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Conserved domains on  [gi|41872389|ref|NP_079483|]
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FAD synthase isoform 1 [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
FAD_synthase cd23948
FAD synthase; FAD synthase (FMN:ATP adenylyl transferase (FMNAT); FAD pyrophosphorylase; ...
 379-557 2.19e-106

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: 317.54  E-value: 2.19e-106
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41872389 379 KVAGALQTIETSLAQYSLTQLCVGFNGGKDCTALLHLFHAAVQRKLPDVPNPLQILYIRSISPFPELEQFLQDTIKRYNL 458
Cdd:cd23948   1 KVKSALEVIEEALDKYGPEEIAISFNGGKDCTVLLHLLRAALKRKYPSPLTPLKALYIKSPDPFPEVEEFVEDTAKRYNL 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41872389 459 QMLEAEGSMKQALGELQARHPQLEAVLMGTRRTDPYSCSLCPFSPTDPGWPAFMRINPLLDWTYRDIWDFLRQLFVPYCI 538
Cdd:cd23948  81 DLITIDGPMKEGLEELLKEHPIIKAVFMGTRRTDPHGENLKPFSPTDPGWPQFMRVNPILDWSYHDVWEFLRTLNLPYCS 160

                       170
                ....*....|....*....
gi 41872389 539 LYDRGYTSLGSRENTVRNP 557
Cdd:cd23948 161 LYDQGYTSLGSVDNTLPNP 179
cinA cd00885
Competence-damaged protein. CinA is the first gene in the competence- inducible (cin) operon ...
 112-266 2.44e-53

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: 179.22  E-value: 2.44e-53
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41872389 112 TAGIIIVGDEILKGHTQDTNTFFLCRTLRSLGVQVCRVSVVPDEVATIAAEVTSFSNRFTHVLTAGGIGPTHDDVTFEAV 191
Cdd:cd00885   1 TAEIIAIGDELLSGQIVDTNAAFLAKELAELGIEVYRVTVVGDDEDRIAEALRRASERADLVITTGGLGPTHDDLTREAV 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41872389 192 AQAFGDELKPHPKLEAATKALGGEGW-------EKLSLVPSSARL---HYGTdpctgqpfrFPLVSVR----NVYLFPGI 257
Cdd:cd00885  81 AKAFGRPLVLDEEALERIEARFARRGremteanLKQAMLPEGATLlpnPVGT---------APGFSVEhngkNVFLLPGV 151


                ....*....
gi 41872389 258 PELLRRVLE 266
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; ...
 379-557 2.19e-106

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: 317.54  E-value: 2.19e-106
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41872389 379 KVAGALQTIETSLAQYSLTQLCVGFNGGKDCTALLHLFHAAVQRKLPDVPNPLQILYIRSISPFPELEQFLQDTIKRYNL 458
Cdd:cd23948   1 KVKSALEVIEEALDKYGPEEIAISFNGGKDCTVLLHLLRAALKRKYPSPLTPLKALYIKSPDPFPEVEEFVEDTAKRYNL 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41872389 459 QMLEAEGSMKQALGELQARHPQLEAVLMGTRRTDPYSCSLCPFSPTDPGWPAFMRINPLLDWTYRDIWDFLRQLFVPYCI 538
Cdd:cd23948  81 DLITIDGPMKEGLEELLKEHPIIKAVFMGTRRTDPHGENLKPFSPTDPGWPQFMRVNPILDWSYHDVWEFLRTLNLPYCS 160

                       170
                ....*....|....*....
gi 41872389 539 LYDRGYTSLGSRENTVRNP 557
Cdd:cd23948 161 LYDQGYTSLGSVDNTLPNP 179
cinA cd00885
Competence-damaged protein. CinA is the first gene in the competence- inducible (cin) operon ...
 112-266 2.44e-53

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: 179.22  E-value: 2.44e-53
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41872389 112 TAGIIIVGDEILKGHTQDTNTFFLCRTLRSLGVQVCRVSVVPDEVATIAAEVTSFSNRFTHVLTAGGIGPTHDDVTFEAV 191
Cdd:cd00885   1 TAEIIAIGDELLSGQIVDTNAAFLAKELAELGIEVYRVTVVGDDEDRIAEALRRASERADLVITTGGLGPTHDDLTREAV 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41872389 192 AQAFGDELKPHPKLEAATKALGGEGW-------EKLSLVPSSARL---HYGTdpctgqpfrFPLVSVR----NVYLFPGI 257
Cdd:cd00885  81 AKAFGRPLVLDEEALERIEARFARRGremteanLKQAMLPEGATLlpnPVGT---------APGFSVEhngkNVFLLPGV 151


                ....*....
gi 41872389 258 PELLRRVLE 266
Cdd:cd00885 152 PSEMKPMLE 160
CinA COG1058
ADP-ribose pyrophosphatase domain of DNA damage- and competence-inducible protein CinA ...
 112-348 7.60e-50

