NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1377038052|ref|NP_001349304|]
View 

FAD synthase [Mus musculus]

Protein Classification

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
FAD_synthase cd23948
FAD synthase; FAD synthase (FMN:ATP adenylyl transferase (FMNAT); FAD pyrophosphorylase; ...
 284-462 9.51e-109

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: 320.24  E-value: 9.51e-109
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1377038052 284 KVAGALQTIETALAQYHLSQLCVGFNGGKDCTALLHLFHAAVQRKFPDVPKPLQILYIRSISPFPELEQFLQDTIKRYNL 363
Cdd:cd23948     1 KVKSALEVIEEALDKYGPEEIAISFNGGKDCTVLLHLLRAALKRKYPSPLTPLKALYIKSPDPFPEVEEFVEDTAKRYNL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1377038052 364 QVLEAEGNMKQALGELQEKHPQLEAVLMGTRRTDPYSCSLSHFSPTDPGWPSFMRINPLLDWTYRNIWEFLRQLFVPYCI 443
Cdd:cd23948    81 DLITIDGPMKEGLEELLKEHPIIKAVFMGTRRTDPHGENLKPFSPTDPGWPQFMRVNPILDWSYHDVWEFLRTLNLPYCS 160

                         170
                  ....*....|....*....
gi 1377038052 444 LYDRGYTSLGSRENTTQNP 462
Cdd:cd23948   161 LYDQGYTSLGSVDNTLPNP 179
cinA cd00885
Competence-damaged protein. CinA is the first gene in the competence- inducible (cin) operon ...
 17-171 5.81e-55

Competence-damaged protein. CinA is the first gene in the competence- inducible (cin) operon and is thought to be specifically required at some stage in the process of transformation. This domain is closely related to a domain, found in a variety of proteins involved in biosynthesis of molybdopterin cofactor, where the domain is presumed to bind molybdopterin.


:

Pssm-ID: 238450 [Multi-domain]  Cd Length: 170  Bit Score: 181.53  E-value: 5.81e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1377038052  17 TAGIIIVGDEILKGHTQDTNTYFLCRTLRSLGVQVCRVSVVPDEVATIASEVNSFSRRFTHVLTAGGIGPTHDDVTFEAV 96
Cdd:cd00885     1 TAEIIAIGDELLSGQIVDTNAAFLAKELAELGIEVYRVTVVGDDEDRIAEALRRASERADLVITTGGLGPTHDDLTREAV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1377038052  97 AQAFGEELKPHPELQAAIKTLGGEGW-------EKLSMVPSSARL---HYGTdprtghpfrFPLVSVR----NVYLFPGI 162
Cdd:cd00885    81 AKAFGRPLVLDEEALERIEARFARRGremteanLKQAMLPEGATLlpnPVGT---------APGFSVEhngkNVFLLPGV 151


                  ....*....
gi 1377038052 163 PELLRRVLE 171
Cdd:cd00885   152 PSEMKPMLE 160
 
Name Accession Description Interval E-value
FAD_synthase cd23948
FAD synthase; FAD synthase (FMN:ATP adenylyl transferase (FMNAT); FAD pyrophosphorylase; ...
 284-462 9.51e-109

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: 320.24  E-value: 9.51e-109
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1377038052 284 KVAGALQTIETALAQYHLSQLCVGFNGGKDCTALLHLFHAAVQRKFPDVPKPLQILYIRSISPFPELEQFLQDTIKRYNL 363
Cdd:cd23948     1 KVKSALEVIEEALDKYGPEEIAISFNGGKDCTVLLHLLRAALKRKYPSPLTPLKALYIKSPDPFPEVEEFVEDTAKRYNL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1377038052 364 QVLEAEGNMKQALGELQEKHPQLEAVLMGTRRTDPYSCSLSHFSPTDPGWPSFMRINPLLDWTYRNIWEFLRQLFVPYCI 443
Cdd:cd23948    81 DLITIDGPMKEGLEELLKEHPIIKAVFMGTRRTDPHGENLKPFSPTDPGWPQFMRVNPILDWSYHDVWEFLRTLNLPYCS 160

                         170
                  ....*....|....*....
gi 1377038052 444 LYDRGYTSLGSRENTTQNP 462
Cdd:cd23948   161 LYDQGYTSLGSVDNTLPNP 179
cinA cd00885
Competence-damaged protein. CinA is the first gene in the competence- inducible (cin) operon ...
 17-171 5.81e-55

Competence-damaged protein. CinA is the first gene in the competence- inducible (cin) operon and is thought to be specifically required at some stage in the process of transformation. This domain is closely related to a domain, found in a variety of proteins involved in biosynthesis of molybdopterin cofactor, where the domain is presumed to bind molybdopterin.


Pssm-ID: 238450 [Multi-domain]  Cd Length: 170  Bit Score: 181.53  E-value: 5.81e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1377038052  17 TAGIIIVGDEILKGHTQDTNTYFLCRTLRSLGVQVCRVSVVPDEVATIASEVNSFSRRFTHVLTAGGIGPTHDDVTFEAV 96
Cdd:cd00885     1 TAEIIAIGDELLSGQIVDTNAAFLAKELAELGIEVYRVTVVGDDEDRIAEALRRASERADLVITTGGLGPTHDDLTREAV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1377038052  97 AQAFGEELKPHPELQAAIKTLGGEGW-------EKLSMVPSSARL---HYGTdprtghpfrFPLVSVR----NVYLFPGI 162
Cdd:cd00885    81 AKAFGRPLVLDEEALERIEARFARRGremteanLKQAMLPEGATLlpnPVGT---------APGFSVEhngkNVFLLPGV 151


                  ....*....
gi 1377038052 163 PELLRRVLE 171
Cdd:cd00885   152 PSEMKPMLE 160
CinA COG1058
ADP-ribose pyrophosphatase domain of DNA damage- and competence-inducible protein CinA ...
 17-253 6.86e-53

ADP-ribose pyrophosphatase domain of DNA damage- and competence-inducible protein CinA [Replication, recombination and repair];


Pssm-ID: 440678  Cd Length: 249  Bit Score: 178.77  E-value: 6.86e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1377038052  17 TAGIIIVGDEILKGHTQDTNTYFLCRTLRSLGVQVCRVSVVPDEVATIASEVNSFSRRFTHVLTAGGIGPTHDDVTFEAV 96
Cdd:COG1058     1 KAEIITIGDELLSGRIVDTNAAWLARELAELGIDVYRITTVGDDPERIVEALREALARADLVITTGGLGPTPDDLTREAV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1377038052  97 AQAFGEELKPHPELQAAIKTLGGEGWEKLS-------MVPSSARL---HYGTDPrtGhpFRFPLVSVRnVYLFPGIPELL 166
Cdd:COG1058    81 AEALGVPLVLDPEALALIEERFAKRGREMTennlkqaLLPEGAELlpnPVGTAP--G--FSIENNGKV-VIFLPGVPSEM 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1377038052 167 RRVLEG-----LKGLFQNTAVqfHLKELYVA-ASEGSIAPILSEAQAHFgRRLSLGSYPdwSSNYFQVKLILDSEEKEPL 240
Cdd:COG1058   156 KPMFEEevlprLKKLFSGEPI--VSRTLRTFgIGESDLAELLEDLEARF-PNVTIGSYP--SDGEVRLRLTARGTDEEEA 230

