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Conserved domains on  [gi|752746905|ref|WP_041394026|]
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phosphoadenosine phosphosulfate reductase [Photobacterium profundum]

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 ...
 1-402 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: 637.37  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752746905   1 MKRQLGKDVVQAARERIHILFDEFEHIYVSFSGGKDSGVLLHLVIEEARKRNRlPVDVLIVDLEAQYQHTIHFVERMVNK 80
Cdd:COG3969    1 MKKYLDENVYEAAQERIEWIFDEFDRVCVSFSGGKDSGVLLHLAAEVARKNGR-KIDVLFIDWEAQYSATIDHVEEMFER 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752746905  81 KE--VNAFWVCLPLSLRNSVSQFQPKWICWDPDKKEDWIRALPLHAsVINEEEYFSFYSFGMEFETFVSAFGEWYSEKKq 158
Cdd:COG3969   80 YEdvVRFYWVCLPLTTRNAVSQFQPEWYCWDPGKKEDWVRPMPEHD-VITDPNFFPFYRYGMEFEEFVPAFGRWLSGKH- 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752746905 159 cPCACLVAIRADESLNRYKTIKNQRKKR-LKQYGWTTKASDVFYKAYLIYDWHVTDIWIANGRFNWDYNHVYDLMHKAGL 237
Cdd:COG3969  158 -PTACLVGIRADESLNRYLAIASQRKLRyYKDKPWTTAPFGNAYNAYPLYDWKTEDIWTANAKFGYDYNRLYDLMYQAGV 236

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752746905 238 SLAQQRLCQPFGDDQRKGLWLYQILEPQTWQKLVVRVEGCNFGARYSKKqgHILGYYKFDLPEGYTYRSYSKYLLNSMPP 317
Cdd:COG3969  237 PLSQMRVCEPFGDEQRKGLWLYHVLEPETWAKLVGRVNGANFGAIYGGT--KALGYRKISLPEGHTWRSYALFLLDSMPE 314

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752746905 318 HLADHYRKRLFKFLNWWRKNGKEQGIlsIPDFADKKLEAKKKVPSWRRICKVLIKNDYWCRGLSFGQSKKLTEHYIDLYE 397
Cdd:COG3969  315 RTAEHYRNKIAVSLRWWQKRGGPLDE--IPDDQDKDIEGTKDIPSWRRICKCILKNDYWCRSLSFGPTKSEIYRRYALRE 392


                 ....*
gi 752746905 398 GYFRK 402
Cdd:COG3969  393 KYKRI 397
 
Name Accession Description Interval E-value
YbdN COG3969
Predicted phosphoadenosine phosphosulfate sulfurtransferase, contains C-terminal DUF3440 ...
 1-402 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: 637.37  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752746905   1 MKRQLGKDVVQAARERIHILFDEFEHIYVSFSGGKDSGVLLHLVIEEARKRNRlPVDVLIVDLEAQYQHTIHFVERMVNK 80
Cdd:COG3969    1 MKKYLDENVYEAAQERIEWIFDEFDRVCVSFSGGKDSGVLLHLAAEVARKNGR-KIDVLFIDWEAQYSATIDHVEEMFER 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752746905  81 KE--VNAFWVCLPLSLRNSVSQFQPKWICWDPDKKEDWIRALPLHAsVINEEEYFSFYSFGMEFETFVSAFGEWYSEKKq 158
Cdd:COG3969   80 YEdvVRFYWVCLPLTTRNAVSQFQPEWYCWDPGKKEDWVRPMPEHD-VITDPNFFPFYRYGMEFEEFVPAFGRWLSGKH- 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752746905 159 cPCACLVAIRADESLNRYKTIKNQRKKR-LKQYGWTTKASDVFYKAYLIYDWHVTDIWIANGRFNWDYNHVYDLMHKAGL 237
Cdd:COG3969  158 -PTACLVGIRADESLNRYLAIASQRKLRyYKDKPWTTAPFGNAYNAYPLYDWKTEDIWTANAKFGYDYNRLYDLMYQAGV 236