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


Pssm-ID: 440678  Cd Length: 249  Bit Score: 172.61  E-value: 7.60e-50
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41872389 112 TAGIIIVGDEILKGHTQDTNTFFLCRTLRSLGVQVCRVSVVPDEVATIAAEVTSFSNRFTHVLTAGGIGPTHDDVTFEAV 191
Cdd:COG1058   1 KAEIITIGDELLSGRIVDTNAAWLARELAELGIDVYRITTVGDDPERIVEALREALARADLVITTGGLGPTPDDLTREAV 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41872389 192 AQAFGDELKPHPKLEAATKALGGEGWEKLS-------LVPSSARL---HYGTDPCtgqpFRFPLVSVRnVYLFPGIPELL 261
Cdd:COG1058  81 AEALGVPLVLDPEALALIEERFAKRGREMTennlkqaLLPEGAELlpnPVGTAPG----FSIENNGKV-VIFLPGVPSEM 155

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41872389 262 RRVLEG-----MKGLFQNPAVqfHSKELYVA-ADEASIAPILAEAQAHFgRRLGLGSYPDWGsnYYQVKLTLDSEEEGPL 335
Cdd:COG1058 156 KPMFEEevlprLKKLFSGEPI--VSRTLRTFgIGESDLAELLEDLEARF-PNVTIGSYPSDG--EVRLRLTARGTDEEEA 230

                       250
                ....*....|...
gi 41872389 336 EECLAYLTARLPQ 348
Cdd:COG1058 231 EAALEALEEELRE 243
PAPS_reduct pfam01507
Phosphoadenosine phosphosulfate reductase family; This domain is found in phosphoadenosine ...
 398-554 5.12e-29

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: 113.16  E-value: 5.12e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41872389   398 QLCVGFNGGKDCTALLHLfhaaVQRKLPDVPnplqILYIRSISPFPELEQFLQDTIKRYNL------------QMLEAEG 465
Cdd:pfam01507   1 ELVVSFSGGKDSLVLLHL----ASKAFPPGP----VIFIDTGYEFPETYEFVDELEEKYGLnlkvylpedsfaEGINPEG 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41872389   466 S----------------MKQALGELQARhpqleAVLMGTRRTDPYSCSLCPFSPTDPGWPAFMRINPLLDWTYRDIWDFL 529
Cdd:pfam01507  73 IpsslyrrccrlrkvepLKRALKELGFD-----AWFTGLRRDESPSRAKLPIVSIDGDFPKVIKVFPLLNWTETDVWQYI 147

                         170       180
                  ....*....|....*....|....*
gi 41872389   530 RQLFVPYCILYDRGYTSLGSRENTV 554
Cdd:pfam01507 148 LANNVPYNPLYDQGYRSIGCYPCTG 172
MoCF_biosynth pfam00994
Probable molybdopterin binding domain; This domain is found a variety of proteins involved in ...
 114-205 1.40e-25

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: 102.33  E-value: 1.40e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41872389   114 GIIIVGDEILKGHTQDTNTFFLCRTLRSLGVQVCRVSVVPDEVATIAAEVTSFSNRFTHVLTAGGIGPTHDDVTFEAVAQ 193
Cdd:pfam00994   1 AIITTGDELLPGQIRDTNGPLLAALLREAGAEVIRYGIVPDDPEAIKEALRAAAEEADVVITTGGTGPGPDDVTPEALAE 80

                          90
                  ....*....|..
gi 41872389   194 AFGDELKPHPKL 205
Cdd:pfam00994  81 LGGRELPGFEEL 92
PRK01215 PRK01215
nicotinamide mononucleotide deamidase-related protein;
112-300 4.22e-25

nicotinamide mononucleotide deamidase-related protein;


Pssm-ID: 179250 [Multi-domain]  Cd Length: 264  Bit Score: 104.71  E-value: 4.22e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41872389  112 TAGIIIVGDEILKGHTQDTNTFFLCRTLRSLGVQVCRVSVVPDEVATIAAEVTSFSNRFTHVLTAGGIGPTHDDVTFEAV 191
Cdd:PRK01215   5 FAWIITIGNELLIGRTVNTNASWIARRLTYLGYTVRRITVVMDDIEEIVSAFREAIDRADVVVSTGGLGPTYDDKTNEGF 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41872389  192 AQAFGDELKPHP--------KLEAATKALGGEGwEKLSLVPSSARlhygtdpctgqPFRFP-------LVSVRN--VYLF 254
Cdd:PRK01215  85 AKALGVELELNEdalrmileKYEKRGIPLTPER-KKMAMMPPGAV-----------PLENPvgtapgiLIEHGGkdIVAL 152

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 41872389  255 PGIPELLRRVLEGM--KGLFQNPAVQFHSKELYVA-ADEASIAPILAEA 300
Cdd:PRK01215 153 PGVPREMEAIFENFvePLLKNRPPLKYYEDSILVEgVMESDLAPYVKEL 201
MoCF_biosynth smart00852
Probable molybdopterin binding domain; This domain is found a variety of proteins involved in ...
 114-199 2.87e-23