                         250
                  ....*....|...
gi 1377038052 241 EECLAYLTARLPQ 253
Cdd:COG1058   231 EAALEALEEELRE 243
MoCF_biosynth pfam00994
Probable molybdopterin binding domain; This domain is found a variety of proteins involved in ...
 19-110 7.80e-28

Probable molybdopterin binding domain; This domain is found a variety of proteins involved in biosynthesis of molybdopterin cofactor. The domain is presumed to bind molybdopterin. The structure of this domain is known, and it forms an alpha/beta structure. In the known structure of Gephyrin this domain mediates trimerization.


Pssm-ID: 425979 [Multi-domain]  Cd Length: 143  Bit Score: 108.10  E-value: 7.80e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1377038052  19 GIIIVGDEILKGHTQDTNTYFLCRTLRSLGVQVCRVSVVPDEVATIASEVNSFSRRFTHVLTAGGIGPTHDDVTFEAVAQ 98
Cdd:pfam00994   1 AIITTGDELLPGQIRDTNGPLLAALLREAGAEVIRYGIVPDDPEAIKEALRAAAEEADVVITTGGTGPGPDDVTPEALAE 80

                          90
                  ....*....|..
gi 1377038052  99 AFGEELKPHPEL 110
Cdd:pfam00994  81 LGGRELPGFEEL 92
PAPS_reduct pfam01507
Phosphoadenosine phosphosulfate reductase family; This domain is found in phosphoadenosine ...
 303-458 1.54e-27

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: 108.15  E-value: 1.54e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1377038052 303 QLCVGFNGGKDCTALLHLfhaaVQRKFPDVPkplqILYIRSISPFPELEQFLQDTIKRY--NLQVLEAEGN--------- 371
Cdd:pfam01507   1 ELVVSFSGGKDSLVLLHL----ASKAFPPGP----VIFIDTGYEFPETYEFVDELEEKYglNLKVYLPEDSfaeginpeg 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1377038052 372 -----------------MKQALGELQEKhpqleAVLMGTRRTDPYSCSLSHFSPTDPGWPSFMRINPLLDWTYRNIWEFL 434
Cdd:pfam01507  73 ipsslyrrccrlrkvepLKRALKELGFD-----AWFTGLRRDESPSRAKLPIVSIDGDFPKVIKVFPLLNWTETDVWQYI 147

                         170       180
                  ....*....|....*....|....
gi 1377038052 435 RQLFVPYCILYDRGYTSLGSRENT 458
Cdd:pfam01507 148 LANNVPYNPLYDQGYRSIGCYPCT 171
PRK01215 PRK01215
nicotinamide mononucleotide deamidase-related protein;
17-205 4.05e-24

nicotinamide mononucleotide deamidase-related protein;


Pssm-ID: 179250 [Multi-domain]  Cd Length: 264  Bit Score: 101.24  E-value: 4.05e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1377038052  17 TAGIIIVGDEILKGHTQDTNTYFLCRTLRSLGVQVCRVSVVPDEVATIASEVNSFSRRFTHVLTAGGIGPTHDDVTFEAV 96
Cdd:PRK01215    5 FAWIITIGNELLIGRTVNTNASWIARRLTYLGYTVRRITVVMDDIEEIVSAFREAIDRADVVVSTGGLGPTYDDKTNEGF 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1377038052  97 AQAFGEELKPHPELQAAIK----TLG---GEGWEKLSMVPSSARlhygtdprtghPFRFP-------LVSVRN--VYLFP 160
Cdd:PRK01215   85 AKALGVELELNEDALRMILekyeKRGiplTPERKKMAMMPPGAV-----------PLENPvgtapgiLIEHGGkdIVALP 153

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1377038052 161 GIPELLRRVLEG-LKGLFQNTA-VQFHLKELYVA-ASEGSIAPILSEA 205
Cdd:PRK01215  154 GVPREMEAIFENfVEPLLKNRPpLKYYEDSILVEgVMESDLAPYVKEL 201
MoCF_biosynth smart00852
Probable molybdopterin binding domain; This domain is found a variety of proteins involved in ...
 19-104 6.94e-24

Probable molybdopterin binding domain; This domain is found a variety of proteins involved in biosynthesis of molybdopterin cofactor. The domain is presumed to bind molybdopterin. The structure of this domain is known, and it forms an alpha/beta structure. In the known structure of Gephyrin this domain mediates trimerisation.


Pssm-ID: 214856 [Multi-domain]  Cd Length: 138  Bit Score: 96.89  E-value: 6.94e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1377038052   19 GIIIVGDEILKGHTQ-DTNTYFLCRTLRSLGVQVCRVSVV--PDEVATIASEVNSFSRRFTHVLTAGGIGPTHDDVTFEA 95
Cdd:smart00852   1 AIISTGDELLSGGQIrDSNGPMLAALLRELGIEVVRVVVVggPDDPEAIREALREALAEADVVITTGGTGPGPDDLTPEA 80


                   ....*....
gi 1377038052   96 VAQAFGEEL 104
Cdd:smart00852  81 LAELGGREL 89
molyb_syn TIGR00177
molybdenum cofactor synthesis domain; The Drosophila protein cinnamon, the Arabidopsis protein ...
 16-104 3.62e-16

molybdenum cofactor synthesis domain; The Drosophila protein cinnamon, the Arabidopsis protein cnx1, and rat protein gephyrin each have one domain like MoeA and one like MoaB and Mog. These domains are, however, distantly related to each other, as captured by this model. Gephyrin is unusual in that it seems to be a tubulin-binding neuroprotein involved in the clustering of both blycine receptors and GABA receptors, rather than a protein of molybdenum cofactor biosynthesis.


