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Conserved domains on  [gi|296434309|ref|NP_001171820|]
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FAD synthase isoform 3 [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; ...
 282-446 4.93e-96

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: 286.34  E-value: 4.93e-96
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296434309 282 KVAGALQTIETSLAQYSLTQLCVGFNGGKDCTALLHLFHAAVQRKLPDVPNPLQILYIRSISPFPELEQFLQDTIKRYNL 361
Cdd:cd23948    1 KVKSALEVIEEALDKYGPEEIAISFNGGKDCTVLLHLLRAALKRKYPSPLTPLKALYIKSPDPFPEVEEFVEDTAKRYNL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296434309 362 QMLEAEGSMKQALGELQARHPQLEAVLMGTRRTDPYSCSLCPFSPTDPGWPAFMRINPLLDWTYRDIWDFLRQLFVPYCI 441
Cdd:cd23948   81 DLITIDGPMKEGLEELLKEHPIIKAVFMGTRRTDPHGENLKPFSPTDPGWPQFMRVNPILDWSYHDVWEFLRTLNLPYCS 160


                 ....*
gi 296434309 442 LYDRG 446
Cdd:cd23948  161 LYDQG 165
cinA cd00885
Competence-damaged protein. CinA is the first gene in the competence- inducible (cin) operon ...
 15-169 1.45e-54

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: 1.45e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296434309  15 TAGIIIVGDEILKGHTQDTNTFFLCRTLRSLGVQVCRVSVVPDEVATIAAEVTSFSNRFTHVLTAGGIGPTHDDVTFEAV 94
Cdd:cd00885    1 TAEIIAIGDELLSGQIVDTNAAFLAKELAELGIEVYRVTVVGDDEDRIAEALRRASERADLVITTGGLGPTHDDLTREAV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296434309  95 AQAFGDELKPHPKLEAATKALGGEGW-------EKLSLVPSSARL---HYGTdpctgqpfrFPLVSVR----NVYLFPGI 160
Cdd:cd00885   81 AKAFGRPLVLDEEALERIEARFARRGremteanLKQAMLPEGATLlpnPVGT---------APGFSVEhngkNVFLLPGV 151


                 ....*....
gi 296434309 161 PELLRRVLE 169
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; ...
 282-446 4.93e-96

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: 286.34  E-value: 4.93e-96
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296434309 282 KVAGALQTIETSLAQYSLTQLCVGFNGGKDCTALLHLFHAAVQRKLPDVPNPLQILYIRSISPFPELEQFLQDTIKRYNL 361
Cdd:cd23948    1 KVKSALEVIEEALDKYGPEEIAISFNGGKDCTVLLHLLRAALKRKYPSPLTPLKALYIKSPDPFPEVEEFVEDTAKRYNL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296434309 362 QMLEAEGSMKQALGELQARHPQLEAVLMGTRRTDPYSCSLCPFSPTDPGWPAFMRINPLLDWTYRDIWDFLRQLFVPYCI 441
Cdd:cd23948   81 DLITIDGPMKEGLEELLKEHPIIKAVFMGTRRTDPHGENLKPFSPTDPGWPQFMRVNPILDWSYHDVWEFLRTLNLPYCS 160


                 ....*
gi 296434309 442 LYDRG 446
Cdd:cd23948  161 LYDQG 165
cinA cd00885
Competence-damaged protein. CinA is the first gene in the competence- inducible (cin) operon ...
 15-169 1.45e-54

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: 1.45e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296434309  15 TAGIIIVGDEILKGHTQDTNTFFLCRTLRSLGVQVCRVSVVPDEVATIAAEVTSFSNRFTHVLTAGGIGPTHDDVTFEAV 94
Cdd:cd00885    1 TAEIIAIGDELLSGQIVDTNAAFLAKELAELGIEVYRVTVVGDDEDRIAEALRRASERADLVITTGGLGPTHDDLTREAV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296434309  95 AQAFGDELKPHPKLEAATKALGGEGW-------EKLSLVPSSARL---HYGTdpctgqpfrFPLVSVR----NVYLFPGI 160
Cdd:cd00885   81 AKAFGRPLVLDEEALERIEARFARRGremteanLKQAMLPEGATLlpnPVGT---------APGFSVEhngkNVFLLPGV 151