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: 95.73  E-value: 2.87e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41872389    114 GIIIVGDEILKGHTQ-DTNTFFLCRTLRSLGVQVCRVSVV--PDEVATIAAEVTSFSNRFTHVLTAGGIGPTHDDVTFEA 190
Cdd:smart00852   1 AIISTGDELLSGGQIrDSNGPMLAALLRELGIEVVRVVVVggPDDPEAIREALREALAEADVVITTGGTGPGPDDLTPEA 80


                   ....*....
gi 41872389    191 VAQAFGDEL 199
Cdd:smart00852  81 LAELGGREL 89
CysD COG0175
3'-phosphoadenosine 5'-phosphosulfate sulfotransferase (PAPS reductase)/FAD synthetase or ...
 381-548 1.12e-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: 73.73  E-value: 1.12e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41872389 381 AGALQTIETSLAQYSLTqLCVGFNGGKDCTALLHLfhaaVQRKLPDVPnplqILYI---RSispFPELEQFLQDTIKRYN 457
Cdd:COG0175  19 AEAIEILREAAAEFGGR-VVVSSSGGKDSTVLLHL----AAKFKPPIP----VLFLdtgYE---FPETYEFRDRLAERLG 86

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41872389 458 L------------QMLEAEG------------------SMKQALGELQArhpqlEAVLMGTRRTDpyscslcpfSPT--- 504
Cdd:COG0175  87 LdlivvrpedafaEQLAEFGpplfyrdprwcckirkvePLKRALAGYDF-----DAWITGLRRDE---------SPTrak 152

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|
gi 41872389 505 ------DPGwPAFMRINPLLDWTYRDIWDFLRQLFVPYCILYDRGYTSLG 548
Cdd:COG0175 153 epvvewDPV-GGLIKVNPLADWTELDVWAYIRREDLPYNPLYDQGYPSIG 201
molyb_syn TIGR00177
molybdenum cofactor synthesis domain; The Drosophila protein cinnamon, the Arabidopsis protein ...
 111-199 1.29e-14

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: 71.19  E-value: 1.29e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41872389   111 VTAGIIIVGDEILKGHTQ-------DTNTFFLCRTLRSLGVQVCRVSVVPDEVATIAAEVTSFSNRFTHVLTAGGIGPTH 183
Cdd:TIGR00177   1 PRVAVISVGDELVEGGQPlepgqiyDSNGPLLAALLQEAGFNVVRLGIVPDDPEEIREILRKAVDEADVVLTTGGTGVGP 80

                          90
                  ....*....|....*.
gi 41872389   184 DDVTFEAVAQAFGDEL 199
Cdd:TIGR00177  81 RDVTPEALEELGEKEI 96
PRK02090 PRK02090
phosphoadenylyl-sulfate reductase;
512-548 2.95e-08

phosphoadenylyl-sulfate reductase;


Pssm-ID: 234997  Cd Length: 241  Bit Score: 54.84  E-value: 2.95e-08
                         10        20        30
                 ....*....|....*....|....*....|....*..
gi 41872389  512 MRINPLLDWTYRDIWDFLRQLFVPYCILYDRGYTSLG 548
Cdd:PRK02090 170 FKINPLADWTNEDVWAYLKEHDLPYHPLVDQGYPSIG 206
PAPS_reductase TIGR02057
phosphoadenosine phosphosulfate reductase, thioredoxin dependent; Requiring thioredoxin as an ...
 380-553 4.73e-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: 54.07  E-value: 4.73e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41872389   380 VAGALQTIETSLAQYSltqlcvGFngGKDCTALLHLFHAAVQrklPDVPnplqILYIRSISPFPELEQFLQDTIKRYNLQ 459
Cdd:TIGR02057  17 IAWSIVTFPHGLVQTS------AF--GIQALVTLHLLSSISE---PMIP----VIFIDTLYHFPQTLTLKDELTKKYYQT 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41872389   460 M-------LEAEGSMKQALGEL------------------QARHPQLE--AVLMGTRRTDPYSCSLCPFSPTDpGWPAFM 512
Cdd:TIGR02057  82 LnlykydgCESEADFEAKYGKLlwqkdiekydyiakvepmQRALKELNasAWFTGRRRDQGSARANLPVIEID-EQNGIL 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 41872389   513 RINPLLDWTYRDIWDFLRQLFVPYCILYDRGYTSLGSRENT 553
Cdd:TIGR02057 161 KVNPLIDWTFEQVYQYLDAHNVPYNPLLDQGYRSIGDYHST 201
 
Name Accession Description Interval E-value
FAD_synthase cd23948
FAD synthase; FAD synthase (FMN:ATP adenylyl transferase (FMNAT); FAD pyrophosphorylase; ...
 379-557 2.19e-106

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: 317.54  E-value: 2.19e-106
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41872389 379 KVAGALQTIETSLAQYSLTQLCVGFNGGKDCTALLHLFHAAVQRKLPDVPNPLQILYIRSISPFPELEQFLQDTIKRYNL 458
Cdd:cd23948   1 KVKSALEVIEEALDKYGPEEIAISFNGGKDCTVLLHLLRAALKRKYPSPLTPLKALYIKSPDPFPEVEEFVEDTAKRYNL 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41872389 459 QMLEAEGSMKQALGELQARHPQLEAVLMGTRRTDPYSCSLCPFSPTDPGWPAFMRINPLLDWTYRDIWDFLRQLFVPYCI 538
Cdd:cd23948  81 DLITIDGPMKEGLEELLKEHPIIKAVFMGTRRTDPHGENLKPFSPTDPGWPQFMRVNPILDWSYHDVWEFLRTLNLPYCS 160

