 --RWCKRYLKLEPLQDFVKDKKDIILITGVRKSESwmKSRASKLY--YNEKIGALSYAIVYDFTEQDVEEYIKANGLKKN 173
Cdd:COG0175   113 dpRWCCKIRKVEPLKRALAGYDFDAWITGLRRDES--PTRAKEPVveWDPVGGLIKVNPLADWTELDVWAYIRREDLPYN 190


                  ....
gi 1002166899 174 YLYD 177
Cdd:COG0175   191 PLYD 194
PAPS_reduct pfam01507
Phosphoadenosine phosphosulfate reductase family; This domain is found in phosphoadenosine ...
 19-189 9.35e-23

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: 91.59  E-value: 9.35e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002166899  19 EIYVMFSGGRDSLVALHLTHSIYPEKTkALFINTGIATPGLLDYVEGVTKELGIELTIIGSKYNYFELVNKIGFPTLTKR 98
Cdd:pfam01507   1 ELVVSFSGGKDSLVLLHLASKAFPPGP-VIFIDTGYEFPETYEFVDELEEKYGLNLKVYLPEDSFAEGINPEGIPSSLYR 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002166899  99 WCKRYLKLEPLQDFVKDKKDIILITGVRKSESwmKSRASKLYYNE--------KIGALSyaivyDFTEQDVEEYIKANGL 170
Cdd:pfam01507  80 RCCRLRKVEPLKRALKELGFDAWFTGLRRDES--PSRAKLPIVSIdgdfpkviKVFPLL-----NWTETDVWQYILANNV 152

                         170       180
                  ....*....|....*....|...
gi 1002166899 171 KKNYLYDiygKAYD---CW-CSA 189
Cdd:pfam01507 153 PYNPLYD---QGYRsigCYpCTG 172
PRK13795 PRK13795
hypothetical protein; Provisional
 20-219 2.16e-22

hypothetical protein; Provisional


Pssm-ID: 237510 [Multi-domain]  Cd Length: 636  Bit Score: 95.83  E-value: 2.16e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002166899  20 IYVMFSGGRDSLVALHLTHSIYPeKTKALFINTGIATPGLLDYVEGVTKELGIELTIIGSKYNYFELVNKIGFPTLTKRW 99
Cdd:PRK13795  246 VSVSFSGGKDSLVVLDLAREALK-DFKAFFNNTGLEFPETVENVKEVAEEYGIELIEADAGDAFWRAVEKFGPPARDYRW 324

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002166899 100 CKRYLKLEPLQDFVKD--KKDIILITGVRKSESWMKSRASKLYYNEKI-GALSYAIVYDFTEQDVEEYIKANGLKKNYLY 176
Cdd:PRK13795  325 CCKVCKLGPITRAIKEnfPKGCLTFVGQRKYESFSRAKSPRVWRNPWVpNQIGASPIQDWTALEVWLYIFWRKLPYNPLY 404

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1002166899 177 DiygKAYD---CW-CSAYKTpADFAVLALKNPEFFQKFveaEAKLRK 219
Cdd:PRK13795  405 E---RGFDrigCWlCPSSSL-AEFERLKELHPELYEKW---EAFLLK 444
PRK08557 PRK08557
hypothetical protein; Provisional
 6-213 2.83e-19

hypothetical protein; Provisional


Pssm-ID: 181465 [Multi-domain]  Cd Length: 417  Bit Score: 86.35  E-value: 2.83e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002166899   6 VKEEAKKILLGFKEIY--------VMFSGGRDSLVALHLTHSIYPEkTKALFINTGIATPGLLDYVEGVTKELGIELTII 77
Cdd:PRK08557  162 LEENSLSILKDYIEKYknkgyainASFSGGKDSSVSTLLAKEVIPD-LEVIFIDTGLEYPETINYVKDFAKKYDLNLDTL 240