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752746905 238 SLAQQRLCQPFGDDQRKGLWLYQILEPQTWQKLVVRVEGCNFGARYSKKqgHILGYYKFDLPEGYTYRSYSKYLLNSMPP 317
Cdd:COG3969  237 PLSQMRVCEPFGDEQRKGLWLYHVLEPETWAKLVGRVNGANFGAIYGGT--KALGYRKISLPEGHTWRSYALFLLDSMPE 314

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752746905 318 HLADHYRKRLFKFLNWWRKNGKEQGIlsIPDFADKKLEAKKKVPSWRRICKVLIKNDYWCRGLSFGQSKKLTEHYIDLYE 397
Cdd:COG3969  315 RTAEHYRNKIAVSLRWWQKRGGPLDE--IPDDQDKDIEGTKDIPSWRRICKCILKNDYWCRSLSFGPTKSEIYRRYALRE 392


                 ....*
gi 752746905 398 GYFRK 402
Cdd:COG3969  393 KYKRI 397
PAPS_reductase-like_YbdN cd23947
uncharacterized phosphoadenosine phosphosulfate reductase-like proteins, similar to ...
 13-243 5.98e-75

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: 231.90  E-value: 5.98e-75
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752746905  13 ARERIHILFDEFEHIYVSFSGGKDSGVLLHLVIEEARkRNRLPVDVLIVDLEAQYQHTIHFVERMVNKKEVNAFWVCLPL 92
Cdd:cd23947    1 ALERIRKVFEEFDPVIVSFSGGKDSLVLLHLALEALR-RLRKDVYVVFIDTGIEFPETIDFVEKLAETLGLDVEAARPPL 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752746905  93 SLRNSVSQFQPKWICwdpdkkedwiralplhasvINEEEYFSFYSFGMEFETFVSAFGEWYSEKKQCPCACLVAIRADES 172
Cdd:cd23947   80 FLEWLTSNFQPQWDP-------------------IWDNPPPPRDYRWCCDELKLEPFTKWLKEKKPEGVLLLVGIRADES 140

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 752746905 173 LNRYKTIKNQRKkrlkqYGWTTKASDVFYKAYLIYDWHVTDIWIANGRFNWDYNHVYDLMHKAGLSLAQQR 243
Cdd:cd23947  141 LNRAKRPRVYRK-----YGWRNSTLPGQIVAYPIKDWSVEDVWLYILRHGLPYNPLYDLGFDRGGCLVCPR 206
DUF3440 pfam11922
Domain of unknown function (DUF3440); This presumed domain is functionally uncharacterized. ...
 236-387 1.71e-35

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: 128.54  E-value: 1.71e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752746905  236 GLSLAQQRLCQPFGDDQRKGLWLYQILEPQTWQKLVVRVEGCNFGARYSKKqgHILGYYKFDLPEGYTYRSYSKYLLNSM 315
Cdd:pfam11922   1 GVPLEQMRVASPFISAAIESLKLYRVIDPDTWGKMIGRVNGVNFAGIYGGT--KAMGWRSIKLPEGHTWKSYMYFLLSTL 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752746905  316 PPHLADHYRKRLFKFLNWWRKNG-----------KEQGI------------------LSIPDfaDKKLEAKKKVPSWRRI 366
Cdd:pfam11922  79 PEETRNNYLKKLSVSIKFWREKGgclseetieelKAAGIpievggksnyttdkrpvrMEYPD--DIDIKEFKEIPTYKRM 156

                         170       180
                  ....*....|....*....|.
gi 752746905  367 CKVLIKNDYWCRGLSFGQSKK 387
Cdd:pfam11922 157 CICILKNDHTCKYMGFGPTKE 177
PRK05253 PRK05253
sulfate adenylyltransferase subunit CysD;
15-78 3.75e-06

sulfate adenylyltransferase subunit CysD;


Pssm-ID: 235375  Cd Length: 301  Bit Score: 48.21  E-value: 3.75e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752746905  15 ERIHIL---FDEFEHIYVSFSGGKDSGVLLHLvieeARK---RNRLPVDVLIVDLEAQYQHTIHFVERMV 78
Cdd:PRK05253  15 ESIHILrevAAEFENPVMLYSIGKDSSVMLHL----ARKafyPGKLPFPLLHVDTGWKFPEMIEFRDRRA 80
 