                       170
                ....*....|....*....
gi 41872389 539 LYDRGYTSLGSRENTVRNP 557
Cdd:cd23948 161 LYDQGYTSLGSVDNTLPNP 179
cinA cd00885
Competence-damaged protein. CinA is the first gene in the competence- inducible (cin) operon ...
 112-266 2.44e-53

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: 179.22  E-value: 2.44e-53
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41872389 112 TAGIIIVGDEILKGHTQDTNTFFLCRTLRSLGVQVCRVSVVPDEVATIAAEVTSFSNRFTHVLTAGGIGPTHDDVTFEAV 191
Cdd:cd00885   1 TAEIIAIGDELLSGQIVDTNAAFLAKELAELGIEVYRVTVVGDDEDRIAEALRRASERADLVITTGGLGPTHDDLTREAV 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41872389 192 AQAFGDELKPHPKLEAATKALGGEGW-------EKLSLVPSSARL---HYGTdpctgqpfrFPLVSVR----NVYLFPGI 257
Cdd:cd00885  81 AKAFGRPLVLDEEALERIEARFARRGremteanLKQAMLPEGATLlpnPVGT---------APGFSVEhngkNVFLLPGV 151


                ....*....
gi 41872389 258 PELLRRVLE 266
Cdd:cd00885 152 PSEMKPMLE 160
CinA COG1058
ADP-ribose pyrophosphatase domain of DNA damage- and competence-inducible protein CinA ...
 112-348 7.60e-50

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


Pssm-ID: 440678  Cd Length: 249  Bit Score: 172.61  E-value: 7.60e-50
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41872389 112 TAGIIIVGDEILKGHTQDTNTFFLCRTLRSLGVQVCRVSVVPDEVATIAAEVTSFSNRFTHVLTAGGIGPTHDDVTFEAV 191
Cdd:COG1058   1 KAEIITIGDELLSGRIVDTNAAWLARELAELGIDVYRITTVGDDPERIVEALREALARADLVITTGGLGPTPDDLTREAV 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41872389 192 AQAFGDELKPHPKLEAATKALGGEGWEKLS-------LVPSSARL---HYGTDPCtgqpFRFPLVSVRnVYLFPGIPELL 261
Cdd:COG1058  81 AEALGVPLVLDPEALALIEERFAKRGREMTennlkqaLLPEGAELlpnPVGTAPG----FSIENNGKV-VIFLPGVPSEM 155

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41872389 262 RRVLEG-----MKGLFQNPAVqfHSKELYVA-ADEASIAPILAEAQAHFgRRLGLGSYPDWGsnYYQVKLTLDSEEEGPL 335
Cdd:COG1058 156 KPMFEEevlprLKKLFSGEPI--VSRTLRTFgIGESDLAELLEDLEARF-PNVTIGSYPSDG--EVRLRLTARGTDEEEA 230

                       250
                ....*....|...
gi 41872389 336 EECLAYLTARLPQ 348
Cdd:COG1058 231 EAALEALEEELRE 243
PAPS_reduct pfam01507
Phosphoadenosine phosphosulfate reductase family; This domain is found in phosphoadenosine ...
 398-554 5.12e-29

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: 113.16  E-value: 5.12e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41872389   398 QLCVGFNGGKDCTALLHLfhaaVQRKLPDVPnplqILYIRSISPFPELEQFLQDTIKRYNL------------QMLEAEG 465
Cdd:pfam01507   1 ELVVSFSGGKDSLVLLHL----ASKAFPPGP----VIFIDTGYEFPETYEFVDELEEKYGLnlkvylpedsfaEGINPEG 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41872389   466 S----------------MKQALGELQARhpqleAVLMGTRRTDPYSCSLCPFSPTDPGWPAFMRINPLLDWTYRDIWDFL 529
Cdd:pfam01507  73 IpsslyrrccrlrkvepLKRALKELGFD-----AWFTGLRRDESPSRAKLPIVSIDGDFPKVIKVFPLLNWTETDVWQYI 147

                         170       180
                  ....*....|....*....|....*
gi 41872389   530 RQLFVPYCILYDRGYTSLGSRENTV 554
Cdd:pfam01507 148 LANNVPYNPLYDQGYRSIGCYPCTG 172
MoCF_biosynth pfam00994
Probable molybdopterin binding domain; This domain is found a variety of proteins involved in ...
 114-205 1.40e-25

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: 102.33  E-value: 1.40e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41872389   114 GIIIVGDEILKGHTQDTNTFFLCRTLRSLGVQVCRVSVVPDEVATIAAEVTSFSNRFTHVLTAGGIGPTHDDVTFEAVAQ 193
Cdd:pfam00994   1 AIITTGDELLPGQIRDTNGPLLAALLREAGAEVIRYGIVPDDPEAIKEALRAAAEEADVVITTGGTGPGPDDVTPEALAE 80