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002166899  78 GSKyNYFELVNKIGFPTLTKRWCKRYLKLEPLQDFVKDK---KDIILITGVRKSESWMKsraSKLYYNEKIGALSYAI-- 152
Cdd:PRK08557  241 DGD-NFWENLEKEGIPTKDNRWCNSACKLMPLKEYLKKKygnKKVLTIDGSRKYESFTR---ANLDYERKSGFIDFQTnv 316

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1002166899 153 --VYDFTEQDVEEYIKANGLKKNYLYDIYGKAYDCWCSAYKTPADFAVLALKNPEFFQKFVEA 213
Cdd:PRK08557  317 fpILDWNSLDIWSYIYLNDILYNPLYDKGFERIGCYLCPSALNSEFLRVKELYPELFNRWVKY 379
PRK13794 PRK13794
hypothetical protein; Provisional
 6-176 9.50e-19

hypothetical protein; Provisional


Pssm-ID: 237509 [Multi-domain]  Cd Length: 479  Bit Score: 85.10  E-value: 9.50e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002166899   6 VKEEAKKIllgFKEIYVMFSGGRDSLVALHLTHSIYPEKTKALFINTGIATPGLLDYVEGVTKELGIELTIIGSKyNYFE 85
Cdd:PRK13794  239 IRNTAEKI---NKPVTVAYSGGKDSLATLLLALKALGINFPVLFNDTGLEFPETLENVEDVEKHYGLEIIRTKSE-EFWE 314

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002166899  86 LVNKIGFPTLTKRWCKRYLKLEPLQDFVKDK--KDIILITGVRKSESWMKSRASKLYYNEKIGA-LSYAIVYDFTEQDVE 162
Cdd:PRK13794  315 KLEEYGPPARDNRWCSEVCKLEPLGKLIDEKyeGECLSFVGQRKYESFNRSKKPRIWRNPYIKKqILAAPILHWTAMHVW 394

                         170
                  ....*....|....
gi 1002166899 163 EYIKANGLKKNYLY 176
Cdd:PRK13794  395 IYLFREKAPYNKLY 408
PRK08576 PRK08576
hypothetical protein; Provisional
 1-176 7.13e-16

hypothetical protein; Provisional


Pssm-ID: 236300 [Multi-domain]  Cd Length: 438  Bit Score: 76.66  E-value: 7.13e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002166899   1 MDLLAVKEEA-KKILLGFKE--IYVMFSGGRDSLVALHLTHSIYpEKTKALFINTGIATPGLLDYVEGVTKELGIELTII 77
Cdd:PRK08576  215 REVLEAFEKAsIKFLRKFEEwtVIVPWSGGKDSTAALLLAKKAF-GDVTAVYVDTGYEMPLTDEYVEKVAEKLGVDLIRA 293

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002166899  78 GSKYNYfeLVNKIGFPTLTKRWCKrYLKLEPLQDFVKDKKDIILITGVRKSESwMKSRASKLYYNEKIGALSYAIVYD-- 155
Cdd:PRK08576  294 GVDVPM--PIEKYGMPTHSNRWCT-KLKVEALEEAIRELEDGLLVVGDRDGES-ARRRLRPPVVERKTNFGKILVVMPik 369

                         170       180
                  ....*....|....*....|..
gi 1002166899 156 -FTEQDVEEYIKANGLKKNYLY 176
Cdd:PRK08576  370 fWSGAMVQLYILMNGLELNPLY 391
PRK06850 PRK06850
hypothetical protein; Provisional
 1-165 2.19e-08

hypothetical protein; Provisional


Pssm-ID: 235877 [Multi-domain]  Cd Length: 507  Bit Score: 54.21  E-value: 2.19e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002166899   1 MDLLAVKEEAKKILLGFKEIY--------VMFSGGRDSLVALHLthsIY-------PEK-TKALFI---NTGIATPGLLD 61
Cdd:PRK06850   10 LVEYEDGEPIEELIEEIQELYcadnrpwvIGYSGGKDSTAVLQL---VWnalaglpPEKrTKPVYVissDTLVENPVVVD 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002166899  62 YV---------EGVTKELGIELTIIGSKYNYFELVNKIG----FPTLTKRWCKRYLKLEPLQDFVKDK----KDIILITG 124
Cdd:PRK06850   87 WVnkslerineAAKKQGLPITPHKLTPKINDTFWVNLIGkgypAPRRKFRWCTERLKIDPSNDFIKDKvsefGEVIVVLG 166

