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Conserved domains on  [gi|502612537|ref|WP_012849506|]
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phosphoadenosine phosphosulfate reductase [Edwardsiella piscicida]

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 ...
 2-403 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: 681.67  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612537   2 KKIPLKENVFVAAYARMNWVFETFPRVCVSFSGGKDSTVLLHIAAEVARRKKRRLFVLFVDWEVQFSHTIQHIESMRQRY 81
Cdd:COG3969    1 MKKYLDENVYEAAQERIEWIFDEFDRVCVSFSGGKDSGVLLHLAAEVARKNGRKIDVLFIDWEAQYSATIDHVEEMFERY 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612537  82 QDVIeRFFWVALPLTTASGVSQYETEWTCWQPGV--TWVRQPPP-DAITDPDFFPFYTSGISFEAFVVAFSLWLSGRKSM 158
Cdd:COG3969   81 EDVV-RFYWVCLPLTTRNAVSQFQPEWYCWDPGKkeDWVRPMPEhDVITDPNFFPFYRYGMEFEEFVPAFGRWLSGKHPT 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612537 159 ATLVGIRADESLNRFMAVASQSKLRYDDDKPWTTAsQDGFYYTAYPLYDWKVSDIWHFNAQQRLPYNPLYDLMYRAGVPL 238
Cdd:COG3969  160 ACLVGIRADESLNRYLAIASQRKLRYYKDKPWTTA-PFGNAYNAYPLYDWKTEDIWTANAKFGYDYNRLYDLMYQAGVPL 238

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612537 239 RQMRICEPFGPEQRKGLWLYHVLEPTTWGRACSRVAGANGGAIYANQSgaFYAlNRQIDKPPQHTWKSYVHYLLASMPQK 318
Cdd:COG3969  239 SQMRVCEPFGDEQRKGLWLYHVLEPETWAKLVGRVNGANFGAIYGGTK--ALG-YRKISLPEGHTWRSYALFLLDSMPER 315

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612537 319 TAEHYRNKIAIYLRWYQRHGYPQD-IPDSQESDL-GARDIPSWRRICKTLIKNDFWCRSLSFSPNRPQAYARYVKRIQQK 396
Cdd:COG3969  316 TAEHYRNKIAVSLRWWQKRGGPLDeIPDDQDKDIeGTKDIPSWRRICKCILKNDYWCRSLSFGPTKSEIYRRYALREKYK 395


                 ....*..
gi 502612537 397 RHQWEII 403
Cdd:COG3969  396 RILWGIL 402
 
Name Accession Description Interval E-value
YbdN COG3969
Predicted phosphoadenosine phosphosulfate sulfurtransferase, contains C-terminal DUF3440 ...
 2-403 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: 681.67  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612537   2 KKIPLKENVFVAAYARMNWVFETFPRVCVSFSGGKDSTVLLHIAAEVARRKKRRLFVLFVDWEVQFSHTIQHIESMRQRY 81
Cdd:COG3969    1 MKKYLDENVYEAAQERIEWIFDEFDRVCVSFSGGKDSGVLLHLAAEVARKNGRKIDVLFIDWEAQYSATIDHVEEMFERY 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612537  82 QDVIeRFFWVALPLTTASGVSQYETEWTCWQPGV--TWVRQPPP-DAITDPDFFPFYTSGISFEAFVVAFSLWLSGRKSM 158
Cdd:COG3969   81 EDVV-RFYWVCLPLTTRNAVSQFQPEWYCWDPGKkeDWVRPMPEhDVITDPNFFPFYRYGMEFEEFVPAFGRWLSGKHPT 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612537 159 ATLVGIRADESLNRFMAVASQSKLRYDDDKPWTTAsQDGFYYTAYPLYDWKVSDIWHFNAQQRLPYNPLYDLMYRAGVPL 238
Cdd:COG3969  160 ACLVGIRADESLNRYLAIASQRKLRYYKDKPWTTA-PFGNAYNAYPLYDWKTEDIWTANAKFGYDYNRLYDLMYQAGVPL 238

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612537 239 RQMRICEPFGPEQRKGLWLYHVLEPTTWGRACSRVAGANGGAIYANQSgaFYAlNRQIDKPPQHTWKSYVHYLLASMPQK 318
Cdd:COG3969  239 SQMRVCEPFGDEQRKGLWLYHVLEPETWAKLVGRVNGANFGAIYGGTK--ALG-YRKISLPEGHTWRSYALFLLDSMPER 315