                          90
                  ....*....|..
gi 41872389   194 AFGDELKPHPKL 205
Cdd:pfam00994  81 LGGRELPGFEEL 92
PRK01215 PRK01215
nicotinamide mononucleotide deamidase-related protein;
112-300 4.22e-25

nicotinamide mononucleotide deamidase-related protein;


Pssm-ID: 179250 [Multi-domain]  Cd Length: 264  Bit Score: 104.71  E-value: 4.22e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41872389  112 TAGIIIVGDEILKGHTQDTNTFFLCRTLRSLGVQVCRVSVVPDEVATIAAEVTSFSNRFTHVLTAGGIGPTHDDVTFEAV 191
Cdd:PRK01215   5 FAWIITIGNELLIGRTVNTNASWIARRLTYLGYTVRRITVVMDDIEEIVSAFREAIDRADVVVSTGGLGPTYDDKTNEGF 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41872389  192 AQAFGDELKPHP--------KLEAATKALGGEGwEKLSLVPSSARlhygtdpctgqPFRFP-------LVSVRN--VYLF 254
Cdd:PRK01215  85 AKALGVELELNEdalrmileKYEKRGIPLTPER-KKMAMMPPGAV-----------PLENPvgtapgiLIEHGGkdIVAL 152

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 41872389  255 PGIPELLRRVLEGM--KGLFQNPAVQFHSKELYVA-ADEASIAPILAEA 300
Cdd:PRK01215 153 PGVPREMEAIFENFvePLLKNRPPLKYYEDSILVEgVMESDLAPYVKEL 201
MoCF_biosynth smart00852
Probable molybdopterin binding domain; This domain is found a variety of proteins involved in ...
 114-199 2.87e-23

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: 95.73  E-value: 2.87e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41872389    114 GIIIVGDEILKGHTQ-DTNTFFLCRTLRSLGVQVCRVSVV--PDEVATIAAEVTSFSNRFTHVLTAGGIGPTHDDVTFEA 190
Cdd:smart00852   1 AIISTGDELLSGGQIrDSNGPMLAALLRELGIEVVRVVVVggPDDPEAIREALREALAEADVVITTGGTGPGPDDLTPEA 80


                   ....*....
gi 41872389    191 VAQAFGDEL 199
Cdd:smart00852  81 LAELGGREL 89
PRK03670 PRK03670
competence damage-inducible protein A; Provisional
 113-345 1.14e-22

competence damage-inducible protein A; Provisional


Pssm-ID: 167581  Cd Length: 252  Bit Score: 97.56  E-value: 1.14e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41872389  113 AGIIIVGDEILKGHTQDTNTFFLCRTLRSLGVQVCRVSVVPDEVATIAAEVTSFSNRFTHVLT-AGGIGPTHDDVTFEAV 191
Cdd:PRK03670   3 AEIITVGDELLTGNTVDSNSAFIAQKLTEKGYWVRRITTVGDDVEEIKSVVLEILSRKPEVLViSGGLGPTHDDVTMLAV 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41872389  192 AQAFGDELKPHPKLEAATKALGGEGWEK-----LSLVPSSARLHY---GTDPCTGQPFRFP--LVSVRNVYLF--PGIPE 259
Cdd:PRK03670  83 AEALGRELVLCEDCLERIKEFYEELYKKgliddPTLNEARKKMAYlpeGAEPLENTEGAAPgaYIEHKGTKIFvlPGMPR 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41872389  260 LLRRVLEG--MKGLFQNPAVQfhSKELYVAADEASIAPILAEAQAHFGRRL-----GLGSYpdwgsnyyqVKLTLDSEEE 332
Cdd:PRK03670 163 EMKAMLEKevLPRLGERKFVQ--KKFLAEITDESKLAPILEEALERFNVKIhsspkGFGKY---------IGIIIFAEDE 231

                        250
                 ....*....|...
gi 41872389  333 GPLEECLAYLTAR 345
Cdd:PRK03670 232 EEIEKAVEFMEER 244
PRK00549 PRK00549
competence damage-inducible protein A; Provisional
 113-207 7.55e-15

competence damage-inducible protein A; Provisional


Pssm-ID: 234789 [Multi-domain]  Cd Length: 414  Bit Score: 76.75  E-value: 7.55e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41872389  113 AGIIIVGDEILKGHTQDTNTFFLCRTLRSLGVQVCRVSVVPDEVATIAAEVTSFSNRFTHVLTAGGIGPTHDDVTFEAVA 192
Cdd:PRK00549   3 AEIIAVGTELLLGQIVNTNAQFLSEKLAELGIDVYHQTVVGDNPERLLSALEIAEERSDLIITTGGLGPTKDDLTKETVA 82