Pssm-ID: 272944 [Multi-domain]  Cd Length: 148  Bit Score: 75.43  E-value: 3.62e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1377038052  16 VTAGIIIVGDEILKGHTQ-------DTNTYFLCRTLRSLGVQVCRVSVVPDEVATIASEVNSFSRRFTHVLTAGGIGPTH 88
Cdd:TIGR00177   1 PRVAVISVGDELVEGGQPlepgqiyDSNGPLLAALLQEAGFNVVRLGIVPDDPEEIREILRKAVDEADVVLTTGGTGVGP 80

                          90
                  ....*....|....*.
gi 1377038052  89 DDVTFEAVAQAFGEEL 104
Cdd:TIGR00177  81 RDVTPEALEELGEKEI 96
CysD COG0175
3'-phosphoadenosine 5'-phosphosulfate sulfotransferase (PAPS reductase)/FAD synthetase or ...
 286-453 1.28e-14

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: 73.34  E-value: 1.28e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1377038052 286 AGALQTIETALAQYHlSQLCVGFNGGKDCTALLHLFhaavqRKF-PDVPkplqILYI---RSispFPELEQFLQDTIKRY 361
Cdd:COG0175    19 AEAIEILREAAAEFG-GRVVVSSSGGKDSTVLLHLA-----AKFkPPIP----VLFLdtgYE---FPETYEFRDRLAERL 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1377038052 362 NLQV-------------------LEAEGN-----------MKQALGELQEkhpqlEAVLMGTRRTDpyscslshfSPT-- 409
Cdd:COG0175    86 GLDLivvrpedafaeqlaefgppLFYRDPrwcckirkvepLKRALAGYDF-----DAWITGLRRDE---------SPTra 151

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1377038052 410 -------DPGwPSFMRINPLLDWTYRNIWEFLRQLFVPYCILYDRGYTSLG 453
Cdd:COG0175   152 kepvvewDPV-GGLIKVNPLADWTELDVWAYIRREDLPYNPLYDQGYPSIG 201
PAPS_reductase TIGR02057
phosphoadenosine phosphosulfate reductase, thioredoxin dependent; Requiring thioredoxin as an ...
 285-459 6.58e-08

phosphoadenosine phosphosulfate reductase, thioredoxin dependent; Requiring thioredoxin as an electron donor, phosphoadenosine phosphosulfate reductase catalyzes the reduction of 3'-phosphoadenylylsulfate (PAPS) to sulfite and phospho-adenosine-phosphate (PAP). Found in enterobacteria, cyanobacteria, and yeast, PAPS reductase is related to a group of plant (TIGR00424) and bacterial (TIGR02055) enzymes preferring 5'-adenylylsulfate (APS) over PAPS as a substrate for reduction to sulfite. [Central intermediary metabolism, Sulfur metabolism]


Pssm-ID: 131112  Cd Length: 226  Bit Score: 53.30  E-value: 6.58e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1377038052 285 VAGALQTIETALAQyhlsqlCVGFngGKDCTALLHLFHAAVQrkfPDVPkplqILYIRSISPFPELEQFLQDTIKRYNL- 363
Cdd:TIGR02057  17 IAWSIVTFPHGLVQ------TSAF--GIQALVTLHLLSSISE---PMIP----VIFIDTLYHFPQTLTLKDELTKKYYQt 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1377038052 364 ------QVLEAEGNMKQALGELQE--------------------KHPQLEAVLMGTRRTDpySCSLSHFSPTD-PGWPSF 416
Cdd:TIGR02057  82 lnlykyDGCESEADFEAKYGKLLWqkdiekydyiakvepmqralKELNASAWFTGRRRDQ--GSARANLPVIEiDEQNGI 159

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1377038052 417 MRINPLLDWTYRNIWEFLRQLFVPYCILYDRGYTSLGSRENTT 459
Cdd:TIGR02057 160 LKVNPLIDWTFEQVYQYLDAHNVPYNPLLDQGYRSIGDYHSTR 202
PRK02090 PRK02090
phosphoadenylyl-sulfate reductase;
417-453 4.05e-07

phosphoadenylyl-sulfate reductase;


Pssm-ID: 234997  Cd Length: 241  Bit Score: 50.99  E-value: 4.05e-07
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 1377038052 417 MRINPLLDWTYRNIWEFLRQLFVPYCILYDRGYTSLG 453
Cdd:PRK02090  170 FKINPLADWTNEDVWAYLKEHDLPYHPLVDQGYPSIG 206
 
Name Accession Description Interval E-value
FAD_synthase cd23948
FAD synthase; FAD synthase (FMN:ATP adenylyl transferase (FMNAT); FAD pyrophosphorylase; ...
 284-462 9.51e-109

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: 320.24  E-value: 9.51e-109
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1377038052 284 KVAGALQTIETALAQYHLSQLCVGFNGGKDCTALLHLFHAAVQRKFPDVPKPLQILYIRSISPFPELEQFLQDTIKRYNL 363
Cdd:cd23948     1 KVKSALEVIEEALDKYGPEEIAISFNGGKDCTVLLHLLRAALKRKYPSPLTPLKALYIKSPDPFPEVEEFVEDTAKRYNL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1377038052 364 QVLEAEGNMKQALGELQEKHPQLEAVLMGTRRTDPYSCSLSHFSPTDPGWPSFMRINPLLDWTYRNIWEFLRQLFVPYCI 443
Cdd:cd23948    81 DLITIDGPMKEGLEELLKEHPIIKAVFMGTRRTDPHGENLKPFSPTDPGWPQFMRVNPILDWSYHDVWEFLRTLNLPYCS 160

                         170
                  ....*....|....*....
gi 1377038052 444 LYDRGYTSLGSRENTTQNP 462
Cdd:cd23948   161 LYDQGYTSLGSVDNTLPNP 179
cinA cd00885
Competence-damaged protein. CinA is the first gene in the competence- inducible (cin) operon ...
 17-171 5.81e-55

Competence-damaged protein. CinA is the first gene in the competence- inducible (cin) operon and is thought to be specifically required at some stage in the process of transformation. This domain is closely related to a domain, found in a variety of proteins involved in biosynthesis of molybdopterin cofactor, where the domain is presumed to bind molybdopterin.