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612537 319 TAEHYRNKIAIYLRWYQRHGYPQD-IPDSQESDL-GARDIPSWRRICKTLIKNDFWCRSLSFSPNRPQAYARYVKRIQQK 396
Cdd:COG3969  316 TAEHYRNKIAVSLRWWQKRGGPLDeIPDDQDKDIeGTKDIPSWRRICKCILKNDYWCRSLSFGPTKSEIYRRYALREKYK 395


                 ....*..
gi 502612537 397 RHQWEII 403
Cdd:COG3969  396 RILWGIL 402
PAPS_reductase-like_YbdN cd23947
uncharacterized phosphoadenosine phosphosulfate reductase-like proteins, similar to ...
 14-242 2.03e-63

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: 202.24  E-value: 2.03e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612537  14 AYARMNWVFETFPRVCVSFSGGKDSTVLLHIAAEVARRKKRRLFVLFVDWEVQFSHTIQHIESMRQRY-QDVIERFFWVA 92
Cdd:cd23947    1 ALERIRKVFEEFDPVIVSFSGGKDSLVLLHLALEALRRLRKDVYVVFIDTGIEFPETIDFVEKLAETLgLDVEAARPPLF 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612537  93 LplttasgvsqyetEWTCWQPgvtwvrQPPPDAITDPDFFPFYTSGISFEAFVVAFSLWLSGRKSM--ATLVGIRADESL 170
Cdd:cd23947   81 L-------------EWLTSNF------QPQWDPIWDNPPPPRDYRWCCDELKLEPFTKWLKEKKPEgvLLLVGIRADESL 141

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 502612537 171 NRFMAVASQSklrydddKPWTTASQDGFYYTAYPLYDWKVSDIWHFNAQQRLPYNPLYDLMYRAGVPLRQMR 242
Cdd:cd23947  142 NRAKRPRVYR-------KYGWRNSTLPGQIVAYPIKDWSVEDVWLYILRHGLPYNPLYDLGFDRGGCLVCPR 206
DUF3440 pfam11922
Domain of unknown function (DUF3440); This presumed domain is functionally uncharacterized. ...
 235-384 6.94e-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: 127.00  E-value: 6.94e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612537  235 GVPLRQMRICEPFGPEQRKGLWLYHVLEPTTWGRACSRVAGANGGAIYANQSGAFYalnRQIDKPPQHTWKSYVHYLLAS 314
Cdd:pfam11922   1 GVPLEQMRVASPFISAAIESLKLYRVIDPDTWGKMIGRVNGVNFAGIYGGTKAMGW---RSIKLPEGHTWKSYMYFLLST 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612537  315 MPQKTAEHYRNKIAIYLRWYQRHG------------------------------------YPQDIPDSQesdlgARDIPS 358
Cdd:pfam11922  78 LPEETRNNYLKKLSVSIKFWREKGgclseetieelkaagipievggksnyttdkrpvrmeYPDDIDIKE-----FKEIPT 152

                         170       180
                  ....*....|....*....|....*.
gi 502612537  359 WRRICKTLIKNDFWCRSLSFSPNRPQ 384
Cdd:pfam11922 153 YKRMCICILKNDHTCKYMGFGPTKEE 178
PRK13795 PRK13795
hypothetical protein; Provisional
 28-229 5.11e-08

hypothetical protein; Provisional


Pssm-ID: 237510 [Multi-domain]  Cd Length: 636  Bit Score: 55.00  E-value: 5.11e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612537  28 VCVSFSGGKDSTVLLHIAAEVArrkkRRLFVLFVDWEVQFSHTIQHIESMRQRYQ-DVIE----RFFWVALPLTTASGVs 102
Cdd:PRK13795 246 VSVSFSGGKDSLVVLDLAREAL----KDFKAFFNNTGLEFPETVENVKEVAEEYGiELIEadagDAFWRAVEKFGPPAR- 320

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612537 103 qyETEWTCwqpGVTWVrQPPPDAITdpDFFPfytsgisfeafvvafslwlsgrKSMATLVGIRADESLNRfmavasqSKL 182
Cdd:PRK13795 321 --DYRWCC---KVCKL-GPITRAIK--ENFP----------------------KGCLTFVGQRKYESFSR-------AKS 363