                         90
                 ....*....|....*
gi 41872389  193 QAFGDELKPHPKLEA 207
Cdd:PRK00549  83 KFLGRELVLDEEALA 97
CysD COG0175
3'-phosphoadenosine 5'-phosphosulfate sulfotransferase (PAPS reductase)/FAD synthetase or ...
 381-548 1.12e-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: 73.73  E-value: 1.12e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41872389 381 AGALQTIETSLAQYSLTqLCVGFNGGKDCTALLHLfhaaVQRKLPDVPnplqILYI---RSispFPELEQFLQDTIKRYN 457
Cdd:COG0175  19 AEAIEILREAAAEFGGR-VVVSSSGGKDSTVLLHL----AAKFKPPIP----VLFLdtgYE---FPETYEFRDRLAERLG 86

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41872389 458 L------------QMLEAEG------------------SMKQALGELQArhpqlEAVLMGTRRTDpyscslcpfSPT--- 504
Cdd:COG0175  87 LdlivvrpedafaEQLAEFGpplfyrdprwcckirkvePLKRALAGYDF-----DAWITGLRRDE---------SPTrak 152

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|
gi 41872389 505 ------DPGwPAFMRINPLLDWTYRDIWDFLRQLFVPYCILYDRGYTSLG 548
Cdd:COG0175 153 epvvewDPV-GGLIKVNPLADWTELDVWAYIRREDLPYNPLYDQGYPSIG 201
molyb_syn TIGR00177
molybdenum cofactor synthesis domain; The Drosophila protein cinnamon, the Arabidopsis protein ...
 111-199 1.29e-14

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: 71.19  E-value: 1.29e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41872389   111 VTAGIIIVGDEILKGHTQ-------DTNTFFLCRTLRSLGVQVCRVSVVPDEVATIAAEVTSFSNRFTHVLTAGGIGPTH 183
Cdd:TIGR00177   1 PRVAVISVGDELVEGGQPlepgqiyDSNGPLLAALLQEAGFNVVRLGIVPDDPEEIREILRKAVDEADVVLTTGGTGVGP 80

                          90
                  ....*....|....*.
gi 41872389   184 DDVTFEAVAQAFGDEL 199
Cdd:TIGR00177  81 RDVTPEALEELGEKEI 96
MoCF_BD cd00758
MoCF_BD: molybdenum cofactor (MoCF) binding domain (BD). This domain is found a variety of ...
 113-197 7.29e-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: 68.52  E-value: 7.29e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41872389 113 AGIIIVGDEILKGHTQDTNTFFLCRTLRSLGVQVCRVSVVPDEVATIAAEVTSFSNRFTHVLTAGGIGPTHDDVTFEAVA 192
Cdd:cd00758   2 VAIVTVSDELSQGQIEDTNGPALEALLEDLGCEVIYAGVVPDDADSIRAALIEASREADLVLTTGGTGVGRRDVTPEALA 81


                ....*
gi 41872389 193 qAFGD 197
Cdd:cd00758  82 -ELGE 85
PAPS_reductase-like_YbdN cd23947
uncharacterized phosphoadenosine phosphosulfate reductase-like proteins, similar to ...
 400-549 3.21e-13

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: 68.96  E-value: 3.21e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41872389 400 CVGFNGGKDCTALLHLFHAAVQRKLPDVPnplqILYIRSISPFPELEQFLQDTIKRYNLQMLEAEGSMKQALGELQA--- 476
Cdd:cd23947  16 IVSFSGGKDSLVLLHLALEALRRLRKDVY----VVFIDTGIEFPETIDFVEKLAETLGLDVEAARPPLFLEWLTSNFqpq 91

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41872389 477 ------------------------------RHPQLEAVLM--GTRRTDPYSCSLCPFSPTDPGW-----PAFMRINPLLD 519
Cdd:cd23947  92 wdpiwdnpppprdyrwccdelklepftkwlKEKKPEGVLLlvGIRADESLNRAKRPRVYRKYGWrnstlPGQIVAYPIKD 171

                       170       180       190
                ....*....|....*....|....*....|
gi 41872389 520 WTYRDIWDFLRQLFVPYCILYDRGYTSLGS 549
Cdd:cd23947 172 WSVEDVWLYILRHGLPYNPLYDLGFDRGGC 201
cinA_nterm TIGR00200
competence/damage-inducible protein CinA N-terminal domain; cinA is a DNA damage- or ...
 113-267 1.43e-11

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: 66.47  E-value: 1.43e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41872389   113 AGIIIVGDEILKGHTQDTNTFFLCRTLRSLGVQVCRVSVV---PDEVATIAAEVtsfSNRFTHVLTAGGIGPTHDDVTFE 189
Cdd:TIGR00200   3 AEIISVGDELLLGQIVNTNAQWLADFLAHQGLPLSRRTTVgdnPERLKTIIRIA---SERADVLIFNGGLGPTSDDLTAE 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41872389   190 AVAQAFGDELKPH----PKLEAATKALG---GEGWEKLSLVPSSARL---HYGTDPctgQPFRFPLvSVRNVYLFPGIPE 259
Cdd:TIGR00200  80 TIATAKGEPLVLNeawlKEIERYFHETGrvmAPNNRKQALLPAGAEFlanPVGTAP---GMFAVQL-NRCLMLFTPGVPS 155