Pssm-ID: 238450 [Multi-domain]  Cd Length: 170  Bit Score: 181.53  E-value: 5.81e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1377038052  17 TAGIIIVGDEILKGHTQDTNTYFLCRTLRSLGVQVCRVSVVPDEVATIASEVNSFSRRFTHVLTAGGIGPTHDDVTFEAV 96
Cdd:cd00885     1 TAEIIAIGDELLSGQIVDTNAAFLAKELAELGIEVYRVTVVGDDEDRIAEALRRASERADLVITTGGLGPTHDDLTREAV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1377038052  97 AQAFGEELKPHPELQAAIKTLGGEGW-------EKLSMVPSSARL---HYGTdprtghpfrFPLVSVR----NVYLFPGI 162
Cdd:cd00885    81 AKAFGRPLVLDEEALERIEARFARRGremteanLKQAMLPEGATLlpnPVGT---------APGFSVEhngkNVFLLPGV 151


                  ....*....
gi 1377038052 163 PELLRRVLE 171
Cdd:cd00885   152 PSEMKPMLE 160
CinA COG1058
ADP-ribose pyrophosphatase domain of DNA damage- and competence-inducible protein CinA ...
 17-253 6.86e-53

ADP-ribose pyrophosphatase domain of DNA damage- and competence-inducible protein CinA [Replication, recombination and repair];


Pssm-ID: 440678  Cd Length: 249  Bit Score: 178.77  E-value: 6.86e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1377038052  17 TAGIIIVGDEILKGHTQDTNTYFLCRTLRSLGVQVCRVSVVPDEVATIASEVNSFSRRFTHVLTAGGIGPTHDDVTFEAV 96
Cdd:COG1058     1 KAEIITIGDELLSGRIVDTNAAWLARELAELGIDVYRITTVGDDPERIVEALREALARADLVITTGGLGPTPDDLTREAV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1377038052  97 AQAFGEELKPHPELQAAIKTLGGEGWEKLS-------MVPSSARL---HYGTDPrtGhpFRFPLVSVRnVYLFPGIPELL 166
Cdd:COG1058    81 AEALGVPLVLDPEALALIEERFAKRGREMTennlkqaLLPEGAELlpnPVGTAP--G--FSIENNGKV-VIFLPGVPSEM 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1377038052 167 RRVLEG-----LKGLFQNTAVqfHLKELYVA-ASEGSIAPILSEAQAHFgRRLSLGSYPdwSSNYFQVKLILDSEEKEPL 240
Cdd:COG1058   156 KPMFEEevlprLKKLFSGEPI--VSRTLRTFgIGESDLAELLEDLEARF-PNVTIGSYP--SDGEVRLRLTARGTDEEEA 230

                         250
                  ....*....|...
gi 1377038052 241 EECLAYLTARLPQ 253
Cdd:COG1058   231 EAALEALEEELRE 243
MoCF_biosynth pfam00994
Probable molybdopterin binding domain; This domain is found a variety of proteins involved in ...
 19-110 7.80e-28

Probable molybdopterin binding domain; This domain is found a variety of proteins involved in biosynthesis of molybdopterin cofactor. The domain is presumed to bind molybdopterin. The structure of this domain is known, and it forms an alpha/beta structure. In the known structure of Gephyrin this domain mediates trimerization.


Pssm-ID: 425979 [Multi-domain]  Cd Length: 143  Bit Score: 108.10  E-value: 7.80e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1377038052  19 GIIIVGDEILKGHTQDTNTYFLCRTLRSLGVQVCRVSVVPDEVATIASEVNSFSRRFTHVLTAGGIGPTHDDVTFEAVAQ 98
Cdd:pfam00994   1 AIITTGDELLPGQIRDTNGPLLAALLREAGAEVIRYGIVPDDPEAIKEALRAAAEEADVVITTGGTGPGPDDVTPEALAE 80

                          90
                  ....*....|..
gi 1377038052  99 AFGEELKPHPEL 110
Cdd:pfam00994  81 LGGRELPGFEEL 92
PAPS_reduct pfam01507
Phosphoadenosine phosphosulfate reductase family; This domain is found in phosphoadenosine ...
 303-458 1.54e-27

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: 108.15  E-value: 1.54e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1377038052 303 QLCVGFNGGKDCTALLHLfhaaVQRKFPDVPkplqILYIRSISPFPELEQFLQDTIKRY--NLQVLEAEGN--------- 371
Cdd:pfam01507   1 ELVVSFSGGKDSLVLLHL----ASKAFPPGP----VIFIDTGYEFPETYEFVDELEEKYglNLKVYLPEDSfaeginpeg 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1377038052 372 -----------------MKQALGELQEKhpqleAVLMGTRRTDPYSCSLSHFSPTDPGWPSFMRINPLLDWTYRNIWEFL 434
Cdd:pfam01507  73 ipsslyrrccrlrkvepLKRALKELGFD-----AWFTGLRRDESPSRAKLPIVSIDGDFPKVIKVFPLLNWTETDVWQYI 147

                         170       180
                  ....*....|....*....|....
gi 1377038052 435 RQLFVPYCILYDRGYTSLGSRENT 458
Cdd:pfam01507 148 LANNVPYNPLYDQGYRSIGCYPCT 171
PRK01215 PRK01215
nicotinamide mononucleotide deamidase-related protein;
17-205 4.05e-24

nicotinamide mononucleotide deamidase-related protein;


Pssm-ID: 179250 [Multi-domain]  Cd Length: 264  Bit Score: 101.24  E-value: 4.05e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1377038052  17 TAGIIIVGDEILKGHTQDTNTYFLCRTLRSLGVQVCRVSVVPDEVATIASEVNSFSRRFTHVLTAGGIGPTHDDVTFEAV 96
Cdd:PRK01215    5 FAWIITIGNELLIGRTVNTNASWIARRLTYLGYTVRRITVVMDDIEEIVSAFREAIDRADVVVSTGGLGPTYDDKTNEGF 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1377038052  97 AQAFGEELKPHPELQAAIK----TLG---GEGWEKLSMVPSSARlhygtdprtghPFRFP-------LVSVRN--VYLFP 160
Cdd:PRK01215   85 AKALGVELELNEDALRMILekyeKRGiplTPERKKMAMMPPGAV-----------PLENPvgtapgiLIEHGGkdIVALP 153

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1377038052 161 GIPELLRRVLEG-LKGLFQNTA-VQFHLKELYVA-ASEGSIAPILSEA 205
Cdd:PRK01215  154 GVPREMEAIFENfVEPLLKNRPpLKYYEDSILVEgVMESDLAPYVKEL 201
MoCF_biosynth smart00852
Probable molybdopterin binding domain; This domain is found a variety of proteins involved in ...
 19-104 6.94e-24

Probable molybdopterin binding domain; This domain is found a variety of proteins involved in biosynthesis of molybdopterin cofactor. The domain is presumed to bind molybdopterin. The structure of this domain is known, and it forms an alpha/beta structure. In the known structure of Gephyrin this domain mediates trimerisation.