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1002166899 125 VRKSESwmKSRASKLYYNEKIGA-------LSYAIVY----DFTEQDVEEYI 165
Cdd:PRK06850  167 VRKAES--AARAQVMAKHEIEGSrlsrhttLPNAFVYtpieDWSNDDVWKYL 216
PAPS_reductase cd23945
Phosphoadenylyl-sulfate reductase (thioredoxin); Phosphoadenosine phosphosulfate (PAPS) ...
 20-177 2.35e-08

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: 52.60  E-value: 2.35e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002166899  20 IYVMFSGGRDSLVALHLTHSIYPeKTKALFINTGIATPGLLDYVEGVTKELGIELTIIGSKY-NYFELVNKIGFPTLTKR 98
Cdd:cd23945    16 LVFATSFGAEDAVILDLLSKVRP-DIPVVFLDTGYLFPETYDLIDEVEARYGLNIEVYFPEGtEAEEEALEGGLNEFYLE 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002166899  99 WCKRYL---KLEPLQDFVKDKKDIILITGVRKSESwmKSRAS--KLYYNEKIGALSYAIVYDFTEQDVEEYIKANGLKKN 173
Cdd:cd23945    95 DEERYDccrKRKPFPLALALLGVKAWITGRRRDQS--PTRANlpIVEVDEEGGLVKINPLADWTWEDVWAYIREHDLPYN 172


                  ....
gi 1002166899 174 YLYD 177
Cdd:cd23945   173 PLHD 176
PRK02090 PRK02090
phosphoadenylyl-sulfate reductase;
25-177 8.85e-08

phosphoadenylyl-sulfate reductase;


Pssm-ID: 234997  Cd Length: 241  Bit Score: 51.38  E-value: 8.85e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002166899  25 SGGRDSLVALHLTHSIYPeKTKALFINTGIATPGLLDYVEGVTKELGIELTIIGSKY-------NYFELVNKIGfpTLTK 97
Cdd:PRK02090   48 SFGAEDAVLLHLVAQVDP-DIPVIFLDTGYLFPETYRFIDELTERLLLNLKVYRPDAsaaeqeaRYGGLWEQSV--EDRD 124

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002166899  98 RWCK-RylKLEPLQDFVKDKKdiILITGVRKSESwmKSRAS--------KLYyneKIGALSyaivyDFTEQDVEEYIKAN 168
Cdd:PRK02090  125 ECCRiR--KVEPLNRALAGLD--AWITGLRREQS--GTRANlpvleidgGRF---KINPLA-----DWTNEDVWAYLKEH 190


                  ....*....
gi 1002166899 169 GLKKNYLYD 177
Cdd:PRK02090  191 DLPYHPLVD 199
LarE-like cd01990
Lactate racemization operon protein LarE and similar proteins; This subfamily includes ...
 22-171 1.71e-06

Lactate racemization operon protein LarE and similar proteins; This subfamily includes Lactiplantibacillus plantarum LarE, a sacrificial sulfur insertase of the N-type ATP pyrophosphatase family. LarE is part of the lar operon, encoding five Lar proteins (LarA-E) that collaboratively synthesize and incorporate a niacin-derived Ni-containing cofactor into LarA, an Ni-dependent lactate racemase. It catalyzes successive thiolation reactions by donating the sulfur atom of their exclusive cysteine residues to the substrate. The LarE-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. Proteins from this subfamily probably binds ATP. This domain is about 200 amino acids long with a strongly conserved motif SGGxDS at the N-terminus.