                 ....*....
gi 296434309 161 PELLRRVLE 169
Cdd:cd00885  152 PSEMKPMLE 160
CinA COG1058
ADP-ribose pyrophosphatase domain of DNA damage- and competence-inducible protein CinA ...
 15-251 1.66e-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: 171.45  E-value: 1.66e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296434309  15 TAGIIIVGDEILKGHTQDTNTFFLCRTLRSLGVQVCRVSVVPDEVATIAAEVTSFSNRFTHVLTAGGIGPTHDDVTFEAV 94
Cdd:COG1058    1 KAEIITIGDELLSGRIVDTNAAWLARELAELGIDVYRITTVGDDPERIVEALREALARADLVITTGGLGPTPDDLTREAV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296434309  95 AQAFGDELKPHPKLEAATKALGGEGWEKLS-------LVPSSARL---HYGTDPCtgqpFRFPLVSVRnVYLFPGIPELL 164
Cdd:COG1058   81 AEALGVPLVLDPEALALIEERFAKRGREMTennlkqaLLPEGAELlpnPVGTAPG----FSIENNGKV-VIFLPGVPSEM 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296434309 165 RRVLEG-----MKGLFQNPAVqfHSKELYVA-ADEASIAPILAEAQAHFgRRLGLGSYPDWGsnYYQVKLTLDSEEEGPL 238
Cdd:COG1058  156 KPMFEEevlprLKKLFSGEPI--VSRTLRTFgIGESDLAELLEDLEARF-PNVTIGSYPSDG--EVRLRLTARGTDEEEA 230

                        250
                 ....*....|...
gi 296434309 239 EECLAYLTARLPQ 251
Cdd:COG1058  231 EAALEALEEELRE 243
PAPS_reduct pfam01507
Phosphoadenosine phosphosulfate reductase family; This domain is found in phosphoadenosine ...
 301-446 4.50e-26

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: 103.92  E-value: 4.50e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296434309  301 QLCVGFNGGKDCTALLHLfhaaVQRKLPDVPnplqILYIRSISPFPELEQFLQDTIKRYNL------------QMLEAEG 368
Cdd:pfam01507   1 ELVVSFSGGKDSLVLLHL----ASKAFPPGP----VIFIDTGYEFPETYEFVDELEEKYGLnlkvylpedsfaEGINPEG 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296434309  369 S----------------MKQALGELQARhpqleAVLMGTRRTDPYSCSLCPFSPTDPGWPAFMRINPLLDWTYRDIWDFL 432
Cdd:pfam01507  73 IpsslyrrccrlrkvepLKRALKELGFD-----AWFTGLRRDESPSRAKLPIVSIDGDFPKVIKVFPLLNWTETDVWQYI 147

                         170
                  ....*....|....
gi 296434309  433 RQLFVPYCILYDRG 446
Cdd:pfam01507 148 LANNVPYNPLYDQG 161
MoCF_biosynth pfam00994
Probable molybdopterin binding domain; This domain is found a variety of proteins involved in ...
 17-108 1.32e-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: 101.56  E-value: 1.32e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296434309   17 GIIIVGDEILKGHTQDTNTFFLCRTLRSLGVQVCRVSVVPDEVATIAAEVTSFSNRFTHVLTAGGIGPTHDDVTFEAVAQ 96
Cdd:pfam00994   1 AIITTGDELLPGQIRDTNGPLLAALLREAGAEVIRYGIVPDDPEAIKEALRAAAEEADVVITTGGTGPGPDDVTPEALAE 80

                          90
                  ....*....|..
gi 296434309   97 AFGDELKPHPKL 108
Cdd:pfam00994  81 LGGRELPGFEEL 92
PRK01215 PRK01215
nicotinamide mononucleotide deamidase-related protein;
15-203 1.62e-25

nicotinamide mononucleotide deamidase-related protein;


Pssm-ID: 179250 [Multi-domain]  Cd Length: 264  Bit Score: 104.71  E-value: 1.62e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296434309  15 TAGIIIVGDEILKGHTQDTNTFFLCRTLRSLGVQVCRVSVVPDEVATIAAEVTSFSNRFTHVLTAGGIGPTHDDVTFEAV 94
Cdd:PRK01215   5 FAWIITIGNELLIGRTVNTNASWIARRLTYLGYTVRRITVVMDDIEEIVSAFREAIDRADVVVSTGGLGPTYDDKTNEGF 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296434309  95 AQAFGDELKPHP--------KLEAATKALGGEGwEKLSLVPSSARlhygtdpctgqPFRFP-------LVSVRN--VYLF 157
Cdd:PRK01215  85 AKALGVELELNEdalrmileKYEKRGIPLTPER-KKMAMMPPGAV-----------PLENPvgtapgiLIEHGGkdIVAL 152

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 296434309 158 PGIPELLRRVLEGM--KGLFQNPAVQFHSKELYVA-ADEASIAPILAEA 203
Cdd:PRK01215 153 PGVPREMEAIFENFvePLLKNRPPLKYYEDSILVEgVMESDLAPYVKEL 201
MoCF_biosynth smart00852
Probable molybdopterin binding domain; This domain is found a variety of proteins involved in ...
 17-102 1.91e-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: 95.35  E-value: 1.91e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296434309    17 GIIIVGDEILKGHTQ-DTNTFFLCRTLRSLGVQVCRVSVV--PDEVATIAAEVTSFSNRFTHVLTAGGIGPTHDDVTFEA 93
Cdd:smart00852   1 AIISTGDELLSGGQIrDSNGPMLAALLRELGIEVVRVVVVggPDDPEAIREALREALAEADVVITTGGTGPGPDDLTPEA 80


                   ....*....
gi 296434309    94 VAQAFGDEL 102
Cdd:smart00852  81 LAELGGREL 89
molyb_syn TIGR00177
molybdenum cofactor synthesis domain; The Drosophila protein cinnamon, the Arabidopsis protein ...
 14-102 1.52e-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: 70.81  E-value: 1.52e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296434309   14 VTAGIIIVGDEILKGHTQ-------DTNTFFLCRTLRSLGVQVCRVSVVPDEVATIAAEVTSFSNRFTHVLTAGGIGPTH 86
Cdd:TIGR00177   1 PRVAVISVGDELVEGGQPlepgqiyDSNGPLLAALLQEAGFNVVRLGIVPDDPEEIREILRKAVDEADVVLTTGGTGVGP 80

                          90
                  ....*....|....*.
gi 296434309   87 DDVTFEAVAQAFGDEL 102
Cdd:TIGR00177  81 RDVTPEALEELGEKEI 96
CysD COG0175
3'-phosphoadenosine 5'-phosphosulfate sulfotransferase (PAPS reductase)/FAD synthetase or ...
 284-446 4.16e-12

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: 65.64  E-value: 4.16e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296434309 284 AGALQTIETSLAQYSLTqLCVGFNGGKDCTALLHLfhaaVQRKLPDVPnplqILYI---RSispFPELEQFLQDTIKRYN 360
Cdd:COG0175   19 AEAIEILREAAAEFGGR-VVVSSSGGKDSTVLLHL----AAKFKPPIP----VLFLdtgYE---FPETYEFRDRLAERLG 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296434309 361 L------------QMLEAEG------------------SMKQALGELQArhpqlEAVLMGTRRTDpyscslcpfSPT--- 407
Cdd:COG0175   87 LdlivvrpedafaEQLAEFGpplfyrdprwcckirkvePLKRALAGYDF-----DAWITGLRRDE---------SPTrak 152

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 296434309 408 ------DPGwPAFMRINPLLDWTYRDIWDFLRQLFVPYCILYDRG 446
Cdd:COG0175  153 epvvewDPV-GGLIKVNPLADWTELDVWAYIRREDLPYNPLYDQG 196
PRK02090 PRK02090
phosphoadenylyl-sulfate reductase;
415-446 9.00e-06

phosphoadenylyl-sulfate reductase;


Pssm-ID: 234997  Cd Length: 241  Bit Score: 46.75  E-value: 9.00e-06
                         10        20        30
                 ....*....|....*....|....*....|..
gi 296434309 415 MRINPLLDWTYRDIWDFLRQLFVPYCILYDRG 446
Cdd:PRK02090 170 FKINPLADWTNEDVWAYLKEHDLPYHPLVDQG 201
PAPS_reductase TIGR02057
phosphoadenosine phosphosulfate reductase, thioredoxin dependent; Requiring thioredoxin as an ...
 283-446 9.58e-06

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: 46.75  E-value: 9.58e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296434309  283 VAGALQTIETSLAQYSltqlcvGFngGKDCTALLHLFHAAVQrklPDVPnplqILYIRSISPFPELEQFLQDTIKRYNLQ 362
Cdd:TIGR02057  17 IAWSIVTFPHGLVQTS------AF--GIQALVTLHLLSSISE---PMIP----VIFIDTLYHFPQTLTLKDELTKKYYQT 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296434309  363 M-------LEAEGSMKQALGEL------------------QARHPQLE--AVLMGTRRTDPYSCSLCPFSPTDpGWPAFM 415
Cdd:TIGR02057  82 LnlykydgCESEADFEAKYGKLlwqkdiekydyiakvepmQRALKELNasAWFTGRRRDQGSARANLPVIEID-EQNGIL 160

                         170       180       190
                  ....*....|....*....|....*....|.
gi 296434309  416 RINPLLDWTYRDIWDFLRQLFVPYCILYDRG 446
Cdd:TIGR02057 161 KVNPLIDWTFEQVYQYLDAHNVPYNPLLDQG 191
 
Name Accession Description Interval E-value
FAD_synthase cd23948
FAD synthase; FAD synthase (FMN:ATP adenylyl transferase (FMNAT); FAD pyrophosphorylase; ...
 282-446 4.93e-96

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: 286.34  E-value: 4.93e-96
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296434309 282 KVAGALQTIETSLAQYSLTQLCVGFNGGKDCTALLHLFHAAVQRKLPDVPNPLQILYIRSISPFPELEQFLQDTIKRYNL 361
Cdd:cd23948    1 KVKSALEVIEEALDKYGPEEIAISFNGGKDCTVLLHLLRAALKRKYPSPLTPLKALYIKSPDPFPEVEEFVEDTAKRYNL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296434309 362 QMLEAEGSMKQALGELQARHPQLEAVLMGTRRTDPYSCSLCPFSPTDPGWPAFMRINPLLDWTYRDIWDFLRQLFVPYCI 441
Cdd:cd23948   81 DLITIDGPMKEGLEELLKEHPIIKAVFMGTRRTDPHGENLKPFSPTDPGWPQFMRVNPILDWSYHDVWEFLRTLNLPYCS 160


                 ....*
gi 296434309 442 LYDRG 446
Cdd:cd23948  161 LYDQG 165
cinA cd00885
Competence-damaged protein. CinA is the first gene in the competence- inducible (cin) operon ...
 15-169 1.45e-54

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: 1.45e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296434309  15 TAGIIIVGDEILKGHTQDTNTFFLCRTLRSLGVQVCRVSVVPDEVATIAAEVTSFSNRFTHVLTAGGIGPTHDDVTFEAV 94
Cdd:cd00885    1 TAEIIAIGDELLSGQIVDTNAAFLAKELAELGIEVYRVTVVGDDEDRIAEALRRASERADLVITTGGLGPTHDDLTREAV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296434309  95 AQAFGDELKPHPKLEAATKALGGEGW-------EKLSLVPSSARL---HYGTdpctgqpfrFPLVSVR----NVYLFPGI 160
Cdd:cd00885   81 AKAFGRPLVLDEEALERIEARFARRGremteanLKQAMLPEGATLlpnPVGT---------APGFSVEhngkNVFLLPGV 151


                 ....*....
gi 296434309 161 PELLRRVLE 169
Cdd:cd00885  152 PSEMKPMLE 160
CinA COG1058
ADP-ribose pyrophosphatase domain of DNA damage- and competence-inducible protein CinA ...
 15-251 1.66e-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: 171.45  E-value: 1.66e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296434309  15 TAGIIIVGDEILKGHTQDTNTFFLCRTLRSLGVQVCRVSVVPDEVATIAAEVTSFSNRFTHVLTAGGIGPTHDDVTFEAV 94
Cdd:COG1058    1 KAEIITIGDELLSGRIVDTNAAWLARELAELGIDVYRITTVGDDPERIVEALREALARADLVITTGGLGPTPDDLTREAV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296434309  95 AQAFGDELKPHPKLEAATKALGGEGWEKLS-------LVPSSARL---HYGTDPCtgqpFRFPLVSVRnVYLFPGIPELL 164
Cdd:COG1058   81 AEALGVPLVLDPEALALIEERFAKRGREMTennlkqaLLPEGAELlpnPVGTAPG----FSIENNGKV-VIFLPGVPSEM 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296434309 165 RRVLEG-----MKGLFQNPAVqfHSKELYVA-ADEASIAPILAEAQAHFgRRLGLGSYPDWGsnYYQVKLTLDSEEEGPL 238
Cdd:COG1058  156 KPMFEEevlprLKKLFSGEPI--VSRTLRTFgIGESDLAELLEDLEARF-PNVTIGSYPSDG--EVRLRLTARGTDEEEA 230

                        250
                 ....*....|...
gi 296434309 239 EECLAYLTARLPQ 251
Cdd:COG1058  231 EAALEALEEELRE 243
PAPS_reduct pfam01507
Phosphoadenosine phosphosulfate reductase family; This domain is found in phosphoadenosine ...
 301-446 4.50e-26

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: 103.92  E-value: 4.50e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296434309  301 QLCVGFNGGKDCTALLHLfhaaVQRKLPDVPnplqILYIRSISPFPELEQFLQDTIKRYNL------------QMLEAEG 368
Cdd:pfam01507   1 ELVVSFSGGKDSLVLLHL----ASKAFPPGP----VIFIDTGYEFPETYEFVDELEEKYGLnlkvylpedsfaEGINPEG 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296434309  369 S----------------MKQALGELQARhpqleAVLMGTRRTDPYSCSLCPFSPTDPGWPAFMRINPLLDWTYRDIWDFL 432
Cdd:pfam01507  73 IpsslyrrccrlrkvepLKRALKELGFD-----AWFTGLRRDESPSRAKLPIVSIDGDFPKVIKVFPLLNWTETDVWQYI 147

                         170
                  ....*....|....
gi 296434309  433 RQLFVPYCILYDRG 446
Cdd:pfam01507 148 LANNVPYNPLYDQG 161
MoCF_biosynth pfam00994
Probable molybdopterin binding domain; This domain is found a variety of proteins involved in ...
 17-108 1.32e-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: 101.56  E-value: 1.32e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296434309   17 GIIIVGDEILKGHTQDTNTFFLCRTLRSLGVQVCRVSVVPDEVATIAAEVTSFSNRFTHVLTAGGIGPTHDDVTFEAVAQ 96
Cdd:pfam00994   1 AIITTGDELLPGQIRDTNGPLLAALLREAGAEVIRYGIVPDDPEAIKEALRAAAEEADVVITTGGTGPGPDDVTPEALAE 80

                          90
                  ....*....|..
gi 296434309   97 AFGDELKPHPKL 108
Cdd:pfam00994  81 LGGRELPGFEEL 92
PRK01215 PRK01215
nicotinamide mononucleotide deamidase-related protein;
15-203 1.62e-25

nicotinamide mononucleotide deamidase-related protein;


Pssm-ID: 179250 [Multi-domain]  Cd Length: 264  Bit Score: 104.71  E-value: 1.62e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296434309  15 TAGIIIVGDEILKGHTQDTNTFFLCRTLRSLGVQVCRVSVVPDEVATIAAEVTSFSNRFTHVLTAGGIGPTHDDVTFEAV 94
Cdd:PRK01215   5 FAWIITIGNELLIGRTVNTNASWIARRLTYLGYTVRRITVVMDDIEEIVSAFREAIDRADVVVSTGGLGPTYDDKTNEGF 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296434309  95 AQAFGDELKPHP--------KLEAATKALGGEGwEKLSLVPSSARlhygtdpctgqPFRFP-------LVSVRN--VYLF 157
Cdd:PRK01215  85 AKALGVELELNEdalrmileKYEKRGIPLTPER-KKMAMMPPGAV-----------PLENPvgtapgiLIEHGGkdIVAL 152

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 296434309 158 PGIPELLRRVLEGM--KGLFQNPAVQFHSKELYVA-ADEASIAPILAEA 203
Cdd:PRK01215 153 PGVPREMEAIFENFvePLLKNRPPLKYYEDSILVEgVMESDLAPYVKEL 201
MoCF_biosynth smart00852
Probable molybdopterin binding domain; This domain is found a variety of proteins involved in ...
 17-102 1.91e-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: 95.35  E-value: 1.91e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296434309    17 GIIIVGDEILKGHTQ-DTNTFFLCRTLRSLGVQVCRVSVV--PDEVATIAAEVTSFSNRFTHVLTAGGIGPTHDDVTFEA 93
Cdd:smart00852   1 AIISTGDELLSGGQIrDSNGPMLAALLRELGIEVVRVVVVggPDDPEAIREALREALAEADVVITTGGTGPGPDDLTPEA 80


                   ....*....
gi 296434309    94 VAQAFGDEL 102
Cdd:smart00852  81 LAELGGREL 89
PRK03670 PRK03670
competence damage-inducible protein A; Provisional
 16-248 5.30e-23

competence damage-inducible protein A; Provisional


Pssm-ID: 167581  Cd Length: 252  Bit Score: 97.56  E-value: 5.30e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296434309  16 AGIIIVGDEILKGHTQDTNTFFLCRTLRSLGVQVCRVSVVPDEVATIAAEVTSFSNRFTHVLT-AGGIGPTHDDVTFEAV 94
Cdd:PRK03670   3 AEIITVGDELLTGNTVDSNSAFIAQKLTEKGYWVRRITTVGDDVEEIKSVVLEILSRKPEVLViSGGLGPTHDDVTMLAV 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296434309  95 AQAFGDELKPHPKLEAATKALGGEGWEK-----LSLVPSSARLHY---GTDPCTGQPFRFP--LVSVRNVYLF--PGIPE 162
Cdd:PRK03670  83 AEALGRELVLCEDCLERIKEFYEELYKKgliddPTLNEARKKMAYlpeGAEPLENTEGAAPgaYIEHKGTKIFvlPGMPR 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296434309 163 LLRRVLEG--MKGLFQNPAVQfhSKELYVAADEASIAPILAEAQAHFGRRL-----GLGSYpdwgsnyyqVKLTLDSEEE 235
Cdd:PRK03670 163 EMKAMLEKevLPRLGERKFVQ--KKFLAEITDESKLAPILEEALERFNVKIhsspkGFGKY---------IGIIIFAEDE 231