Pssm-ID: 214856 [Multi-domain]  Cd Length: 138  Bit Score: 96.89  E-value: 6.94e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1377038052   19 GIIIVGDEILKGHTQ-DTNTYFLCRTLRSLGVQVCRVSVV--PDEVATIASEVNSFSRRFTHVLTAGGIGPTHDDVTFEA 95
Cdd:smart00852   1 AIISTGDELLSGGQIrDSNGPMLAALLRELGIEVVRVVVVggPDDPEAIREALREALAEADVVITTGGTGPGPDDLTPEA 80


                   ....*....
gi 1377038052   96 VAQAFGEEL 104
Cdd:smart00852  81 LAELGGREL 89
PRK03670 PRK03670
competence damage-inducible protein A; Provisional
 18-250 1.41e-23

competence damage-inducible protein A; Provisional


Pssm-ID: 167581  Cd Length: 252  Bit Score: 99.49  E-value: 1.41e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1377038052  18 AGIIIVGDEILKGHTQDTNTYFLCRTLRSLGVQVCRVSVVPDEVATIASEVNSFSRRFTHVLT-AGGIGPTHDDVTFEAV 96
Cdd:PRK03670    3 AEIITVGDELLTGNTVDSNSAFIAQKLTEKGYWVRRITTVGDDVEEIKSVVLEILSRKPEVLViSGGLGPTHDDVTMLAV 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1377038052  97 AQAFGEELKPHPELQAAIKTLGGEGWEK-LSMVPS--SARLHYGTDPRTGHPFRF-------PLVSVRNVYLF--PGIPE 164
Cdd:PRK03670   83 AEALGRELVLCEDCLERIKEFYEELYKKgLIDDPTlnEARKKMAYLPEGAEPLENtegaapgAYIEHKGTKIFvlPGMPR 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1377038052 165 LLRRVLEG--LKGLFQNTAVQfhLKELYVAASEGSIAPILSEAQAHFGRRLSlgSYPDWSSNYfqVKLILDSEEKEPLEE 242
Cdd:PRK03670  163 EMKAMLEKevLPRLGERKFVQ--KKFLAEITDESKLAPILEEALERFNVKIH--SSPKGFGKY--IGIIIFAEDEEEIEK 236


                  ....*...
gi 1377038052 243 CLAYLTAR 250
Cdd:PRK03670  237 AVEFMEER 244
PRK00549 PRK00549
competence damage-inducible protein A; Provisional
 18-184 6.30e-17

competence damage-inducible protein A; Provisional


Pssm-ID: 234789 [Multi-domain]  Cd Length: 414  Bit Score: 82.53  E-value: 6.30e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1377038052  18 AGIIIVGDEILKGHTQDTNTYFLCRTLRSLGVQVCRVSVVPDEVATIASEVNSFSRRFTHVLTAGGIGPTHDDVTFEAVA 97
Cdd:PRK00549    3 AEIIAVGTELLLGQIVNTNAQFLSEKLAELGIDVYHQTVVGDNPERLLSALEIAEERSDLIITTGGLGPTKDDLTKETVA 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1377038052  98 QAFGEELKPHPELQAAI----KTLG---GEGWEKLSMVPSSARL---HYGTDPrtGHpfrfpLVSVRN--VYLFPGIP-E 164
Cdd:PRK00549   83 KFLGRELVLDEEALAKIedyfAKRGremTENNRKQALIPEGATVlpnPVGTAP--GM-----IIEVDGktYIVLPGPPsE 155

                         170       180
                  ....*....|....*....|
gi 1377038052 165 llrrvlegLKGLFQNTAVQF 184
Cdd:PRK00549  156 --------LKPMFEEYVVPY 167
molyb_syn TIGR00177
molybdenum cofactor synthesis domain; The Drosophila protein cinnamon, the Arabidopsis protein ...
 16-104 3.62e-16

molybdenum cofactor synthesis domain; The Drosophila protein cinnamon, the Arabidopsis protein cnx1, and rat protein gephyrin each have one domain like MoeA and one like MoaB and Mog. These domains are, however, distantly related to each other, as captured by this model. Gephyrin is unusual in that it seems to be a tubulin-binding neuroprotein involved in the clustering of both blycine receptors and GABA receptors, rather than a protein of molybdenum cofactor biosynthesis.


Pssm-ID: 272944 [Multi-domain]  Cd Length: 148  Bit Score: 75.43  E-value: 3.62e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1377038052  16 VTAGIIIVGDEILKGHTQ-------DTNTYFLCRTLRSLGVQVCRVSVVPDEVATIASEVNSFSRRFTHVLTAGGIGPTH 88
Cdd:TIGR00177   1 PRVAVISVGDELVEGGQPlepgqiyDSNGPLLAALLQEAGFNVVRLGIVPDDPEEIREILRKAVDEADVVLTTGGTGVGP 80

                          90
                  ....*....|....*.
gi 1377038052  89 DDVTFEAVAQAFGEEL 104
Cdd:TIGR00177  81 RDVTPEALEELGEKEI 96
CysD COG0175
3'-phosphoadenosine 5'-phosphosulfate sulfotransferase (PAPS reductase)/FAD synthetase or ...
 286-453 1.28e-14

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: 73.34  E-value: 1.28e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1377038052 286 AGALQTIETALAQYHlSQLCVGFNGGKDCTALLHLFhaavqRKF-PDVPkplqILYI---RSispFPELEQFLQDTIKRY 361
Cdd:COG0175    19 AEAIEILREAAAEFG-GRVVVSSSGGKDSTVLLHLA-----AKFkPPIP----VLFLdtgYE---FPETYEFRDRLAERL 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1377038052 362 NLQV-------------------LEAEGN-----------MKQALGELQEkhpqlEAVLMGTRRTDpyscslshfSPT-- 409
Cdd:COG0175    86 GLDLivvrpedafaeqlaefgppLFYRDPrwcckirkvepLKRALAGYDF-----DAWITGLRRDE---------SPTra 151

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1377038052 410 -------DPGwPSFMRINPLLDWTYRNIWEFLRQLFVPYCILYDRGYTSLG 453
Cdd:COG0175   152 kepvvewDPV-GGLIKVNPLADWTELDVWAYIRREDLPYNPLYDQGYPSIG 201
MoCF_BD cd00758
MoCF_BD: molybdenum cofactor (MoCF) binding domain (BD). This domain is found a variety of ...
 18-104 4.65e-14

MoCF_BD: molybdenum cofactor (MoCF) binding domain (BD). This domain is found a variety of proteins involved in biosynthesis of molybdopterin cofactor, like MoaB, MogA, and MoeA. The domain is presumed to bind molybdopterin.