Pssm-ID: 467494 [Multi-domain]  Cd Length: 222  Bit Score: 47.64  E-value: 1.71e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002166899  22 VMFSGGRDSLVALHLTHSIYPEKTKALFINTGIATPGLLDYVEGVTKELGIELTIIgsKYNYFELVNKIGFPtlTKRW-- 99
Cdd:cd01990     4 VAFSGGVDSSLLAKLAKEVLGDNVVAVTADSPLVPREELEEAKRIAEEIGIRHEII--KTDELDDEEYVAND--PDRCyh 79

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1002166899 100 CKRYLkLEPLQDFVKDKKDIILITGVRKSESWMKSRAskLYYNEKIGALSYAIVYDFTEQDVEEYIKANGLK 171
Cdd:cd01990    80 CKKAL-YSTLKEIAKERGYDVVLDGTNADDLKDYRPG--LLAAAELGIRSPLPELGLTKSEIRELARELGLP 148
CTU1-like cd01713
cytoplasmic tRNA 2-thiolation protein 1 and similar proteins; This subfamily includes human ...
 6-78 1.00e-05

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: 45.27  E-value: 1.00e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002166899   6 VKEEAKKILLGFKEIY------VMFSGGRDSLVALHLTHSI-----YPEKTKALFINTGIA--TPGLLDYVEGVTKELGI 72
Cdd:cd01713     1 IERRVHRTIRKYRLIKpgdrvaVGLSGGKDSTVLLYVLKELnkrhdYGVELIAVTIDEGIKgyRDDSLEAARKLAEEYGI 80


                  ....*.
gi 1002166899  73 ELTIIG 78
Cdd:cd01713    81 PLEIVS 86
TilS COG0037
tRNA(Ile)-lysidine synthase TilS/MesJ [Translation, ribosomal structure and biogenesis]; tRNA ...
 8-92 3.24e-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: 40.97  E-value: 3.24e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002166899   8 EEAKKILLGFkeiyvmfSGGRDSLVALHLTHSIYPE---KTKALFINTGI--ATPGLLDYVEGVTKELGIELTIIGSKYN 82
Cdd:COG0037    13 EPGDRILVAV-------SGGKDSLALLHLLAKLRRRlgfELVAVHVDHGLreESDEDAEFVAELCEELGIPLHVVRVDVP 85

                          90
                  ....*....|
gi 1002166899  83 YFELVNKIGF 92
Cdd:COG0037    86 AIAKKEGKSP 95
AANH-like cd01986
adenine nucleotide alpha hydrolase (AANH)-like proteins; This group of adenine nucleotide ...
 22-63 6.91e-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: 37.43  E-value: 6.91e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 1002166899  22 VMFSGGRDSLVALHLTHS-IYPEKTKALFINTGIATPGLLDYV 63
Cdd:cd01986     3 VGYSGGKDSSVALHLASRlGRKAEVAVVHIDHGIGFKEEAESV 45
TtuA-like cd01993
tRNA-5-methyluridine(54) 2-sulfurtransferase and similar proteins; tRNA-5-methyluridine(54) ...
 20-83 8.75e-03

tRNA-5-methyluridine(54) 2-sulfurtransferase and similar proteins; tRNA-5-methyluridine(54) 2-sulfurtransferase, also called tRNA thiouridine synthetase TtuA, catalyzes the ATP-dependent 2-thiolation of 5-methyluridine residue at position 54 in the T loop of tRNAs, leading to 5-methyl-2-thiouridine (m(5)s(2)U or s(2)T). TtuA 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: 467497 [Multi-domain]  Cd Length: 190  Bit Score: 36.15  E-value: 8.75e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1002166899  20 IYVMFSGGRDSLVALHLTHSIYPEkTKALFINTGIA--TPGLLDYVEGVTKELGIELTIIGSKYNY 83
Cdd:cd01993    11 ILVAVSGGKDSLALLAVLKKLGYN-VEALYINLGIGeySEKSEEVVKKLAEKLNLPLHVVDLKEEY 75
 
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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