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 502612537 183 RYDDDKPWtTASQDGfyytAYPLYDWKVSDIWHFNAQQRLPYNPLYD 229
Cdd:PRK13795 364 PRVWRNPW-VPNQIG----ASPIQDWTALEVWLYIFWRKLPYNPLYE 405
lysidine_TilS_N TIGR02432
tRNA(Ile)-lysidine synthetase, N-terminal domain; The only examples in which the wobble ...
 27-62 4.38e-05

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: 43.77  E-value: 4.38e-05
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 502612537   27 RVCVSFSGGKDSTVLLHIAAEVARRKKRRLFVLFVD 62
Cdd:TIGR02432   1 RILVAVSGGVDSMALLHLLLKLQPKIKIKLIAAHVD 36
 
Name Accession Description Interval E-value
YbdN COG3969
Predicted phosphoadenosine phosphosulfate sulfurtransferase, contains C-terminal DUF3440 ...
 2-403 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: 681.67  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612537   2 KKIPLKENVFVAAYARMNWVFETFPRVCVSFSGGKDSTVLLHIAAEVARRKKRRLFVLFVDWEVQFSHTIQHIESMRQRY 81
Cdd:COG3969    1 MKKYLDENVYEAAQERIEWIFDEFDRVCVSFSGGKDSGVLLHLAAEVARKNGRKIDVLFIDWEAQYSATIDHVEEMFERY 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612537  82 QDVIeRFFWVALPLTTASGVSQYETEWTCWQPGV--TWVRQPPP-DAITDPDFFPFYTSGISFEAFVVAFSLWLSGRKSM 158
Cdd:COG3969   81 EDVV-RFYWVCLPLTTRNAVSQFQPEWYCWDPGKkeDWVRPMPEhDVITDPNFFPFYRYGMEFEEFVPAFGRWLSGKHPT 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612537 159 ATLVGIRADESLNRFMAVASQSKLRYDDDKPWTTAsQDGFYYTAYPLYDWKVSDIWHFNAQQRLPYNPLYDLMYRAGVPL 238
Cdd:COG3969  160 ACLVGIRADESLNRYLAIASQRKLRYYKDKPWTTA-PFGNAYNAYPLYDWKTEDIWTANAKFGYDYNRLYDLMYQAGVPL 238

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612537 239 RQMRICEPFGPEQRKGLWLYHVLEPTTWGRACSRVAGANGGAIYANQSgaFYAlNRQIDKPPQHTWKSYVHYLLASMPQK 318
Cdd:COG3969  239 SQMRVCEPFGDEQRKGLWLYHVLEPETWAKLVGRVNGANFGAIYGGTK--ALG-YRKISLPEGHTWRSYALFLLDSMPER 315

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612537 319 TAEHYRNKIAIYLRWYQRHGYPQD-IPDSQESDL-GARDIPSWRRICKTLIKNDFWCRSLSFSPNRPQAYARYVKRIQQK 396
Cdd:COG3969  316 TAEHYRNKIAVSLRWWQKRGGPLDeIPDDQDKDIeGTKDIPSWRRICKCILKNDYWCRSLSFGPTKSEIYRRYALREKYK 395


                 ....*..
gi 502612537 397 RHQWEII 403
Cdd:COG3969  396 RILWGIL 402
PAPS_reductase-like_YbdN cd23947
uncharacterized phosphoadenosine phosphosulfate reductase-like proteins, similar to ...
 14-242 2.03e-63

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: 202.24  E-value: 2.03e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612537  14 AYARMNWVFETFPRVCVSFSGGKDSTVLLHIAAEVARRKKRRLFVLFVDWEVQFSHTIQHIESMRQRY-QDVIERFFWVA 92
Cdd:cd23947    1 ALERIRKVFEEFDPVIVSFSGGKDSLVLLHLALEALRRLRKDVYVVFIDTGIEFPETIDFVEKLAETLgLDVEAARPPLF 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612537  93 LplttasgvsqyetEWTCWQPgvtwvrQPPPDAITDPDFFPFYTSGISFEAFVVAFSLWLSGRKSM--ATLVGIRADESL 170
Cdd:cd23947   81 L-------------EWLTSNF------QPQWDPIWDNPPPPRDYRWCCDELKLEPFTKWLKEKKPEgvLLLVGIRADESL 141

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 502612537 171 NRFMAVASQSklrydddKPWTTASQDGFYYTAYPLYDWKVSDIWHFNAQQRLPYNPLYDLMYRAGVPLRQMR 242
Cdd:cd23947  142 NRAKRPRVYR-------KYGWRNSTLPGQIVAYPIKDWSVEDVWLYILRHGLPYNPLYDLGFDRGGCLVCPR 206
DUF3440 pfam11922
Domain of unknown function (DUF3440); This presumed domain is functionally uncharacterized. ...
 235-384 6.94e-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: 127.00  E-value: 6.94e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612537  235 GVPLRQMRICEPFGPEQRKGLWLYHVLEPTTWGRACSRVAGANGGAIYANQSGAFYalnRQIDKPPQHTWKSYVHYLLAS 314
Cdd:pfam11922   1 GVPLEQMRVASPFISAAIESLKLYRVIDPDTWGKMIGRVNGVNFAGIYGGTKAMGW---RSIKLPEGHTWKSYMYFLLST 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612537  315 MPQKTAEHYRNKIAIYLRWYQRHG------------------------------------YPQDIPDSQesdlgARDIPS 358
Cdd:pfam11922  78 LPEETRNNYLKKLSVSIKFWREKGgclseetieelkaagipievggksnyttdkrpvrmeYPDDIDIKE-----FKEIPT 152

                         170       180
                  ....*....|....*....|....*.
gi 502612537  359 WRRICKTLIKNDFWCRSLSFSPNRPQ 384
Cdd:pfam11922 153 YKRMCICILKNDHTCKYMGFGPTKEE 178
CysD COG0175
3'-phosphoadenosine 5'-phosphosulfate sulfotransferase (PAPS reductase)/FAD synthetase or ...
 13-246 5.15e-18

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: 82.59  E-value: 5.15e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612537  13 AAYARMNWVFETFP-RVCVSFSGGKDSTVLLHIAAEVarrkKRRLFVLFVDWEVQFSHTIQHIESMRQRYQ-DVI----E 86
Cdd:COG0175   20 EAIEILREAAAEFGgRVVVSSSGGKDSTVLLHLAAKF----KPPIPVLFLDTGYEFPETYEFRDRLAERLGlDLIvvrpE 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612537  87 RFFWVALpltTASGVSQYET--EWTCwqpgvtWVRQpppdaitdpdffpfytsgisfeafVVAFSLWLSGRKSMATLVGI 164
Cdd:COG0175   96 DAFAEQL---AEFGPPLFYRdpRWCC------KIRK------------------------VEPLKRALAGYDFDAWITGL 142

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612537 165 RADESLNRfmavasqSKLRYdddkpwttASQD--GFYYTAYPLYDWKVSDIWHFNAQQRLPYNPLYDLMYRagvplrqmR 242
Cdd:COG0175  143 RRDESPTR-------AKEPV--------VEWDpvGGLIKVNPLADWTELDVWAYIRREDLPYNPLYDQGYP--------S 199


                 ....*
gi 502612537 243 I-CEP 246
Cdd:COG0175  200 IgCAP 204
PAPS_reduct pfam01507
Phosphoadenosine phosphosulfate reductase family; This domain is found in phosphoadenosine ...
 30-233 4.95e-14

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: 69.63  E-value: 4.95e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612537   30 VSFSGGKDSTVLLHIAAEVarrkKRRLFVLFVDWEVQFSHTIQHIESMRQRYQDVIErffwVALP-LTTASGVSQYETEW 108
Cdd:pfam01507   4 VSFSGGKDSLVLLHLASKA----FPPGPVIFIDTGYEFPETYEFVDELEEKYGLNLK----VYLPeDSFAEGINPEGIPS 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612537  109 TCWQpgvtWVRQPppdaitdpdffpfytsgisfeAFVVAFSLWLSGRKSMATLVGIRADESLNRfmavASQSKLRYDDDK 188
Cdd:pfam01507  76 SLYR----RCCRL---------------------RKVEPLKRALKELGFDAWFTGLRRDESPSR----AKLPIVSIDGDF 126

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 502612537  189 PWTtasqdgfyYTAYPLYDWKVSDIWHFNAQQRLPYNPLYDLMYR 233
Cdd:pfam01507 127 PKV--------IKVFPLLNWTETDVWQYILANNVPYNPLYDQGYR 163
FAD_synthase cd23948
FAD synthase; FAD synthase (FMN:ATP adenylyl transferase (FMNAT); FAD pyrophosphorylase; ...
 21-232 5.23e-11

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: 61.00  E-value: 5.23e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612537  21 VFETFP--RVCVSFSGGKDSTVLLHIAAEVARRKKR----RLFVLFVDWEVQFSHTIQHIESMRQRYqdvierffwvALP 94
Cdd:cd23948   12 ALDKYGpeEIAISFNGGKDCTVLLHLLRAALKRKYPspltPLKALYIKSPDPFPEVEEFVEDTAKRY----------NLD 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612537  95 LTT-----ASGVSQYETEwtcwqpgvtwvrQPPPDAItdpdffpfytsgisfeafvvafslwlsgrksmatLVGIRAD-- 167
Cdd:cd23948   82 LITidgpmKEGLEELLKE------------HPIIKAV----------------------------------FMGTRRTdp 115

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 502612537 168 --ESLNRFmavaSQSklryddDKPWTTasqdgfYYTAYPLYDWKVSDIWHFNAQQRLPYNPLYDLMY 232
Cdd:cd23948  116 hgENLKPF----SPT------DPGWPQ------FMRVNPILDWSYHDVWEFLRTLNLPYCSLYDQGY 166
PAPS_reductase cd23945
Phosphoadenylyl-sulfate reductase (thioredoxin); Phosphoadenosine phosphosulfate (PAPS) ...
 16-233 1.05e-09

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: 57.22  E-value: 1.05e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612537  16 ARMNWVFETF-PRVCVSFSGGKDSTVLLHIAAEVARRKKrrlfVLFVDWEVQFSHTIQHIESMRQRYQDVIERFFwvalP 94
Cdd:cd23945    3 EILLWAAEEFgPKLVFATSFGAEDAVILDLLSKVRPDIP----VVFLDTGYLFPETYDLIDEVEARYGLNIEVYF----P 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612537  95 LTTAsgVSQYETEWTCWqpgvtwvrqpppdaitdpdffPFYTSGISFEAF-----VVAFSLWLSGRKSMATlvGIRADES 169
Cdd:cd23945   75 EGTE--AEEEALEGGLN---------------------EFYLEDEERYDCcrkrkPFPLALALLGVKAWIT--GRRRDQS 129

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 502612537 170 LNRfmavASQSKLRYDDdkpwttasQDGfYYTAYPLYDWKVSDIWHFNAQQRLPYNPLYDLMYR 233
Cdd:cd23945  130 PTR----ANLPIVEVDE--------EGG-LVKINPLADWTWEDVWAYIREHDLPYNPLHDQGYP 180
AANH-like cd01986
adenine nucleotide alpha hydrolase (AANH)-like proteins; This group of adenine nucleotide ...
 28-101 1.95e-08

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: 50.91  E-value: 1.95e-08
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 502612537  28 VCVSFSGGKDSTVLLHIAAEVARrkKRRLFVLFVDWEVQFShtiQHIESMRQRYQDVIERFFWVALPLTTASGV 101
Cdd:cd01986    1 VVVGYSGGKDSSVALHLASRLGR--KAEVAVVHIDHGIGFK---EEAESVASIARRSILKKLAEKGARAIATGV 69
TilS COG0037
tRNA(Ile)-lysidine synthase TilS/MesJ [Translation, ribosomal structure and biogenesis]; tRNA ...
 27-62 2.01e-08

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: 54.45  E-value: 2.01e-08
                         10        20        30
                 ....*....|....*....|....*....|....*.
gi 502612537  27 RVCVSFSGGKDSTVLLHIAAEVARRKKRRLFVLFVD 62
Cdd:COG0037   17 RILVAVSGGKDSLALLHLLAKLRRRLGFELVAVHVD 52
PRK13795 PRK13795
hypothetical protein; Provisional
 28-229 5.11e-08

hypothetical protein; Provisional


Pssm-ID: 237510 [Multi-domain]  Cd Length: 636  Bit Score: 55.00  E-value: 5.11e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612537  28 VCVSFSGGKDSTVLLHIAAEVArrkkRRLFVLFVDWEVQFSHTIQHIESMRQRYQ-DVIE----RFFWVALPLTTASGVs 102
Cdd:PRK13795 246 VSVSFSGGKDSLVVLDLAREAL----KDFKAFFNNTGLEFPETVENVKEVAEEYGiELIEadagDAFWRAVEKFGPPAR- 320

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612537 103 qyETEWTCwqpGVTWVrQPPPDAITdpDFFPfytsgisfeafvvafslwlsgrKSMATLVGIRADESLNRfmavasqSKL 182
Cdd:PRK13795 321 --DYRWCC---KVCKL-GPITRAIK--ENFP----------------------KGCLTFVGQRKYESFSR-------AKS 363

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 502612537 183 RYDDDKPWtTASQDGfyytAYPLYDWKVSDIWHFNAQQRLPYNPLYD 229
Cdd:PRK13795 364 PRVWRNPW-VPNQIG----ASPIQDWTALEVWLYIFWRKLPYNPLYE 405
PRK08557 PRK08557
hypothetical protein; Provisional
 11-229 4.93e-07

hypothetical protein; Provisional


Pssm-ID: 181465 [Multi-domain]  Cd Length: 417  Bit Score: 51.29  E-value: 4.93e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612537  11 FVAAYARMNWVfetfprVCVSFSGGKDSTVLLHIAAEVArrkkRRLFVLFVDWEVQFSHTIQHIESMRQRYQ---DVIE- 86
Cdd:PRK08557 173 YIEKYKNKGYA------INASFSGGKDSSVSTLLAKEVI----PDLEVIFIDTGLEYPETINYVKDFAKKYDlnlDTLDg 242

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612537  87 RFFWVALpltTASGVSQYETEW---TC-WQPGVTWVRQPPPDaitdpdffpfytsgisfeafvvafslwlsgrKSMATLV 162
Cdd:PRK08557 243 DNFWENL---EKEGIPTKDNRWcnsACkLMPLKEYLKKKYGN-------------------------------KKVLTID 288

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612537 163 GIRADESLNRfmavasqSKLRYDddkpwttaSQDGFY---YTAYPLYDWKVSDIWHFNAQQRLPYNPLYD 229
Cdd:PRK08557 289 GSRKYESFTR-------ANLDYE--------RKSGFIdfqTNVFPILDWNSLDIWSYIYLNDILYNPLYD 343
TilS_N cd01992
N-terminal domain of tRNA(Ile)-lysidine synthase and similar proteins; tRNA(Ile)-lysidine ...
 27-62 7.70e-06

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: 46.05  E-value: 7.70e-06
                         10        20        30
                 ....*....|....*....|....*....|....*.
gi 502612537  27 RVCVSFSGGKDSTVLLHIAAEVARRKKRRLFVLFVD 62
Cdd:cd01992    1 KILVAVSGGPDSMALLHLLKELRPKLGLKLVAVHVD 36
PRK13794 PRK13794
hypothetical protein; Provisional
 27-228 1.31e-05

hypothetical protein; Provisional


Pssm-ID: 237509 [Multi-domain]  Cd Length: 479  Bit Score: 46.97  E-value: 1.31e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612537  27 RVCVSFSGGKDSTVLLHIAAEVARRKkrrLFVLFVDWEVQFSHTIQHIESMRQRYQDVIERF----FWVALpltTASGVS 102
Cdd:PRK13794 249 PVTVAYSGGKDSLATLLLALKALGIN---FPVLFNDTGLEFPETLENVEDVEKHYGLEIIRTkseeFWEKL---EEYGPP 322

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612537 103 QYETEWTCWQPGVTWVRQpppdAITDpdffpfytsgiSFEAFVVAFslwlsgrksmatlVGIRADESLNRfmavaSQSKL 182
Cdd:PRK13794 323 ARDNRWCSEVCKLEPLGK----LIDE-----------KYEGECLSF-------------VGQRKYESFNR-----SKKPR 369

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 502612537 183 RYdddKPWTTASQdgfyYTAYPLYDWKVSDIWHFNAQQRLPYNPLY 228
Cdd:PRK13794 370 IW---RNPYIKKQ----ILAAPILHWTAMHVWIYLFREKAPYNKLY 408
lysidine_TilS_N TIGR02432
tRNA(Ile)-lysidine synthetase, N-terminal domain; The only examples in which the wobble ...
 27-62 4.38e-05

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: 43.77  E-value: 4.38e-05
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 502612537   27 RVCVSFSGGKDSTVLLHIAAEVARRKKRRLFVLFVD 62
Cdd:TIGR02432   1 RILVAVSGGVDSMALLHLLLKLQPKIKIKLIAAHVD 36
CTU1-like cd01713
cytoplasmic tRNA 2-thiolation protein 1 and similar proteins; This subfamily includes human ...
 27-62 8.97e-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: 43.35  E-value: 8.97e-05
                         10        20        30
                 ....*....|....*....|....*....|....*...
gi 502612537  27 RVCVSFSGGKDSTVLLHIAAEVARRKKR--RLFVLFVD 62
Cdd:cd01713   20 RVAVGLSGGKDSTVLLYVLKELNKRHDYgvELIAVTID 57
COG1606 COG1606
ATP-utilizing enzyme, PP-loop superfamily [General function prediction only];
22-48 1.69e-04

ATP-utilizing enzyme, PP-loop superfamily [General function prediction only];


Pssm-ID: 441214 [Multi-domain]  Cd Length: 265  Bit Score: 42.79  E-value: 1.69e-04
                         10        20
                 ....*....|....*....|....*..
gi 502612537  22 FETFPRVCVSFSGGKDSTVLLHIAAEV 48
Cdd:COG1606   12 LKELGSVLVAFSGGVDSTLLAKVAHDV 38
ATP_bind_3 pfam01171
PP-loop family; This family of proteins belongs to the PP-loop superfamily.
 30-62 2.74e-03

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


Pssm-ID: 426097 [Multi-domain]  Cd Length: 178  Bit Score: 38.38  E-value: 2.74e-03
                          10        20        30
                  ....*....|....*....|....*....|...
gi 502612537   30 VSFSGGKDSTVLLHIAAEVARRKKRRLFVLFVD 62
Cdd:pfam01171   1 VAVSGGPDSMALLYLLAKLKIKLGIELTAAHVN 33
Asn_synthase_B_C cd01991
C-terminal domain of asparagine synthase B; The C-terminal domain of asparagine synthase (or ...
 26-57 5.02e-03

C-terminal domain of asparagine synthase B; The C-terminal domain of asparagine synthase (or synthetase) B is always associated with an N-terminal amidotransferase domain. Family members that contain this domain catalyze the conversion of aspartate to asparagine. Asparagine synthase B catalyzes the synthesis of asparagine from aspartate, Mg(2+)ATP, and glutamine. The three-dimensional architecture of the N-terminal domain of asparagine synthetase B is similar to that observed for glutamine phosphoribosylpyrophosphate amidotransferase while the molecular motif of the C-domain is reminiscent to that observed for GMP synthetase.


Pssm-ID: 467495 [Multi-domain]  Cd Length: 224  Bit Score: 38.02  E-value: 5.02e-03
                         10        20        30
                 ....*....|....*....|....*....|..
gi 502612537  26 PRVCVSFSGGKDSTVLLHIAAEVARRKKRRLF 57
Cdd:cd01991    3 VPVGVLLSGGLDSSLIAALAARLLPETPIDLF 34
PRK05253 PRK05253
sulfate adenylyltransferase subunit CysD;
21-45 6.25e-03

sulfate adenylyltransferase subunit CysD;


Pssm-ID: 235375  Cd Length: 301  Bit Score: 38.19  E-value: 6.25e-03
                         10        20
                 ....*....|....*....|....*
gi 502612537  21 VFETFPRVCVSFSGGKDSTVLLHIA 45
Cdd:PRK05253  23 VAAEFENPVMLYSIGKDSSVMLHLA 47
TtcA-like cd24138
tRNA-cytidine(32) 2-sulfurtransferase and similar proteins; tRNA-cytidine(32) ...
 27-69 8.80e-03

tRNA-cytidine(32) 2-sulfurtransferase and similar proteins; tRNA-cytidine(32) 2-sulfurtransferase, also called two-thiocytidine biosynthesis protein A or tRNA 2-thiocytidine biosynthesis protein TtcA, catalyzes the ATP-dependent 2-thiolation of cytidine in position 32 of tRNA, to form 2-thiocytidine (s(2)C32). TtcA belongs to the adenine nucleotide alpha hydrolase superfamily (AANH) that includes N-type ATP PPases and ATP sulfurylases. It forms an alpha/beta/alpha fold which binds to the adenosine group. This domain has a strongly conserved motif SGGKD at the N-terminus.


Pssm-ID: 467514 [Multi-domain]  Cd Length: 187  Bit Score: 37.25  E-value: 8.80e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 502612537  27 RVCVSFSGGKDSTVLLHIAAEVARRKKrrlfvlfVDWEVQFSH 69
Cdd:cd24138   10 RILVGLSGGKDSLTLLHLLEELKRRAP-------IKFELVAVT 45
 
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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