Pssm-ID: 238387 [Multi-domain]  Cd Length: 133  Bit Score: 68.91  E-value: 4.65e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1377038052  18 AGIIIVGDEILKGHTQDTNTYFLCRTLRSLGVQVCRVSVVPDEVATIASEVNSFSRRFTHVLTAGGIGPTHDDVTFEAVA 97
Cdd:cd00758     2 VAIVTVSDELSQGQIEDTNGPALEALLEDLGCEVIYAGVVPDDADSIRAALIEASREADLVLTTGGTGVGRRDVTPEALA 81


                  ....*..
gi 1377038052  98 QAFGEEL 104
Cdd:cd00758    82 ELGEREA 88
cinA_nterm TIGR00200
competence/damage-inducible protein CinA N-terminal domain; cinA is a DNA damage- or ...
 18-307 1.41e-13

competence/damage-inducible protein CinA N-terminal domain; cinA is a DNA damage- or competence-inducible protein that is polycistronic with recA in a number of species [DNA metabolism, DNA replication, recombination, and repair]


Pssm-ID: 161761 [Multi-domain]  Cd Length: 413  Bit Score: 72.25  E-value: 1.41e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1377038052  18 AGIIIVGDEILKGHTQDTNTYFLCRTLRSLGVQVCRVSVVPDEVATIASEVNSFSRRFTHVLTAGGIGPTHDDVTFEAVA 97
Cdd:TIGR00200   3 AEIISVGDELLLGQIVNTNAQWLADFLAHQGLPLSRRTTVGDNPERLKTIIRIASERADVLIFNGGLGPTSDDLTAETIA 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1377038052  98 QAFGEELKPHPELQAAIKTLGGE-------GWEKLSMVPSSARL---HYGTDP-RTGHPFRFPLvsvrnVYLFPGIPELL 166
Cdd:TIGR00200  83 TAKGEPLVLNEAWLKEIERYFHEtgrvmapNNRKQALLPAGAEFlanPVGTAPgMFAVQLNRCL-----MLFTPGVPSEF 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1377038052 167 RRvleglkgLFQNTAVQFHLKELyvaaseGSIAPILSEAQAHFGRRLS-----LGSYPDWSSNYFQVKLILDSEekEPLE 241
Cdd:TIGR00200 158 RV-------MVEHEALPRLRERF------SLPQPIVSLVLRFFGIGESqleadLADSLDTLTNPTGAPMAYRGE--VPLR 222

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1377038052 242 ECLAYLTARLPQGSLVPYQPDAVEKAGEAVYKLAESGscLGKKVAGALQTIETALAqyhLSQLCVG 307
Cdd:TIGR00200 223 ELKLTGPESEQQRAMEKLWLDIKRVAGQSVIGEDTEG--LPAQISRELQERGFTLT---LAESFTG 283
PAPS_reductase-like_YbdN cd23947
uncharacterized phosphoadenosine phosphosulfate reductase-like proteins, similar to ...
 305-454 1.20e-11

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: 63.95  E-value: 1.20e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1377038052 305 CVGFNGGKDCTALLHLfhaaVQRKFPDVPKPLQILYIRSISPFPELEQFLQDTIKRYNLQVLEAEG------NMKQALGE 378
Cdd:cd23947    16 IVSFSGGKDSLVLLHL----ALEALRRLRKDVYVVFIDTGIEFPETIDFVEKLAETLGLDVEAARPplflewLTSNFQPQ 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1377038052 379 -----------------------------LQEKHPQLEAVLMGTRRTDPYSCSLSHFSPTDPGWPS-----FMRINPLLD 424
Cdd:cd23947    92 wdpiwdnpppprdyrwccdelklepftkwLKEKKPEGVLLLVGIRADESLNRAKRPRVYRKYGWRNstlpgQIVAYPIKD 171

                         170       180       190
                  ....*....|....*....|....*....|
gi 1377038052 425 WTYRNIWEFLRQLFVPYCILYDRGYTSLGS 454
Cdd:cd23947   172 WSVEDVWLYILRHGLPYNPLYDLGFDRGGC 201
PAPS_reductase cd23945
Phosphoadenylyl-sulfate reductase (thioredoxin); Phosphoadenosine phosphosulfate (PAPS) ...
 288-453 3.13e-11

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: 62.23  E-value: 3.13e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1377038052 288 ALQTIETALAQYHlSQLCVGFNGGKDCTALLHLFHaavqRKFPDVPkplqILYIRSISPFPELEQFLQDTIKRYNLQVLE 367
Cdd:cd23945     1 PLEILLWAAEEFG-PKLVFATSFGAEDAVILDLLS----KVRPDIP----VVFLDTGYLFPETYDLIDEVEARYGLNIEV 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1377038052 368 AEGNMKQALGELQEKHPQLEavlmGTRRTDPYSC-----------SLSHF-----------SPT---------DPGWPSF 416
Cdd:cd23945    72 YFPEGTEAEEEALEGGLNEF----YLEDEERYDCcrkrkpfplalALLGVkawitgrrrdqSPTranlpivevDEEGGLV 147

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1377038052 417 mRINPLLDWTYRNIWEFLRQLFVPYCILYDRGYTSLG 453
Cdd:cd23945   148 -KINPLADWTWEDVWAYIREHDLPYNPLHDQGYPSIG 183
MogA_MoaB cd00886
MogA_MoaB family. Members of this family are involved in biosynthesis of the molybdenum ...
 16-97 8.40e-11

MogA_MoaB family. Members of this family are involved in biosynthesis of the molybdenum cofactor (MoCF) an essential cofactor of a diverse group of redox enzymes. MoCF biosynthesis is an evolutionarily conserved pathway present in eubacteria, archaea, and eukaryotes. MoCF contains a tricyclic pyranopterin, termed molybdopterin (MPT). MogA, together with MoeA, is responsible for the metal incorporation into MPT, the third step in MoCF biosynthesis. The plant homolog Cnx1 is a MoeA-MogA fusion protein. The mammalian homolog gephyrin is a MogA-MoeA fusion protein, that plays a critical role in postsynaptic anchoring of inhibitory glycine receptors and major GABAa receptor subtypes. In contrast, MoaB shows high similarity to MogA, but little is known about its physiological role. All well studied members of this family form highly stable trimers.


Pssm-ID: 238451 [Multi-domain]  Cd Length: 152  Bit Score: 60.18  E-value: 8.40e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1377038052  16 VTAGIIIVGDEILKGHTQDTNTYFLCRTLRSLGVQVCRVSVVPDEVATIASEVNSFSRRFTH--VLTAGGIGPTHDDVTF 93
Cdd:cd00886     1 LRAAVLTVSDTRSAGEAEDRSGPALVELLEEAGHEVVAYEIVPDDKDEIREALIEWADEDGVdlILTTGGTGLAPRDVTP 80


                  ....
gi 1377038052  94 EAVA 97
Cdd:cd00886    81 EATR 84
MoaB COG0521
Molybdopterin biosynthesis enzyme MoaB/MogA [Coenzyme transport and metabolism]; Molybdopterin ...
 12-102 8.52e-10

Molybdopterin biosynthesis enzyme MoaB/MogA [Coenzyme transport and metabolism]; Molybdopterin biosynthesis enzyme MoaB/MogA is part of the Pathway/BioSystem: Molybdopterin biosynthesis