                  ....*...
gi 41872389   260 LLRRVLEG 267
Cdd:TIGR00200 156 EFRVMVEH 163
MogA_MoaB cd00886
MogA_MoaB family. Members of this family are involved in biosynthesis of the molybdenum ...
 111-192 3.09e-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: 61.72  E-value: 3.09e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41872389 111 VTAGIIIVGDEILKGHTQDTNTFFLCRTLRSLGVQVCRVSVVPDEVATIAAEVTSFSNRFTH--VLTAGGIGPTHDDVTF 188
Cdd:cd00886   1 LRAAVLTVSDTRSAGEAEDRSGPALVELLEEAGHEVVAYEIVPDDKDEIREALIEWADEDGVdlILTTGGTGLAPRDVTP 80


                ....
gi 41872389 189 EAVA 192
Cdd:cd00886  81 EATR 84
PAPS_reductase cd23945
Phosphoadenylyl-sulfate reductase (thioredoxin); Phosphoadenosine phosphosulfate (PAPS) ...
 513-548 2.35e-10

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: 59.92  E-value: 2.35e-10
                        10        20        30
                ....*....|....*....|....*....|....*.
gi 41872389 513 RINPLLDWTYRDIWDFLRQLFVPYCILYDRGYTSLG 548
Cdd:cd23945 148 KINPLADWTWEDVWAYIREHDLPYNPLHDQGYPSIG 183
MoaB COG0521
Molybdopterin biosynthesis enzyme MoaB/MogA [Coenzyme transport and metabolism]; Molybdopterin ...
 103-192 9.18e-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: 9.18e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41872389 103 SELSPGRSVTAGIIIVGDEILKGHTQDTNTFFLCRTLRSLGVQVCRVSVVPDEVATIAAEVTSFSNRFTH--VLTAGGIG 180
Cdd:COG0521   2 SSARAFVPLRIAVLTVSDRRSRGEREDTSGPALVELLEEAGHEVVARRIVPDDKDAIRAALRELIDDEGVdlVLTTGGTG 81

                        90
                ....*....|..
gi 41872389 181 PTHDDVTFEAVA 192
Cdd:COG0521  82 LSPRDVTPEATR 93
PRK02090 PRK02090
phosphoadenylyl-sulfate reductase;
512-548 2.95e-08

phosphoadenylyl-sulfate reductase;


Pssm-ID: 234997  Cd Length: 241  Bit Score: 54.84  E-value: 2.95e-08
                         10        20        30
                 ....*....|....*....|....*....|....*..
gi 41872389  512 MRINPLLDWTYRDIWDFLRQLFVPYCILYDRGYTSLG 548
Cdd:PRK02090 170 FKINPLADWTNEDVWAYLKEHDLPYHPLVDQGYPSIG 206
PAPS_reductase TIGR02057
phosphoadenosine phosphosulfate reductase, thioredoxin dependent; Requiring thioredoxin as an ...
 380-553 4.73e-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: 54.07  E-value: 4.73e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41872389   380 VAGALQTIETSLAQYSltqlcvGFngGKDCTALLHLFHAAVQrklPDVPnplqILYIRSISPFPELEQFLQDTIKRYNLQ 459
Cdd:TIGR02057  17 IAWSIVTFPHGLVQTS------AF--GIQALVTLHLLSSISE---PMIP----VIFIDTLYHFPQTLTLKDELTKKYYQT 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41872389   460 M-------LEAEGSMKQALGEL------------------QARHPQLE--AVLMGTRRTDPYSCSLCPFSPTDpGWPAFM 512
Cdd:TIGR02057  82 LnlykydgCESEADFEAKYGKLlwqkdiekydyiakvepmQRALKELNasAWFTGRRRDQGSARANLPVIEID-EQNGIL 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 41872389   513 RINPLLDWTYRDIWDFLRQLFVPYCILYDRGYTSLGSRENT 553
Cdd:TIGR02057 161 KVNPLIDWTFEQVYQYLDAHNVPYNPLLDQGYRSIGDYHST 201
PRK03673 PRK03673
nicotinamide mononucleotide deamidase-related protein YfaY;
119-203 7.07e-07

nicotinamide mononucleotide deamidase-related protein YfaY;


Pssm-ID: 179629 [Multi-domain]  Cd Length: 396  Bit Score: 51.62  E-value: 7.07e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41872389  119 GDEILKGHTQDTNTFFLCRTLRSLGVQVCRVSVVPDEVATIAAEVTSFSNRFTHVLTAGGIGPTHDDVTFEAVAQAFGDE 198
Cdd:PRK03673  10 GDEVLHGQIVDTNAAWLADFFFHQGLPLSRRNTVGDNLDALVAILRERSQHADVLIVNGGLGPTSDDLSALAAATAAGEG 89


                 ....*
gi 41872389  199 LKPHP 203
Cdd:PRK03673  90 LVLHE 94
APS_reduc TIGR00424
5'-adenylylsulfate reductase, thioredoxin-independent; This enzyme, involved in the ...
 350-567 7.93e-07

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: 51.94  E-value: 7.93e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41872389   350 SLVPYMPNAVEQASEAVYKLAESGSSLGKKV--AGALQTIETSLAQYSlTQLCVGFNGGKDcTALLHLFHAAVQrklpdv 427
Cdd:TIGR00424  68 SIVPSAATTVAPEVEEKVVEVEDFEKLAKKLenASPLEIMDKALEKFG-NDIAIAFSGAED-VALIEYAHLTGR------ 139