                        250
                 ....*....|...
gi 296434309 236 GPLEECLAYLTAR 248
Cdd:PRK03670 232 EEIEKAVEFMEER 244
PRK00549 PRK00549
competence damage-inducible protein A; Provisional
 16-110 5.05e-15

competence damage-inducible protein A; Provisional


Pssm-ID: 234789 [Multi-domain]  Cd Length: 414  Bit Score: 76.37  E-value: 5.05e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296434309  16 AGIIIVGDEILKGHTQDTNTFFLCRTLRSLGVQVCRVSVVPDEVATIAAEVTSFSNRFTHVLTAGGIGPTHDDVTFEAVA 95
Cdd:PRK00549   3 AEIIAVGTELLLGQIVNTNAQFLSEKLAELGIDVYHQTVVGDNPERLLSALEIAEERSDLIITTGGLGPTKDDLTKETVA 82

                         90
                 ....*....|....*
gi 296434309  96 QAFGDELKPHPKLEA 110
Cdd:PRK00549  83 KFLGRELVLDEEALA 97
molyb_syn TIGR00177
molybdenum cofactor synthesis domain; The Drosophila protein cinnamon, the Arabidopsis protein ...
 14-102 1.52e-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: 70.81  E-value: 1.52e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296434309   14 VTAGIIIVGDEILKGHTQ-------DTNTFFLCRTLRSLGVQVCRVSVVPDEVATIAAEVTSFSNRFTHVLTAGGIGPTH 86
Cdd:TIGR00177   1 PRVAVISVGDELVEGGQPlepgqiyDSNGPLLAALLQEAGFNVVRLGIVPDDPEEIREILRKAVDEADVVLTTGGTGVGP 80

                          90
                  ....*....|....*.
gi 296434309   87 DDVTFEAVAQAFGDEL 102
Cdd:TIGR00177  81 RDVTPEALEELGEKEI 96
MoCF_BD cd00758
MoCF_BD: molybdenum cofactor (MoCF) binding domain (BD). This domain is found a variety of ...
 16-100 7.69e-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: 68.14  E-value: 7.69e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296434309  16 AGIIIVGDEILKGHTQDTNTFFLCRTLRSLGVQVCRVSVVPDEVATIAAEVTSFSNRFTHVLTAGGIGPTHDDVTFEAVA 95
Cdd:cd00758    2 VAIVTVSDELSQGQIEDTNGPALEALLEDLGCEVIYAGVVPDDADSIRAALIEASREADLVLTTGGTGVGRRDVTPEALA 81


                 ....*
gi 296434309  96 qAFGD 100
Cdd:cd00758   82 -ELGE 85
PAPS_reductase-like_YbdN cd23947
uncharacterized phosphoadenosine phosphosulfate reductase-like proteins, similar to ...
 303-446 2.83e-12

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: 65.49  E-value: 2.83e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296434309 303 CVGFNGGKDCTALLHLFHAAVQRKLPDVPnplqILYIRSISPFPELEQFLQDTIKRYNLQMLEAEGSMKQALGELQA--- 379
Cdd:cd23947   16 IVSFSGGKDSLVLLHLALEALRRLRKDVY----VVFIDTGIEFPETIDFVEKLAETLGLDVEAARPPLFLEWLTSNFqpq 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296434309 380 ------------------------------RHPQLEAVLM--GTRRTDPYSCSLCPFSPTDPGW-----PAFMRINPLLD 422
Cdd:cd23947   92 wdpiwdnpppprdyrwccdelklepftkwlKEKKPEGVLLlvGIRADESLNRAKRPRVYRKYGWrnstlPGQIVAYPIKD 171

                        170       180
                 ....*....|....*....|....
gi 296434309 423 WTYRDIWDFLRQLFVPYCILYDRG 446
Cdd:cd23947  172 WSVEDVWLYILRHGLPYNPLYDLG 195
CysD COG0175
3'-phosphoadenosine 5'-phosphosulfate sulfotransferase (PAPS reductase)/FAD synthetase or ...
 284-446 4.16e-12

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: 65.64  E-value: 4.16e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296434309 284 AGALQTIETSLAQYSLTqLCVGFNGGKDCTALLHLfhaaVQRKLPDVPnplqILYI---RSispFPELEQFLQDTIKRYN 360
Cdd:COG0175   19 AEAIEILREAAAEFGGR-VVVSSSGGKDSTVLLHL----AAKFKPPIP----VLFLdtgYE---FPETYEFRDRLAERLG 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296434309 361 L------------QMLEAEG------------------SMKQALGELQArhpqlEAVLMGTRRTDpyscslcpfSPT--- 407
Cdd:COG0175   87 LdlivvrpedafaEQLAEFGpplfyrdprwcckirkvePLKRALAGYDF-----DAWITGLRRDE---------SPTrak 152

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 296434309 408 ------DPGwPAFMRINPLLDWTYRDIWDFLRQLFVPYCILYDRG 446
Cdd:COG0175  153 epvvewDPV-GGLIKVNPLADWTELDVWAYIRREDLPYNPLYDQG 196
cinA_nterm TIGR00200
competence/damage-inducible protein CinA N-terminal domain; cinA is a DNA damage- or ...
 16-170 8.81e-12

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: 8.81e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296434309   16 AGIIIVGDEILKGHTQDTNTFFLCRTLRSLGVQVCRVSVV---PDEVATIAAEVtsfSNRFTHVLTAGGIGPTHDDVTFE 92
Cdd:TIGR00200   3 AEIISVGDELLLGQIVNTNAQWLADFLAHQGLPLSRRTTVgdnPERLKTIIRIA---SERADVLIFNGGLGPTSDDLTAE 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296434309   93 AVAQAFGDELKPH----PKLEAATKALG---GEGWEKLSLVPSSARL---HYGTDPctgQPFRFPLvSVRNVYLFPGIPE 162
Cdd:TIGR00200  80 TIATAKGEPLVLNeawlKEIERYFHETGrvmAPNNRKQALLPAGAEFlanPVGTAP---GMFAVQL-NRCLMLFTPGVPS 155


                  ....*...
gi 296434309  163 LLRRVLEG 170
Cdd:TIGR00200 156 EFRVMVEH 163
MogA_MoaB cd00886
MogA_MoaB family. Members of this family are involved in biosynthesis of the molybdenum ...
 14-95 2.84e-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: 61.34  E-value: 2.84e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296434309  14 VTAGIIIVGDEILKGHTQDTNTFFLCRTLRSLGVQVCRVSVVPDEVATIAAEVTSFSNRFTH--VLTAGGIGPTHDDVTF 91
Cdd:cd00886    1 LRAAVLTVSDTRSAGEAEDRSGPALVELLEEAGHEVVAYEIVPDDKDEIREALIEWADEDGVdlILTTGGTGLAPRDVTP 80


                 ....
gi 296434309  92 EAVA 95
Cdd:cd00886   81 EATR 84
MoaB COG0521
Molybdopterin biosynthesis enzyme MoaB/MogA [Coenzyme transport and metabolism]; Molybdopterin ...
 6-95 7.88e-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: 57.43  E-value: 7.88e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296434309   6 SELSPGRSVTAGIIIVGDEILKGHTQDTNTFFLCRTLRSLGVQVCRVSVVPDEVATIAAEVTSFSNRFTH--VLTAGGIG 83
Cdd:COG0521    2 SSARAFVPLRIAVLTVSDRRSRGEREDTSGPALVELLEEAGHEVVARRIVPDDKDAIRAALRELIDDEGVdlVLTTGGTG 81

                         90
                 ....*....|..
gi 296434309  84 PTHDDVTFEAVA 95
Cdd:COG0521   82 LSPRDVTPEATR 93
PAPS_reductase cd23945
Phosphoadenylyl-sulfate reductase (thioredoxin); Phosphoadenosine phosphosulfate (PAPS) ...
 416-446 1.79e-07

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: 51.06  E-value: 1.79e-07
                         10        20        30
                 ....*....|....*....|....*....|.
gi 296434309 416 RINPLLDWTYRDIWDFLRQLFVPYCILYDRG 446
Cdd:cd23945  148 KINPLADWTWEDVWAYIREHDLPYNPLHDQG 178
PRK03673 PRK03673
nicotinamide mononucleotide deamidase-related protein YfaY;
22-106 3.98e-07

nicotinamide mononucleotide deamidase-related protein YfaY;


Pssm-ID: 179629 [Multi-domain]  Cd Length: 396  Bit Score: 52.01  E-value: 3.98e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296434309  22 GDEILKGHTQDTNTFFLCRTLRSLGVQVCRVSVVPDEVATIAAEVTSFSNRFTHVLTAGGIGPTHDDVTFEAVAQAFGDE 101
Cdd:PRK03673  10 GDEVLHGQIVDTNAAWLADFFFHQGLPLSRRNTVGDNLDALVAILRERSQHADVLIVNGGLGPTSDDLSALAAATAAGEG 89


                 ....*
gi 296434309 102 LKPHP 106
Cdd:PRK03673  90 LVLHE 94
PRK02090 PRK02090
phosphoadenylyl-sulfate reductase;
415-446 9.00e-06

phosphoadenylyl-sulfate reductase;


Pssm-ID: 234997  Cd Length: 241  Bit Score: 46.75  E-value: 9.00e-06
                         10        20        30
                 ....*....|....*....|....*....|..
gi 296434309 415 MRINPLLDWTYRDIWDFLRQLFVPYCILYDRG 446
Cdd:PRK02090 170 FKINPLADWTNEDVWAYLKEHDLPYHPLVDQG 201
PAPS_reductase TIGR02057
phosphoadenosine phosphosulfate reductase, thioredoxin dependent; Requiring thioredoxin as an ...
 283-446 9.58e-06

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: 46.75  E-value: 9.58e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296434309  283 VAGALQTIETSLAQYSltqlcvGFngGKDCTALLHLFHAAVQrklPDVPnplqILYIRSISPFPELEQFLQDTIKRYNLQ 362
Cdd:TIGR02057  17 IAWSIVTFPHGLVQTS------AF--GIQALVTLHLLSSISE---PMIP----VIFIDTLYHFPQTLTLKDELTKKYYQT 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296434309  363 M-------LEAEGSMKQALGEL------------------QARHPQLE--AVLMGTRRTDPYSCSLCPFSPTDpGWPAFM 415
Cdd:TIGR02057  82 LnlykydgCESEADFEAKYGKLlwqkdiekydyiakvepmQRALKELNasAWFTGRRRDQGSARANLPVIEID-EQNGIL 160

                         170       180       190
                  ....*....|....*....|....*....|.
gi 296434309  416 RINPLLDWTYRDIWDFLRQLFVPYCILYDRG 446
Cdd:TIGR02057 161 KVNPLIDWTFEQVYQYLDAHNVPYNPLLDQG 191
MoeA cd00887
MoeA family. Members of this family are involved in biosynthesis of the molybdenum cofactor ...
 12-102 4.36e-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: 45.56  E-value: 4.36e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296434309  12 RSVTAGIIIVGDEIL-------KGHTQDTNTFFLCRTLRSLGVQVCRVSVVPDEVATIAAEVTSFSNRFTHVLTAGGIGP 84
Cdd:cd00887  167 RRPRVAIISTGDELVepgeplaPGQIYDSNSYMLAALLRELGAEVVDLGIVPDDPEALREALEEALEEADVVITSGGVSV 246

                         90
                 ....*....|....*...
gi 296434309  85 THDDVTFEAVAQAFGDEL 102
Cdd:cd00887  247 GDYDFVKEVLEELGGEVL 264
MoeA COG0303
Molybdopterin Mo-transferase (molybdopterin biosynthesis) [Coenzyme transport and metabolism]; ...
 12-102 7.13e-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: 44.69  E-value: 7.13e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296434309  12 RSVTAGIIIVGDEIL-------KGHTQDTNTFFLCRTLRSLGVQVCRVSVVPDEVATIAAEVTSFSNRFTHVLTAGGIGP 84
Cdd:COG0303  171 RRPRVAILSTGDELVepgeplgPGQIYDSNSYMLAALLREAGAEVVDLGIVPDDPEALRAALREALAEADLVITSGGVSV 250

                         90
                 ....*....|....*...
gi 296434309  85 THDDVTFEAVAqAFGDEL 102
Cdd:COG0303  251 GDYDLVKEALE-ELGAEV 267
AANH-like cd01986
adenine nucleotide alpha hydrolase (AANH)-like proteins; This group of adenine nucleotide ...
 303-393 3.71e-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: 3.71e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296434309 303 CVGFNGGKDCTALLHLFHAAVQRKlpdvpnPLQILYIRSISPFPELEQFLQDTIKRynlqmleaegSMKQALGELQARHp 382
Cdd:cd01986    2 VVGYSGGKDSSVALHLASRLGRKA------EVAVVHIDHGIGFKEEAESVASIARR----------SILKKLAEKGARA- 64

                         90
                 ....*....|.
gi 296434309 383 qleaVLMGTRR 393
Cdd:cd01986   65 ----IATGVLR 71
MoeA_like cd03522
MoeA_like. This domain is similar to a domain found in a variety of proteins involved in ...
 7-100 3.79e-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: 3.79e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296434309   7 ELSPGRSVTAGIIIVGDEILKGHTQDTNTFFLCRTLRSLGVQVCRVSVVPDEVATIAAEVTSF--SNRFTHVLTAGGI-G 83
Cdd:cd03522  153 RVAPFRPLRVGLIVTGSEVYGGRIEDKFGPVLRARLAALGVELVEQVIVPHDEAAIAAAIAEAleAGAELLILTGGASvD 232

                         90
                 ....*....|....*..
gi 296434309  84 PthDDVTFEAVAQAFGD 100
Cdd:cd03522  233 P--DDVTPAAIRAAGGE 247
PLN02699 PLN02699
Bifunctional molybdopterin adenylyltransferase/molybdopterin molybdenumtransferase
 46-93 8.69e-03

Bifunctional molybdopterin adenylyltransferase/molybdopterin molybdenumtransferase


Pssm-ID: 215376 [Multi-domain]  Cd Length: 659  Bit Score: 38.64  E-value: 8.69e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 296434309  46 GVQVCRVSVVPDEVATIAAEVTSFS--NRFTHVLTAGGIGPTHDDVTFEA 93
Cdd:PLN02699 496 GAKVVATAVVPDDVEKIKDVLQKWSdiDRMDLILTLGGTGFTPRDVTPEA 545
 
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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