Pssm-ID: 440287 [Multi-domain]  Cd Length: 169  Bit Score: 57.82  E-value: 8.52e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1377038052  12 SGRSVTAGIIIVGDEILKGHTQDTNTYFLCRTLRSLGVQVCRVSVVPDEVATIASEVNSFSRRFTH--VLTAGGIGPTHD 89
Cdd:COG0521     6 AFVPLRIAVLTVSDRRSRGEREDTSGPALVELLEEAGHEVVARRIVPDDKDAIRAALRELIDDEGVdlVLTTGGTGLSPR 85

                          90       100
                  ....*....|....*....|
gi 1377038052  90 DVTFEAVAQ-------AFGE 102
Cdd:COG0521    86 DVTPEATRPlldkelpGFGE 105
PAPS_reductase TIGR02057
phosphoadenosine phosphosulfate reductase, thioredoxin dependent; Requiring thioredoxin as an ...
 285-459 6.58e-08

phosphoadenosine phosphosulfate reductase, thioredoxin dependent; Requiring thioredoxin as an electron donor, phosphoadenosine phosphosulfate reductase catalyzes the reduction of 3'-phosphoadenylylsulfate (PAPS) to sulfite and phospho-adenosine-phosphate (PAP). Found in enterobacteria, cyanobacteria, and yeast, PAPS reductase is related to a group of plant (TIGR00424) and bacterial (TIGR02055) enzymes preferring 5'-adenylylsulfate (APS) over PAPS as a substrate for reduction to sulfite. [Central intermediary metabolism, Sulfur metabolism]


Pssm-ID: 131112  Cd Length: 226  Bit Score: 53.30  E-value: 6.58e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1377038052 285 VAGALQTIETALAQyhlsqlCVGFngGKDCTALLHLFHAAVQrkfPDVPkplqILYIRSISPFPELEQFLQDTIKRYNL- 363
Cdd:TIGR02057  17 IAWSIVTFPHGLVQ------TSAF--GIQALVTLHLLSSISE---PMIP----VIFIDTLYHFPQTLTLKDELTKKYYQt 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1377038052 364 ------QVLEAEGNMKQALGELQE--------------------KHPQLEAVLMGTRRTDpySCSLSHFSPTD-PGWPSF 416
Cdd:TIGR02057  82 lnlykyDGCESEADFEAKYGKLLWqkdiekydyiakvepmqralKELNASAWFTGRRRDQ--GSARANLPVIEiDEQNGI 159

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1377038052 417 MRINPLLDWTYRNIWEFLRQLFVPYCILYDRGYTSLGSRENTT 459
Cdd:TIGR02057 160 LKVNPLIDWTFEQVYQYLDAHNVPYNPLLDQGYRSIGDYHSTR 202
PRK03673 PRK03673
nicotinamide mononucleotide deamidase-related protein YfaY;
24-109 1.59e-07

nicotinamide mononucleotide deamidase-related protein YfaY;


Pssm-ID: 179629 [Multi-domain]  Cd Length: 396  Bit Score: 53.55  E-value: 1.59e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1377038052  24 GDEILKGHTQDTNTYFLCRTLRSLGVQVCRVSVVPDEVATIASEVNSFSRRFTHVLTAGGIGPTHDDVTFEAVAQAFGEE 103
Cdd:PRK03673   10 GDEVLHGQIVDTNAAWLADFFFHQGLPLSRRNTVGDNLDALVAILRERSQHADVLIVNGGLGPTSDDLSALAAATAAGEG 89


                  ....*.
gi 1377038052 104 LKPHPE 109
Cdd:PRK03673   90 LVLHEE 95
PRK02090 PRK02090
phosphoadenylyl-sulfate reductase;
417-453 4.05e-07

phosphoadenylyl-sulfate reductase;


Pssm-ID: 234997  Cd Length: 241  Bit Score: 50.99  E-value: 4.05e-07
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 1377038052 417 MRINPLLDWTYRNIWEFLRQLFVPYCILYDRGYTSLG 453
Cdd:PRK02090  170 FKINPLADWTNEDVWAYLKEHDLPYHPLVDQGYPSIG 206
Sulfate_adenylyltransferase_2 cd23946
Sulfate adenylyltransferase subunit 2; Sulfate adenylyltransferase subunits 1 and 2 form ATP ...
 300-445 4.52e-07

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: 50.57  E-value: 4.52e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1377038052 300 HLSQLCVGFNGGKDCTALLHLFHAAVqrkFPDVPkPLQILYIRSISPFPELEQFLQDTIKRYNLQ--------------- 364
Cdd:cd23946    19 EFSNPVMLYSIGKDSSVMLHLARKAF---YPGKP-PFPLLHVDTTWKFREMIEFRDRVAKEYGLDlivhvnpdgveagin 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1377038052 365 -----------VLEAEGnMKQALgelqEKHpQLEAVLMGTRRTDPYSCS-------LSHFSPTDPG------WPSF---- 416
Cdd:cd23946    95 pfthgsakhtdIMKTEG-LKQAL----DKY-GFDAAFGGARRDEEKSRAkervysfRDSNHRWDPKnqrpelWNQYngrv 168

                         170       180       190
                  ....*....|....*....|....*....|....
gi 1377038052 417 -----MRINPLLDWTYRNIWEFLRQLFVPYCILY 445
Cdd:cd23946   169 kkgesIRVFPLSNWTELDIWQYIYLENIPIVPLY 202
MoeA cd00887
MoeA family. Members of this family are involved in biosynthesis of the molybdenum cofactor ...
 14-104 6.90e-06

MoeA family. Members of this family are involved in biosynthesis of the molybdenum cofactor (MoCF), an essential cofactor of a diverse group of redox enzymes. MoCF biosynthesis is an evolutionarily conserved pathway present in eubacteria, archaea and eukaryotes. MoCF contains a tricyclic pyranopterin, termed molybdopterin (MPT). MoeA, together with MoaB, is responsible for the metal incorporation into MPT, the third step in MoCF biosynthesis. The plant homolog Cnx1 is a MoeA-MogA fusion protein. The mammalian homolog gephyrin is a MogA-MoeA fusion protein, that plays a critical role in postsynaptic anchoring of inhibitory glycine receptors and major GABAa receptor subtypes.