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41872389   428 pnPLQILYIRSISPFPELEQFLQDTIKRYNLQM-------LEAEGSMK------------QALGELQARHP------QLE 482
Cdd:TIGR00424 140 --PFRVFSLDTGRLNPETYRFFDAVEKQYGIRIeymfpdaVEVQALVRskglfsfyedghQECCRVRKVRPlrralkGLK 217

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41872389   483 AVLMGTRR-TDPYSCSLCPFSPTDP-------GWPAFMRINPLLDWTYRDIWDFLRQLFVPYCILYDRGYTSLGSRentv 554
Cdd:TIGR00424 218 AWITGQRKdQSPGTRSEIPVVQVDPvfegldgGVGSLVKWNPVANVEGKDVWNFLRTMDVPVNTLHAQGYVSIGCE---- 293

                         250
                  ....*....|...
gi 41872389   555 rnPALKCLSPGGH 567
Cdd:TIGR00424 294 --PCTRPVLPGQH 304
MoeA cd00887
MoeA family. Members of this family are involved in biosynthesis of the molybdenum cofactor ...
 109-199 5.11e-05

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: 45.95  E-value: 5.11e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41872389 109 RSVTAGIIIVGDEIL-------KGHTQDTNTFFLCRTLRSLGVQVCRVSVVPDEVATIAAEVTSFSNRFTHVLTAGGIGP 181
Cdd:cd00887 167 RRPRVAIISTGDELVepgeplaPGQIYDSNSYMLAALLRELGAEVVDLGIVPDDPEALREALEEALEEADVVITSGGVSV 246

                        90
                ....*....|....*...
gi 41872389 182 THDDVTFEAVAQAFGDEL 199
Cdd:cd00887 247 GDYDFVKEVLEELGGEVL 264
MoeA COG0303
Molybdopterin Mo-transferase (molybdopterin biosynthesis) [Coenzyme transport and metabolism]; ...
 109-199 9.76e-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: 45.08  E-value: 9.76e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41872389 109 RSVTAGIIIVGDEIL-------KGHTQDTNTFFLCRTLRSLGVQVCRVSVVPDEVATIAAEVTSFSNRFTHVLTAGGIGP 181
Cdd:COG0303 171 RRPRVAILSTGDELVepgeplgPGQIYDSNSYMLAALLREAGAEVVDLGIVPDDPEALRAALREALAEADLVITSGGVSV 250

                        90
                ....*....|....*...
gi 41872389 182 THDDVTFEAVAqAFGDEL 199
Cdd:COG0303 251 GDYDLVKEALE-ELGAEV 267
PLN02309 PLN02309
5'-adenylylsulfate reductase
 487-567 6.59e-04

5'-adenylylsulfate reductase


Pssm-ID: 215175 [Multi-domain]  Cd Length: 457  Bit Score: 42.47  E-value: 6.59e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41872389  487 GTRRTDPySCSLCP-FSPTDPGWPAFMRINPLLDWTYRDIWDFLRQLFVPYCILYDRGYTSLGSRENTvrNPALkclsPG 565
Cdd:PLN02309 225 GTRAEVP-VVQVDPvFEGLDGGPGSLVKWNPLANVTGNEVWNFLRTMDVPVNSLHAQGYVSIGCEPCT--RPVL----PG 297


                 ..
gi 41872389  566 GH 567
Cdd:PLN02309 298 QH 299
MoeA_like cd03522
MoeA_like. This domain is similar to a domain found in a variety of proteins involved in ...
 104-197 4.29e-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: 39.45  E-value: 4.29e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41872389 104 ELSPGRSVTAGIIIVGDEILKGHTQDTNTFFLCRTLRSLGVQVCRVSVVPDEVATIAAEVTSF--SNRFTHVLTAGGI-G 180
Cdd:cd03522 153 RVAPFRPLRVGLIVTGSEVYGGRIEDKFGPVLRARLAALGVELVEQVIVPHDEAAIAAAIAEAleAGAELLILTGGASvD 232

                        90
                ....*....|....*..
gi 41872389 181 PthDDVTFEAVAQAFGD 197
Cdd:cd03522 233 P--DDVTPAAIRAAGGE 247
AANH-like cd01986
adenine nucleotide alpha hydrolase (AANH)-like proteins; This group of adenine nucleotide ...
 400-490 4.96e-03

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: 35.89  E-value: 4.96e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41872389 400 CVGFNGGKDCTALLHLFHAAVQRKlpdvpnPLQILYIRSISPFPELEQFLQDTIKRynlqmleaegSMKQALGELQARHp 479
Cdd:cd01986   2 VVGYSGGKDSSVALHLASRLGRKA------EVAVVHIDHGIGFKEEAESVASIARR----------SILKKLAEKGARA- 64

                        90
                ....*....|.
gi 41872389 480 qleaVLMGTRR 490
Cdd:cd01986  65 ----IATGVLR 71
 
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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