Name Accession Description Interval E-value
YbdN COG3969
Predicted phosphoadenosine phosphosulfate sulfurtransferase, contains C-terminal DUF3440 ...
 1-402 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: 637.37  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752746905   1 MKRQLGKDVVQAARERIHILFDEFEHIYVSFSGGKDSGVLLHLVIEEARKRNRlPVDVLIVDLEAQYQHTIHFVERMVNK 80
Cdd:COG3969    1 MKKYLDENVYEAAQERIEWIFDEFDRVCVSFSGGKDSGVLLHLAAEVARKNGR-KIDVLFIDWEAQYSATIDHVEEMFER 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752746905  81 KE--VNAFWVCLPLSLRNSVSQFQPKWICWDPDKKEDWIRALPLHAsVINEEEYFSFYSFGMEFETFVSAFGEWYSEKKq 158
Cdd:COG3969   80 YEdvVRFYWVCLPLTTRNAVSQFQPEWYCWDPGKKEDWVRPMPEHD-VITDPNFFPFYRYGMEFEEFVPAFGRWLSGKH- 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752746905 159 cPCACLVAIRADESLNRYKTIKNQRKKR-LKQYGWTTKASDVFYKAYLIYDWHVTDIWIANGRFNWDYNHVYDLMHKAGL 237
Cdd:COG3969  158 -PTACLVGIRADESLNRYLAIASQRKLRyYKDKPWTTAPFGNAYNAYPLYDWKTEDIWTANAKFGYDYNRLYDLMYQAGV 236

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752746905 238 SLAQQRLCQPFGDDQRKGLWLYQILEPQTWQKLVVRVEGCNFGARYSKKqgHILGYYKFDLPEGYTYRSYSKYLLNSMPP 317
Cdd:COG3969  237 PLSQMRVCEPFGDEQRKGLWLYHVLEPETWAKLVGRVNGANFGAIYGGT--KALGYRKISLPEGHTWRSYALFLLDSMPE 314

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752746905 318 HLADHYRKRLFKFLNWWRKNGKEQGIlsIPDFADKKLEAKKKVPSWRRICKVLIKNDYWCRGLSFGQSKKLTEHYIDLYE 397
Cdd:COG3969  315 RTAEHYRNKIAVSLRWWQKRGGPLDE--IPDDQDKDIEGTKDIPSWRRICKCILKNDYWCRSLSFGPTKSEIYRRYALRE 392


                 ....*
gi 752746905 398 GYFRK 402
Cdd:COG3969  393 KYKRI 397
PAPS_reductase-like_YbdN cd23947
uncharacterized phosphoadenosine phosphosulfate reductase-like proteins, similar to ...
 13-243 5.98e-75

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: 231.90  E-value: 5.98e-75
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752746905  13 ARERIHILFDEFEHIYVSFSGGKDSGVLLHLVIEEARkRNRLPVDVLIVDLEAQYQHTIHFVERMVNKKEVNAFWVCLPL 92
Cdd:cd23947    1 ALERIRKVFEEFDPVIVSFSGGKDSLVLLHLALEALR-RLRKDVYVVFIDTGIEFPETIDFVEKLAETLGLDVEAARPPL 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752746905  93 SLRNSVSQFQPKWICwdpdkkedwiralplhasvINEEEYFSFYSFGMEFETFVSAFGEWYSEKKQCPCACLVAIRADES 172
Cdd:cd23947   80 FLEWLTSNFQPQWDP-------------------IWDNPPPPRDYRWCCDELKLEPFTKWLKEKKPEGVLLLVGIRADES 140

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 752746905 173 LNRYKTIKNQRKkrlkqYGWTTKASDVFYKAYLIYDWHVTDIWIANGRFNWDYNHVYDLMHKAGLSLAQQR 243
Cdd:cd23947  141 LNRAKRPRVYRK-----YGWRNSTLPGQIVAYPIKDWSVEDVWLYILRHGLPYNPLYDLGFDRGGCLVCPR 206
DUF3440 pfam11922
Domain of unknown function (DUF3440); This presumed domain is functionally uncharacterized. ...
 236-387 1.71e-35

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: 128.54  E-value: 1.71e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752746905  236 GLSLAQQRLCQPFGDDQRKGLWLYQILEPQTWQKLVVRVEGCNFGARYSKKqgHILGYYKFDLPEGYTYRSYSKYLLNSM 315
Cdd:pfam11922   1 GVPLEQMRVASPFISAAIESLKLYRVIDPDTWGKMIGRVNGVNFAGIYGGT--KAMGWRSIKLPEGHTWKSYMYFLLSTL 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752746905  316 PPHLADHYRKRLFKFLNWWRKNG-----------KEQGI------------------LSIPDfaDKKLEAKKKVPSWRRI 366
Cdd:pfam11922  79 PEETRNNYLKKLSVSIKFWREKGgclseetieelKAAGIpievggksnyttdkrpvrMEYPD--DIDIKEFKEIPTYKRM 156

                         170       180
                  ....*....|....*....|.
gi 752746905  367 CKVLIKNDYWCRGLSFGQSKK 387
Cdd:pfam11922 157 CICILKNDHTCKYMGFGPTKE 177
PAPS_reduct pfam01507
Phosphoadenosine phosphosulfate reductase family; This domain is found in phosphoadenosine ...
 26-230 4.04e-07

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: 49.60  E-value: 4.04e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752746905   26 HIYVSFSGGKDSGVLLHLvieeARKRNRlPVDVLIVDLEAQYQHTIHFVERMVNKKEVNafwVCLPLSLRNSVSQFQP-K 104
Cdd:pfam01507   1 ELVVSFSGGKDSLVLLHL----ASKAFP-PGPVIFIDTGYEFPETYEFVDELEEKYGLN---LKVYLPEDSFAEGINPeG 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752746905  105 WICWDPDKKEDWIRALPLHasvineeEYFSFYSFGmefetfvsafgewysekkqcpcACLVAIRADESLNRYKtiknqrk 184
Cdd:pfam01507  73 IPSSLYRRCCRLRKVEPLK-------RALKELGFD----------------------AWFTGLRRDESPSRAK------- 116

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 752746905  185 krlKQYGWTTKASDVFYKAYLIYDWHVTDIWIANGRFNWDYNHVYD 230
Cdd:pfam01507 117 ---LPIVSIDGDFPKVIKVFPLLNWTETDVWQYILANNVPYNPLYD 159
CysD COG0175
3'-phosphoadenosine 5'-phosphosulfate sulfotransferase (PAPS reductase)/FAD synthetase or ...
 3-80 7.46e-07

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: 49.84  E-value: 7.46e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 752746905   3 RQLGKDVVQAARERIHILFDEF-EHIYVSFSGGKDSGVLLHLVieearKRNRLPVDVLIVDLEAQYQHTIHFVERMVNK 80
Cdd:COG0175   11 EELNAELEAEAIEILREAAAEFgGRVVVSSSGGKDSTVLLHLA-----AKFKPPIPVLFLDTGYEFPETYEFRDRLAER 84
PRK05253 PRK05253
sulfate adenylyltransferase subunit CysD;
15-78 3.75e-06

sulfate adenylyltransferase subunit CysD;


Pssm-ID: 235375  Cd Length: 301  Bit Score: 48.21  E-value: 3.75e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752746905  15 ERIHIL---FDEFEHIYVSFSGGKDSGVLLHLvieeARK---RNRLPVDVLIVDLEAQYQHTIHFVERMV 78
Cdd:PRK05253  15 ESIHILrevAAEFENPVMLYSIGKDSSVMLHL----ARKafyPGKLPFPLLHVDTGWKFPEMIEFRDRRA 80
PRK12563 PRK12563
sulfate adenylyltransferase subunit CysD;
15-80 1.19e-05

sulfate adenylyltransferase subunit CysD;


Pssm-ID: 237138  Cd Length: 312  Bit Score: 46.71  E-value: 1.19e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 752746905  15 ERIHILFD---EFEHIYVSFSGGKDSGVLLHLVIeEARKRNRLPVDVLIVDLEAQYQHTIHFVERMVNK 80
Cdd:PRK12563  25 ESIHILREvvaECSKPVMLYSIGKDSVVMLHLAM-KAFRPTRPPFPLLHVDTTWKFREMIDFRDRRAKE 92
AANH-like cd01986
adenine nucleotide alpha hydrolase (AANH)-like proteins; This group of adenine nucleotide ...
 29-88 1.21e-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: 40.13  E-value: 1.21e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 752746905  29 VSFSGGKDSGVLLHLVIEEARKRnrlPVDVLIVDLEAQYQHTIHFVERMVNKKEVNAFWV 88
Cdd:cd01986    3 VGYSGGKDSSVALHLASRLGRKA---EVAVVHIDHGIGFKEEAESVASIARRSILKKLAE 59
FAD_synthase cd23948
FAD synthase; FAD synthase (FMN:ATP adenylyl transferase (FMNAT); FAD pyrophosphorylase; ...
 10-80 1.72e-04

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: 42.12  E-value: 1.72e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 752746905  10 VQAARERIHILFDEF--EHIYVSFSGGKDSGVLLHL---VIEEARKRNRLPVDVLIVDLEAQYQHTIHFVERMVNK 80
Cdd:cd23948    2 VKSALEVIEEALDKYgpEEIAISFNGGKDCTVLLHLlraALKRKYPSPLTPLKALYIKSPDPFPEVEEFVEDTAKR 77
TilS COG0037
tRNA(Ile)-lysidine synthase TilS/MesJ [Translation, ribosomal structure and biogenesis]; tRNA ...
 9-77 2.21e-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: 42.51  E-value: 2.21e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 752746905   9 VVQAAREriHILFDEFEHIYVSFSGGKDSGVLLHLVIEEARKRNrLPVDVLIVD--LEAQYQHTIHFVERM 77
Cdd:COG0037    2 VRKAIRD--YRLLEPGDRILVAVSGGKDSLALLHLLAKLRRRLG-FELVAVHVDhgLREESDEDAEFVAEL 69
PRK13795 PRK13795
hypothetical protein; Provisional
 27-87 5.75e-04

hypothetical protein; Provisional


Pssm-ID: 237510 [Multi-domain]  Cd Length: 636  Bit Score: 41.90  E-value: 5.75e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 752746905  27 IYVSFSGGKDSGVLLHLVIEEARKrnrlpVDVLIVDLEAQYQHTIHFVERMVNKKEV--------NAFW 87
Cdd:PRK13795 246 VSVSFSGGKDSLVVLDLAREALKD-----FKAFFNNTGLEFPETVENVKEVAEEYGIelieadagDAFW 309
Sulfate_adenylyltransferase_2 cd23946
Sulfate adenylyltransferase subunit 2; Sulfate adenylyltransferase subunits 1 and 2 form ATP ...
 15-80 9.19e-04

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: 40.17  E-value: 9.19e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 752746905  15 ERIHIL---FDEFEHIYVSFSGGKDSGVLLHLViEEARKRNRLPVDVLIVDLEAQYQHTIHFVERMVNK 80
Cdd:cd23946    8 ESIHIIrevAAEFSNPVMLYSIGKDSSVMLHLA-RKAFYPGKPPFPLLHVDTTWKFREMIEFRDRVAKE 75
CTU1-like cd01713
cytoplasmic tRNA 2-thiolation protein 1 and similar proteins; This subfamily includes human ...
 7-61 1.38e-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: 39.88  E-value: 1.38e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 752746905   7 KDVVQAAREriHILFDEFEHIYVSFSGGKDSGVLLHlVIEEARKRNRLPVDVLIV 61
Cdd:cd01713    3 RRVHRTIRK--YRLIKPGDRVAVGLSGGKDSTVLLY-VLKELNKRHDYGVELIAV 54
 
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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