Pssm-ID: 238452 [Multi-domain]  Cd Length: 394  Bit Score: 48.26  E-value: 6.90e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1377038052  14 RSVTAGIIIVGDEIL-------KGHTQDTNTYFLCRTLRSLGVQVCRVSVVPDEVATIASEVNSFSRRFTHVLTAGGIGP 86
Cdd:cd00887   167 RRPRVAIISTGDELVepgeplaPGQIYDSNSYMLAALLRELGAEVVDLGIVPDDPEALREALEEALEEADVVITSGGVSV 246

                          90
                  ....*....|....*...
gi 1377038052  87 THDDVTFEAVAQAFGEEL 104
Cdd:cd00887   247 GDYDFVKEVLEELGGEVL 264
MoeA COG0303
Molybdopterin Mo-transferase (molybdopterin biosynthesis) [Coenzyme transport and metabolism]; ...
 14-104 1.58e-05

Molybdopterin Mo-transferase (molybdopterin biosynthesis) [Coenzyme transport and metabolism]; Molybdopterin Mo-transferase (molybdopterin biosynthesis) is part of the Pathway/BioSystem: Molybdopterin biosynthesis


Pssm-ID: 440072 [Multi-domain]  Cd Length: 401  Bit Score: 47.01  E-value: 1.58e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1377038052  14 RSVTAGIIIVGDEIL-------KGHTQDTNTYFLCRTLRSLGVQVCRVSVVPDEVATIASEVNSFSRRFTHVLTAGGIGP 86
Cdd:COG0303   171 RRPRVAILSTGDELVepgeplgPGQIYDSNSYMLAALLREAGAEVVDLGIVPDDPEALRAALREALAEADLVITSGGVSV 250

                          90
                  ....*....|....*...
gi 1377038052  87 THDDVTFEAVAqAFGEEL 104
Cdd:COG0303   251 GDYDLVKEALE-ELGAEV 267
APS_reduc TIGR00424
5'-adenylylsulfate reductase, thioredoxin-independent; This enzyme, involved in the ...
 255-472 1.62e-05

5'-adenylylsulfate reductase, thioredoxin-independent; This enzyme, involved in the assimilation of inorganic sulfate, is closely related to the thioredoxin-dependent PAPS reductase of Bacteria (CysH) and Saccharomyces cerevisiae. However, it has its own C-terminal thioredoxin-like domain and is not thioredoxin-dependent. Also, it has a substrate preference for 5'-adenylylsulfate (APS) over 3'-phosphoadenylylsulfate (PAPS) so the pathway does not require an APS kinase (CysC) to convert APS to PAPS. Arabidopsis thaliana appears to have three isozymes, all able to complement E. coli CysH mutants (even in backgrounds lacking thioredoxin or APS kinase) but likely localized to different compartments in Arabidopsis. [Central intermediary metabolism, Sulfur metabolism]


Pssm-ID: 273072 [Multi-domain]  Cd Length: 463  Bit Score: 47.32  E-value: 1.62e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1377038052 255 SLVPYQPDAVEKAGEAVYKLAESGSCLGKKV--AGALQTIETALAQYHlSQLCVGFNGGKDcTALLHLFHAAvqrkfpdv 332
Cdd:TIGR00424  68 SIVPSAATTVAPEVEEKVVEVEDFEKLAKKLenASPLEIMDKALEKFG-NDIAIAFSGAED-VALIEYAHLT-------- 137

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1377038052 333 PKPLQILYIRSISPFPELEQFLQDTIKRYNLQV-------LEAEG-------------------------NMKQAL---- 376
Cdd:TIGR00424 138 GRPFRVFSLDTGRLNPETYRFFDAVEKQYGIRIeymfpdaVEVQAlvrskglfsfyedghqeccrvrkvrPLRRALkglk 217

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1377038052 377 ----GELQEKHPqleavlmGTRRTDPYSCSLSHFSPTDPGWPSFMRINPLLDWTYRNIWEFLRQLFVPYCILYDRGYTSL 452
Cdd:TIGR00424 218 awitGQRKDQSP-------GTRSEIPVVQVDPVFEGLDGGVGSLVKWNPVANVEGKDVWNFLRTMDVPVNTLHAQGYVSI 290

                         250       260
                  ....*....|....*....|
gi 1377038052 453 GSRenttqnPALKCLSPGGH 472
Cdd:TIGR00424 291 GCE------PCTRPVLPGQH 304
AANH-like cd01986
adenine nucleotide alpha hydrolase (AANH)-like proteins; This group of adenine nucleotide ...
 305-395 5.34e-04

adenine nucleotide alpha hydrolase (AANH)-like proteins; This group of adenine nucleotide alpha hydrolase (AANH)-like proteins includes N-type ATP PPases and ATP sulfurylases. The domain forms an alpha/beta/alpha fold which binds to adenosine nucleotide.


Pssm-ID: 467490 [Multi-domain]  Cd Length: 74  Bit Score: 38.59  E-value: 5.34e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1377038052 305 CVGFNGGKDCTALLHLFHaavqRKFPDvpKPLQILYIRSISPFPELEQFLQDTIKRynlqvleaegnmkQALGELQEKhp 384
Cdd:cd01986     2 VVGYSGGKDSSVALHLAS----RLGRK--AEVAVVHIDHGIGFKEEAESVASIARR-------------SILKKLAEK-- 60

                          90
                  ....*....|.
gi 1377038052 385 QLEAVLMGTRR 395
Cdd:cd01986    61 GARAIATGVLR 71
PLN02309 PLN02309
5'-adenylylsulfate reductase
 406-472 3.40e-03

5'-adenylylsulfate reductase


Pssm-ID: 215175 [Multi-domain]  Cd Length: 457  Bit Score: 39.77  E-value: 3.40e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1377038052 406 FSPTDPGWPSFMRINPLLDWTYRNIWEFLRQLFVPYCILYDRGYTSLGSRENTtqNPALkclsPGGH 472
Cdd:PLN02309  239 FEGLDGGPGSLVKWNPLANVTGNEVWNFLRTMDVPVNSLHAQGYVSIGCEPCT--RPVL----PGQH 299
MoeA_like cd03522
MoeA_like. This domain is similar to a domain found in a variety of proteins involved in ...
 14-102 4.46e-03

MoeA_like. This domain is similar to a domain found in a variety of proteins involved in biosynthesis of molybdopterin cofactor, like MoaB, MogA, and MoeA. There this domain is presumed to bind molybdopterin. The exact function of this subgroup is unknown.


Pssm-ID: 239599  Cd Length: 312  Bit Score: 39.07  E-value: 4.46e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1377038052  14 RSVTAGIIIVGDEILKGHTQDTNTYFLCRTLRSLGVQVCRVSVVPDEVATIASEVNSFSRRF--THVLTAGGI-GPthDD 90
Cdd:cd03522   158 RPLRVGLIVTGSEVYGGRIEDKFGPVLRARLAALGVELVEQVIVPHDEAAIAAAIAEALEAGaeLLILTGGASvDP--DD 235

                          90
                  ....*....|..
gi 1377038052  91 VTFEAVAQAFGE 102
Cdd:cd03522   236 VTPAAIRAAGGE 247
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH