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Conserved domains on  [gi|2102663963|ref|XP_043798083|]
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FAD synthase-like [Apis laboriosa]

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; ...
 266-440 5.10e-85

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: 258.61  E-value: 5.10e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2102663963 266 HIKYAVDILQQCYKMYKPEEIFISFNGGKDCTVVLHLAACITKLQNISS---LLCLYV-IAEPFPEVDSFVEKAVQYYDL 341
Cdd:cd23948     1 KVKSALEVIEEALDKYGPEEIAISFNGGKDCTVLLHLLRAALKRKYPSPltpLKALYIkSPDPFPEVEEFVEDTAKRYNL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2102663963 342 ELIKKKYPMRLALCSLLNEKTNIKASLMGMRKGDPGSENLEAFTPTDPNWPNLIRVNPILNWSYDQVWKFLLKHNVPYCP 421
Cdd:cd23948    81 DLITIDGPMKEGLEELLKEHPIIKAVFMGTRRTDPHGENLKPFSPTDPGWPQFMRVNPILDWSYHDVWEFLRTLNLPYCS 160

                         170
                  ....*....|....*....
gi 2102663963 422 LYDKGYTSLGTKSTTKPNP 440
Cdd:cd23948   161 LYDQGYTSLGSVDNTLPNP 179
MoCF_BD super family cl00451
MoCF_BD: molybdenum cofactor (MoCF) binding domain (BD). This domain is found a variety of ...
 7-167 5.72e-46

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.


The actual alignment was detected with superfamily member cd00885:

Pssm-ID: 444911 [Multi-domain]  Cd Length: 170  Bit Score: 157.26  E-value: 5.72e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2102663963   7 TAGLIVIGDEILRGQIIDTNTSYLAKRLQASGIKLRKVTVILDIVDEIAKTVLDFSKEYSIVFTSGGVGPTHDDVTYEAI 86
Cdd:cd00885     1 TAEIIAIGDELLSGQIVDTNAAFLAKELAELGIEVYRVTVVGDDEDRIAEALRRASERADLVITTGGLGPTHDDLTREAV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2102663963  87 AKGLGLKLEQHEELVDIYLNLF--------PNHKKEAQrltiVPRPCELIyvYSPKKYA---IVKV--KNIYMLPGSPKY 153
Cdd:cd00885    81 AKAFGRPLVLDEEALERIEARFarrgremtEANLKQAM----LPEGATLL--PNPVGTApgfSVEHngKNVFLLPGVPSE 154

                         170
                  ....*....|....*
gi 2102663963 154 FELSID-TIIPQLKG 167
Cdd:cd00885   155 MKPMLEeEVLPRLRE 169
 
Name Accession Description Interval E-value
FAD_synthase cd23948
FAD synthase; FAD synthase (FMN:ATP adenylyl transferase (FMNAT); FAD pyrophosphorylase; ...
 266-440 5.10e-85

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: 258.61  E-value: 5.10e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2102663963 266 HIKYAVDILQQCYKMYKPEEIFISFNGGKDCTVVLHLAACITKLQNISS---LLCLYV-IAEPFPEVDSFVEKAVQYYDL 341
Cdd:cd23948     1 KVKSALEVIEEALDKYGPEEIAISFNGGKDCTVLLHLLRAALKRKYPSPltpLKALYIkSPDPFPEVEEFVEDTAKRYNL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2102663963 342 ELIKKKYPMRLALCSLLNEKTNIKASLMGMRKGDPGSENLEAFTPTDPNWPNLIRVNPILNWSYDQVWKFLLKHNVPYCP 421
Cdd:cd23948    81 DLITIDGPMKEGLEELLKEHPIIKAVFMGTRRTDPHGENLKPFSPTDPGWPQFMRVNPILDWSYHDVWEFLRTLNLPYCS 160

                         170
                  ....*....|....*....
gi 2102663963 422 LYDKGYTSLGTKSTTKPNP 440
Cdd:cd23948   161 LYDQGYTSLGSVDNTLPNP 179
cinA cd00885
Competence-damaged protein. CinA is the first gene in the competence- inducible (cin) operon ...
 7-167 5.72e-46

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: 157.26  E-value: 5.72e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2102663963   7 TAGLIVIGDEILRGQIIDTNTSYLAKRLQASGIKLRKVTVILDIVDEIAKTVLDFSKEYSIVFTSGGVGPTHDDVTYEAI 86
Cdd:cd00885     1 TAEIIAIGDELLSGQIVDTNAAFLAKELAELGIEVYRVTVVGDDEDRIAEALRRASERADLVITTGGLGPTHDDLTREAV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2102663963  87 AKGLGLKLEQHEELVDIYLNLF--------PNHKKEAQrltiVPRPCELIyvYSPKKYA---IVKV--KNIYMLPGSPKY 153
Cdd:cd00885    81 AKAFGRPLVLDEEALERIEARFarrgremtEANLKQAM----LPEGATLL--PNPVGTApgfSVEHngKNVFLLPGVPSE 154

                         170
                  ....*....|....*
gi 2102663963 154 FELSID-TIIPQLKG 167
Cdd:cd00885   155 MKPMLEeEVLPRLRE 169
CinA COG1058
ADP-ribose pyrophosphatase domain of DNA damage- and competence-inducible protein CinA ...
 7-245 1.49e-44

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


Pssm-ID: 440678  Cd Length: 249  Bit Score: 156.43  E-value: 1.49e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2102663963   7 TAGLIVIGDEILRGQIIDTNTSYLAKRLQASGIKLRKVTVILDIVDEIAKTVLDFSKEYSIVFTSGGVGPTHDDVTYEAI 86
Cdd:COG1058     1 KAEIITIGDELLSGRIVDTNAAWLARELAELGIDVYRITTVGDDPERIVEALREALARADLVITTGGLGPTPDDLTREAV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2102663963  87 AKGLGLKLEQHEELVDIYLNLF--------PNHKKEAQrltiVPRPCELIyvysPKKY-----AIVKVKN--IYMLPGSP 151
Cdd:COG1058    81 AEALGVPLVLDPEALALIEERFakrgremtENNLKQAL----LPEGAELL----PNPVgtapgFSIENNGkvVIFLPGVP 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2102663963 152 ---KY-FELSIDTIIPQLKGNIPLYFEQIDI-NLNELSIVQILDEHAKLWKDkINIGSYPQiIPECSfTRITLEGKKEDV 226
Cdd:COG1058   153 semKPmFEEEVLPRLKKLFSGEPIVSRTLRTfGIGESDLAELLEDLEARFPN-VTIGSYPS-DGEVR-LRLTARGTDEEE 229

                         250
                  ....*....|....*....
gi 2102663963 227 LEAKAKFLyslpIQKIRNL 245
Cdd:COG1058   230 AEAALEAL----EEELRER 244
PAPS_reduct pfam01507
Phosphoadenosine phosphosulfate reductase family; This domain is found in phosphoadenosine ...
 285-438 8.78e-32

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: 119.71  E-value: 8.78e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2102663963 285 EIFISFNGGKDCTVVLHLAaciTKLQNISSLLCLYVIAEpFPEVDSFVEKAVQYYDLEL--------------------- 343
Cdd:pfam01507   1 ELVVSFSGGKDSLVLLHLA---SKAFPPGPVIFIDTGYE-FPETYEFVDELEEKYGLNLkvylpedsfaeginpegipss 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2102663963 344 -------IKKKYPMRLALcsllnEKTNIKASLMGMRKGDPGSENLEAFTPTDPNWPNLIRVNPILNWSYDQVWKFLLKHN 416
Cdd:pfam01507  77 lyrrccrLRKVEPLKRAL-----KELGFDAWFTGLRRDESPSRAKLPIVSIDGDFPKVIKVFPLLNWTETDVWQYILANN 151

                         170       180
                  ....*....|....*....|..
gi 2102663963 417 VPYCPLYDKGYTSLGTKSTTKP 438
Cdd:pfam01507 152 VPYNPLYDQGYRSIGCYPCTGP 173
MoCF_biosynth pfam00994
Probable molybdopterin binding domain; This domain is found a variety of proteins involved in ...
 9-166 8.99e-32

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: 118.51  E-value: 8.99e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2102663963   9 GLIVIGDEILRGQIIDTNTSYLAKRLQASGIKLRKVTVILDIVDEIAKTVLDFSKEYSIVFTSGGVGPTHDDVTYEAIAK 88
Cdd:pfam00994   1 AIITTGDELLPGQIRDTNGPLLAALLREAGAEVIRYGIVPDDPEAIKEALRAAAEEADVVITTGGTGPGPDDVTPEALAE 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2102663963  89 GLGLKLEQHEELVDiYLNLFPNHKKEAQRLTIVPRPCeliyvyspkkyaivkvKNIYMLPGSPKYFELSIDTII-PQLK 166
Cdd:pfam00994  81 LGGRELPGFEELFR-GVSLKPGKPVGTAPGAILSRAG----------------KTVFGLPGSPVAAKVMFELLLlPLLR 142
MoCF_biosynth smart00852
Probable molybdopterin binding domain; This domain is found a variety of proteins involved in ...
 9-152 9.32e-27

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: 104.59  E-value: 9.32e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2102663963    9 GLIVIGDEILRGQII-DTNTSYLAKRLQASGIKLRKVTVIL--DIVDEIAKTVLDFSKEYSIVFTSGGVGPTHDDVTYEA 85
Cdd:smart00852   1 AIISTGDELLSGGQIrDSNGPMLAALLRELGIEVVRVVVVGgpDDPEAIREALREALAEADVVITTGGTGPGPDDLTPEA 80

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2102663963   86 IAKGLGLKLEqheelvdiylnlfpnHKKEAQRltivP-RPCELIYVYSPKKYAIVKVKNIYMLPGSPK 152
Cdd:smart00852  81 LAELGGRELL---------------GHGVAMR----PgGPPGPLANLSGTAPGVRGKKPVFGLPGNPV 129
PRK01215 PRK01215
nicotinamide mononucleotide deamidase-related protein;
6-207 1.52e-23

nicotinamide mononucleotide deamidase-related protein;


Pssm-ID: 179250 [Multi-domain]  Cd Length: 264  Bit Score: 99.32  E-value: 1.52e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2102663963   6 YTAGLIVIGDEILRGQIIDTNTSYLAKRLQASGIKLRKVTVILDIVDEIA---KTVLDFSKeysIVFTSGGVGPTHDDVT 82
Cdd:PRK01215    4 WFAWIITIGNELLIGRTVNTNASWIARRLTYLGYTVRRITVVMDDIEEIVsafREAIDRAD---VVVSTGGLGPTYDDKT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2102663963  83 YEAIAKGLGLKLEQHEELVDIYLNLFPNHK----KEAQRLTIVPRPCELI---YVYSPKKYAIVKVKNIYMLPGSPKYFE 155
Cdd:PRK01215   81 NEGFAKALGVELELNEDALRMILEKYEKRGipltPERKKMAMMPPGAVPLenpVGTAPGILIEHGGKDIVALPGVPREME 160

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2102663963 156 LSIDTII-PQLKGNIPLYFEQIDINLN---ELSIVQILDEHAKLWkDKINIGSYPQ 207
Cdd:PRK01215  161 AIFENFVePLLKNRPPLKYYEDSILVEgvmESDLAPYVKELVKKY-DRVYVKSHPK 215
CysD COG0175
3'-phosphoadenosine 5'-phosphosulfate sulfotransferase (PAPS reductase)/FAD synthetase or ...
 270-431 6.59e-21

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: 91.06  E-value: 6.59e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2102663963 270 AVDILQQCYKMYkPEEIFISFNGGKDCTVVLHLAACITKlqNIssllclYVI-----AEpFPEVDSFVEKAVQYYDLELI 344
Cdd:COG0175    21 AIEILREAAAEF-GGRVVVSSSGGKDSTVLLHLAAKFKP--PI------PVLfldtgYE-FPETYEFRDRLAERLGLDLI 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2102663963 345 K------------------------------KKYPMRLALcsllnEKTNIKASLMGMRKGDPGS-ENLEAFTPtDPNwPN 393
Cdd:COG0175    91 VvrpedafaeqlaefgpplfyrdprwcckirKVEPLKRAL-----AGYDFDAWITGLRRDESPTrAKEPVVEW-DPV-GG 163

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 2102663963 394 LIRVNPILNWSYDQVWKFLLKHNVPYCPLYDKGYTSLG 431
Cdd:COG0175   164 LIKVNPLADWTELDVWAYIRREDLPYNPLYDQGYPSIG 201
molyb_syn TIGR00177
molybdenum cofactor synthesis domain; The Drosophila protein cinnamon, the Arabidopsis protein ...
 6-162 9.99e-21

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: 88.14  E-value: 9.99e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2102663963   6 YTAGLIVIGDEILRG-------QIIDTNTSYLAKRLQASGIKLRKVTVILDIVDEIAKTVLDFSKEYSIVFTSGGVGPTH 78
Cdd:TIGR00177   1 PRVAVISVGDELVEGgqplepgQIYDSNGPLLAALLQEAGFNVVRLGIVPDDPEEIREILRKAVDEADVVLTTGGTGVGP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2102663963  79 DDVTYEAIakglglkleqhEELVDIylnLFPNHKKEAQR--LTIVPRPCELIYVyspkkyAIVKVKNIYMLPGSPKYFEL 156
Cdd:TIGR00177  81 RDVTPEAL-----------EELGEK---EIPGFGEFRMLssLPVLSRPGKPATA------GVRGGTLIFNLPGNPVSALV 140


                  ....*.
gi 2102663963 157 SIDTII 162
Cdd:TIGR00177 141 TFEVLI 146
PAPS_reductase TIGR02057
phosphoadenosine phosphosulfate reductase, thioredoxin dependent; Requiring thioredoxin as an ...
 333-438 1.07e-13

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: 70.25  E-value: 1.07e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2102663963 333 EKAVQYYDLelIKKKYPMRLALCSLlnektNIKASLMGMRKGDPGS-ENLEAFTPTDPNwpNLIRVNPILNWSYDQVWKF 411
Cdd:TIGR02057 106 QKDIEKYDY--IAKVEPMQRALKEL-----NASAWFTGRRRDQGSArANLPVIEIDEQN--GILKVNPLIDWTFEQVYQY 176

                          90       100
                  ....*....|....*....|....*..
gi 2102663963 412 LLKHNVPYCPLYDKGYTSLGTKSTTKP 438
Cdd:TIGR02057 177 LDAHNVPYNPLLDQGYRSIGDYHSTRK 203
PRK02090 PRK02090
phosphoadenylyl-sulfate reductase;
344-438 1.38e-12

phosphoadenylyl-sulfate reductase;


Pssm-ID: 234997  Cd Length: 241  Bit Score: 67.17  E-value: 1.38e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2102663963 344 IKKKYPMRLALCSLlnektniKASLMGMRKGDPGS-ENLEAFTPTDpnwpNLIRVNPILNWSYDQVWKFLLKHNVPYCPL 422
Cdd:PRK02090  129 IRKVEPLNRALAGL-------DAWITGLRREQSGTrANLPVLEIDG----GRFKINPLADWTNEDVWAYLKEHDLPYHPL 197

                          90
                  ....*....|....*.
gi 2102663963 423 YDKGYTSLGTKSTTKP 438
Cdd:PRK02090  198 VDQGYPSIGCEPCTRP 213
 
Name Accession Description Interval E-value
FAD_synthase cd23948
FAD synthase; FAD synthase (FMN:ATP adenylyl transferase (FMNAT); FAD pyrophosphorylase; ...
 266-440 5.10e-85

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: 258.61  E-value: 5.10e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2102663963 266 HIKYAVDILQQCYKMYKPEEIFISFNGGKDCTVVLHLAACITKLQNISS---LLCLYV-IAEPFPEVDSFVEKAVQYYDL 341
Cdd:cd23948     1 KVKSALEVIEEALDKYGPEEIAISFNGGKDCTVLLHLLRAALKRKYPSPltpLKALYIkSPDPFPEVEEFVEDTAKRYNL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2102663963 342 ELIKKKYPMRLALCSLLNEKTNIKASLMGMRKGDPGSENLEAFTPTDPNWPNLIRVNPILNWSYDQVWKFLLKHNVPYCP 421
Cdd:cd23948    81 DLITIDGPMKEGLEELLKEHPIIKAVFMGTRRTDPHGENLKPFSPTDPGWPQFMRVNPILDWSYHDVWEFLRTLNLPYCS 160

                         170
                  ....*....|....*....
gi 2102663963 422 LYDKGYTSLGTKSTTKPNP 440
Cdd:cd23948   161 LYDQGYTSLGSVDNTLPNP 179
cinA cd00885
Competence-damaged protein. CinA is the first gene in the competence- inducible (cin) operon ...
 7-167 5.72e-46

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: 157.26  E-value: 5.72e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2102663963   7 TAGLIVIGDEILRGQIIDTNTSYLAKRLQASGIKLRKVTVILDIVDEIAKTVLDFSKEYSIVFTSGGVGPTHDDVTYEAI 86
Cdd:cd00885     1 TAEIIAIGDELLSGQIVDTNAAFLAKELAELGIEVYRVTVVGDDEDRIAEALRRASERADLVITTGGLGPTHDDLTREAV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2102663963  87 AKGLGLKLEQHEELVDIYLNLF--------PNHKKEAQrltiVPRPCELIyvYSPKKYA---IVKV--KNIYMLPGSPKY 153
Cdd:cd00885    81 AKAFGRPLVLDEEALERIEARFarrgremtEANLKQAM----LPEGATLL--PNPVGTApgfSVEHngKNVFLLPGVPSE 154

                         170
                  ....*....|....*
gi 2102663963 154 FELSID-TIIPQLKG 167
Cdd:cd00885   155 MKPMLEeEVLPRLRE 169
CinA COG1058
ADP-ribose pyrophosphatase domain of DNA damage- and competence-inducible protein CinA ...
 7-245 1.49e-44

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


Pssm-ID: 440678  Cd Length: 249  Bit Score: 156.43  E-value: 1.49e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2102663963   7 TAGLIVIGDEILRGQIIDTNTSYLAKRLQASGIKLRKVTVILDIVDEIAKTVLDFSKEYSIVFTSGGVGPTHDDVTYEAI 86
Cdd:COG1058     1 KAEIITIGDELLSGRIVDTNAAWLARELAELGIDVYRITTVGDDPERIVEALREALARADLVITTGGLGPTPDDLTREAV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2102663963  87 AKGLGLKLEQHEELVDIYLNLF--------PNHKKEAQrltiVPRPCELIyvysPKKY-----AIVKVKN--IYMLPGSP 151
Cdd:COG1058    81 AEALGVPLVLDPEALALIEERFakrgremtENNLKQAL----LPEGAELL----PNPVgtapgFSIENNGkvVIFLPGVP 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2102663963 152 ---KY-FELSIDTIIPQLKGNIPLYFEQIDI-NLNELSIVQILDEHAKLWKDkINIGSYPQiIPECSfTRITLEGKKEDV 226
Cdd:COG1058   153 semKPmFEEEVLPRLKKLFSGEPIVSRTLRTfGIGESDLAELLEDLEARFPN-VTIGSYPS-DGEVR-LRLTARGTDEEE 229

                         250
                  ....*....|....*....
gi 2102663963 227 LEAKAKFLyslpIQKIRNL 245
Cdd:COG1058   230 AEAALEAL----EEELRER 244
PAPS_reduct pfam01507
Phosphoadenosine phosphosulfate reductase family; This domain is found in phosphoadenosine ...
 285-438 8.78e-32

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: 119.71  E-value: 8.78e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2102663963 285 EIFISFNGGKDCTVVLHLAaciTKLQNISSLLCLYVIAEpFPEVDSFVEKAVQYYDLEL--------------------- 343
Cdd:pfam01507   1 ELVVSFSGGKDSLVLLHLA---SKAFPPGPVIFIDTGYE-FPETYEFVDELEEKYGLNLkvylpedsfaeginpegipss 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2102663963 344 -------IKKKYPMRLALcsllnEKTNIKASLMGMRKGDPGSENLEAFTPTDPNWPNLIRVNPILNWSYDQVWKFLLKHN 416
Cdd:pfam01507  77 lyrrccrLRKVEPLKRAL-----KELGFDAWFTGLRRDESPSRAKLPIVSIDGDFPKVIKVFPLLNWTETDVWQYILANN 151

                         170       180
                  ....*....|....*....|..
gi 2102663963 417 VPYCPLYDKGYTSLGTKSTTKP 438
Cdd:pfam01507 152 VPYNPLYDQGYRSIGCYPCTGP 173
MoCF_biosynth pfam00994
Probable molybdopterin binding domain; This domain is found a variety of proteins involved in ...
 9-166 8.99e-32

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: 118.51  E-value: 8.99e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2102663963   9 GLIVIGDEILRGQIIDTNTSYLAKRLQASGIKLRKVTVILDIVDEIAKTVLDFSKEYSIVFTSGGVGPTHDDVTYEAIAK 88
Cdd:pfam00994   1 AIITTGDELLPGQIRDTNGPLLAALLREAGAEVIRYGIVPDDPEAIKEALRAAAEEADVVITTGGTGPGPDDVTPEALAE 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2102663963  89 GLGLKLEQHEELVDiYLNLFPNHKKEAQRLTIVPRPCeliyvyspkkyaivkvKNIYMLPGSPKYFELSIDTII-PQLK 166
Cdd:pfam00994  81 LGGRELPGFEELFR-GVSLKPGKPVGTAPGAILSRAG----------------KTVFGLPGSPVAAKVMFELLLlPLLR 142
MoCF_biosynth smart00852
Probable molybdopterin binding domain; This domain is found a variety of proteins involved in ...
 9-152 9.32e-27

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: 104.59  E-value: 9.32e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2102663963    9 GLIVIGDEILRGQII-DTNTSYLAKRLQASGIKLRKVTVIL--DIVDEIAKTVLDFSKEYSIVFTSGGVGPTHDDVTYEA 85
Cdd:smart00852   1 AIISTGDELLSGGQIrDSNGPMLAALLRELGIEVVRVVVVGgpDDPEAIREALREALAEADVVITTGGTGPGPDDLTPEA 80

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2102663963   86 IAKGLGLKLEqheelvdiylnlfpnHKKEAQRltivP-RPCELIYVYSPKKYAIVKVKNIYMLPGSPK 152
Cdd:smart00852  81 LAELGGRELL---------------GHGVAMR----PgGPPGPLANLSGTAPGVRGKKPVFGLPGNPV 129
PRK01215 PRK01215
nicotinamide mononucleotide deamidase-related protein;
6-207 1.52e-23

nicotinamide mononucleotide deamidase-related protein;


Pssm-ID: 179250 [Multi-domain]  Cd Length: 264  Bit Score: 99.32  E-value: 1.52e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2102663963   6 YTAGLIVIGDEILRGQIIDTNTSYLAKRLQASGIKLRKVTVILDIVDEIA---KTVLDFSKeysIVFTSGGVGPTHDDVT 82
Cdd:PRK01215    4 WFAWIITIGNELLIGRTVNTNASWIARRLTYLGYTVRRITVVMDDIEEIVsafREAIDRAD---VVVSTGGLGPTYDDKT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2102663963  83 YEAIAKGLGLKLEQHEELVDIYLNLFPNHK----KEAQRLTIVPRPCELI---YVYSPKKYAIVKVKNIYMLPGSPKYFE 155
Cdd:PRK01215   81 NEGFAKALGVELELNEDALRMILEKYEKRGipltPERKKMAMMPPGAVPLenpVGTAPGILIEHGGKDIVALPGVPREME 160

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2102663963 156 LSIDTII-PQLKGNIPLYFEQIDINLN---ELSIVQILDEHAKLWkDKINIGSYPQ 207
Cdd:PRK01215  161 AIFENFVePLLKNRPPLKYYEDSILVEgvmESDLAPYVKELVKKY-DRVYVKSHPK 215
PRK03670 PRK03670
competence damage-inducible protein A; Provisional
 8-152 1.82e-22

competence damage-inducible protein A; Provisional


Pssm-ID: 167581  Cd Length: 252  Bit Score: 96.02  E-value: 1.82e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2102663963   8 AGLIVIGDEILRGQIIDTNTSYLAKRLQASGIKLRKVTVILDIVDEIAKTVLD-FSKEYSIVFTSGGVGPTHDDVTYEAI 86
Cdd:PRK03670    3 AEIITVGDELLTGNTVDSNSAFIAQKLTEKGYWVRRITTVGDDVEEIKSVVLEiLSRKPEVLVISGGLGPTHDDVTMLAV 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2102663963  87 AKGLGLKLEQHEELVD----IYLNLF-------PNHKKEAQRLTIVPR---PCELIYVYSPKKYAIVKVKNIYMLPGSPK 152
Cdd:PRK03670   83 AEALGRELVLCEDCLErikeFYEELYkkgliddPTLNEARKKMAYLPEgaePLENTEGAAPGAYIEHKGTKIFVLPGMPR 162
CysD COG0175
3'-phosphoadenosine 5'-phosphosulfate sulfotransferase (PAPS reductase)/FAD synthetase or ...
 270-431 6.59e-21

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: 91.06  E-value: 6.59e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2102663963 270 AVDILQQCYKMYkPEEIFISFNGGKDCTVVLHLAACITKlqNIssllclYVI-----AEpFPEVDSFVEKAVQYYDLELI 344
Cdd:COG0175    21 AIEILREAAAEF-GGRVVVSSSGGKDSTVLLHLAAKFKP--PI------PVLfldtgYE-FPETYEFRDRLAERLGLDLI 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2102663963 345 K------------------------------KKYPMRLALcsllnEKTNIKASLMGMRKGDPGS-ENLEAFTPtDPNwPN 393
Cdd:COG0175    91 VvrpedafaeqlaefgpplfyrdprwcckirKVEPLKRAL-----AGYDFDAWITGLRRDESPTrAKEPVVEW-DPV-GG 163

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 2102663963 394 LIRVNPILNWSYDQVWKFLLKHNVPYCPLYDKGYTSLG 431
Cdd:COG0175   164 LIKVNPLADWTELDVWAYIRREDLPYNPLYDQGYPSIG 201
molyb_syn TIGR00177
molybdenum cofactor synthesis domain; The Drosophila protein cinnamon, the Arabidopsis protein ...
 6-162 9.99e-21

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: 88.14  E-value: 9.99e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2102663963   6 YTAGLIVIGDEILRG-------QIIDTNTSYLAKRLQASGIKLRKVTVILDIVDEIAKTVLDFSKEYSIVFTSGGVGPTH 78
Cdd:TIGR00177   1 PRVAVISVGDELVEGgqplepgQIYDSNGPLLAALLQEAGFNVVRLGIVPDDPEEIREILRKAVDEADVVLTTGGTGVGP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2102663963  79 DDVTYEAIakglglkleqhEELVDIylnLFPNHKKEAQR--LTIVPRPCELIYVyspkkyAIVKVKNIYMLPGSPKYFEL 156
Cdd:TIGR00177  81 RDVTPEAL-----------EELGEK---EIPGFGEFRMLssLPVLSRPGKPATA------GVRGGTLIFNLPGNPVSALV 140


                  ....*.
gi 2102663963 157 SIDTII 162
Cdd:TIGR00177 141 TFEVLI 146
PRK00549 PRK00549
competence damage-inducible protein A; Provisional
 8-152 2.87e-19

competence damage-inducible protein A; Provisional


Pssm-ID: 234789 [Multi-domain]  Cd Length: 414  Bit Score: 89.46  E-value: 2.87e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2102663963   8 AGLIVIGDEILRGQIIDTNTSYLAKRLQASGIKLRKVTVILDIVDEIaKTVLDFSKEYS-IVFTSGGVGPTHDDVTYEAI 86
Cdd:PRK00549    3 AEIIAVGTELLLGQIVNTNAQFLSEKLAELGIDVYHQTVVGDNPERL-LSALEIAEERSdLIITTGGLGPTKDDLTKETV 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2102663963  87 AKGLGLKLEQHEEL---VDIYL-----NLFPNHKKEAQrltiVPRPCELIyvysPKKY-----AIVKVKN-IYM-LPGSP 151
Cdd:PRK00549   82 AKFLGRELVLDEEAlakIEDYFakrgrEMTENNRKQAL----IPEGATVL----PNPVgtapgMIIEVDGkTYIvLPGPP 153


                  .
gi 2102663963 152 K 152
Cdd:PRK00549  154 S 154
PAPS_reductase cd23945
Phosphoadenylyl-sulfate reductase (thioredoxin); Phosphoadenosine phosphosulfate (PAPS) ...
 283-431 8.35e-17

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: 78.02  E-value: 8.35e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2102663963 283 PEEIFISFNGGKDCTVVLHLAACITKLQNISSLLCLYViaepFPEVDSFVEKAVQYYDLELIKKKYPMRLAL-------- 354
Cdd:cd23945    13 GPKLVFATSFGAEDAVILDLLSKVRPDIPVVFLDTGYL----FPETYDLIDEVEARYGLNIEVYFPEGTEAEeealeggl 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2102663963 355 -------------CSL-------LNEKtNIKASLMGMRKGD-PGSENLEAFTPTDPNwpNLIRVNPILNWSYDQVWKFLL 413
Cdd:cd23945    89 nefyledeerydcCRKrkpfplaLALL-GVKAWITGRRRDQsPTRANLPIVEVDEEG--GLVKINPLADWTWEDVWAYIR 165

                         170
                  ....*....|....*...
gi 2102663963 414 KHNVPYCPLYDKGYTSLG 431
Cdd:cd23945   166 EHDLPYNPLHDQGYPSIG 183
cinA_nterm TIGR00200
competence/damage-inducible protein CinA N-terminal domain; cinA is a DNA damage- or ...
 8-166 2.81e-15

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: 77.64  E-value: 2.81e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2102663963   8 AGLIVIGDEILRGQIIDTNTSYLAKRLQASGIKLRKVTVILDIVDEIaKTVLDFSKEYS-IVFTSGGVGPTHDDVTYEAI 86
Cdd:TIGR00200   3 AEIISVGDELLLGQIVNTNAQWLADFLAHQGLPLSRRTTVGDNPERL-KTIIRIASERAdVLIFNGGLGPTSDDLTAETI 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2102663963  87 AKGLGLKLEQHEELVDIYLNLF--------PNHKKEAqrltIVPRPCELI---YVYSPKKYAiVKVKNIYML--PGSPKY 153
Cdd:TIGR00200  82 ATAKGEPLVLNEAWLKEIERYFhetgrvmaPNNRKQA----LLPAGAEFLanpVGTAPGMFA-VQLNRCLMLftPGVPSE 156

                         170
                  ....*....|....
gi 2102663963 154 FELSID-TIIPQLK 166
Cdd:TIGR00200 157 FRVMVEhEALPRLR 170
PAPS_reductase-like_YbdN cd23947
uncharacterized phosphoadenosine phosphosulfate reductase-like proteins, similar to ...
 284-431 8.13e-15

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: 73.19  E-value: 8.13e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2102663963 284 EEIFISFNGGKDCTVVLHLAA-CITKLQNIssllcLYVI-----AEpFPEVDSFVEKAVQYYDLELIKKKYPMRLALC-- 355
Cdd:cd23947    13 DPVIVSFSGGKDSLVLLHLALeALRRLRKD-----VYVVfidtgIE-FPETIDFVEKLAETLGLDVEAARPPLFLEWLts 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2102663963 356 --------------------------------SLLNEKTNIKASLM-GMRKGDpgSEN-------LEAFTPTDPNWPNLI 395
Cdd:cd23947    87 nfqpqwdpiwdnpppprdyrwccdelklepftKWLKEKKPEGVLLLvGIRADE--SLNrakrprvYRKYGWRNSTLPGQI 164

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 2102663963 396 RVNPILNWSYDQVWKFLLKHNVPYCPLYDKGYTSLG 431
Cdd:cd23947   165 VAYPIKDWSVEDVWLYILRHGLPYNPLYDLGFDRGG 200
PAPS_reductase TIGR02057
phosphoadenosine phosphosulfate reductase, thioredoxin dependent; Requiring thioredoxin as an ...
 333-438 1.07e-13

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: 70.25  E-value: 1.07e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2102663963 333 EKAVQYYDLelIKKKYPMRLALCSLlnektNIKASLMGMRKGDPGS-ENLEAFTPTDPNwpNLIRVNPILNWSYDQVWKF 411
Cdd:TIGR02057 106 QKDIEKYDY--IAKVEPMQRALKEL-----NASAWFTGRRRDQGSArANLPVIEIDEQN--GILKVNPLIDWTFEQVYQY 176

                          90       100
                  ....*....|....*....|....*..
gi 2102663963 412 LLKHNVPYCPLYDKGYTSLGTKSTTKP 438
Cdd:TIGR02057 177 LDAHNVPYNPLLDQGYRSIGDYHSTRK 203
MoCF_BD cd00758
MoCF_BD: molybdenum cofactor (MoCF) binding domain (BD). This domain is found a variety of ...
 8-165 3.51e-13

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: 66.21  E-value: 3.51e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2102663963   8 AGLIVIGDEILRGQIIDTNTSYLAKRLQASGIKLRKVTVILDIVDEIAKTVLDFSKEYSIVFTSGGVGPTHDDVTYEAIA 87
Cdd:cd00758     2 VAIVTVSDELSQGQIEDTNGPALEALLEDLGCEVIYAGVVPDDADSIRAALIEASREADLVLTTGGTGVGRRDVTPEALA 81

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2102663963  88 KgLGlkleqHEELVDIYLNLFPNhkkeaqrltivprpceliyvySPKKYAIVKVKNIYMLPGSPKY-FELSIDTIIPQL 165
Cdd:cd00758    82 E-LG-----EREAHGKGVALAPG---------------------SRTAFGIIGKVLIINLPGSPKSaLTTFEALVLPAL 133
MogA_MoaB cd00886
MogA_MoaB family. Members of this family are involved in biosynthesis of the molybdenum ...
 6-165 9.11e-13

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: 65.58  E-value: 9.11e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2102663963   6 YTAGLIVIGDEILRGQIIDTNTSYLAKRLQASGIKLRKVTVILDIVDEIAKTVLDFSKE--YSIVFTSGGVGPTHDDVTY 83
Cdd:cd00886     1 LRAAVLTVSDTRSAGEAEDRSGPALVELLEEAGHEVVAYEIVPDDKDEIREALIEWADEdgVDLILTTGGTGLAPRDVTP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2102663963  84 EAIakglglkleqhEELVDiylnlfpnhkKEaqrltiVPRPCELIYVYSpkkYAIVK----------VKN---IYMLPGS 150
Cdd:cd00886    81 EAT-----------RPLLD----------KE------LPGFGEAFRALS---LEETGtamlsravagIRGgtlIFNLPGS 130

                         170
                  ....*....|....*
gi 2102663963 151 PKYFELSIDTIIPQL 165
Cdd:cd00886   131 PKAVREALEVILPEL 145
PRK02090 PRK02090
phosphoadenylyl-sulfate reductase;
344-438 1.38e-12

phosphoadenylyl-sulfate reductase;


Pssm-ID: 234997  Cd Length: 241  Bit Score: 67.17  E-value: 1.38e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2102663963 344 IKKKYPMRLALCSLlnektniKASLMGMRKGDPGS-ENLEAFTPTDpnwpNLIRVNPILNWSYDQVWKFLLKHNVPYCPL 422
Cdd:PRK02090  129 IRKVEPLNRALAGL-------DAWITGLRREQSGTrANLPVLEIDG----GRFKINPLADWTNEDVWAYLKEHDLPYHPL 197

                          90
                  ....*....|....*.
gi 2102663963 423 YDKGYTSLGTKSTTKP 438
Cdd:PRK02090  198 VDQGYPSIGCEPCTRP 213
PRK03673 PRK03673
nicotinamide mononucleotide deamidase-related protein YfaY;
14-171 2.06e-12

nicotinamide mononucleotide deamidase-related protein YfaY;


Pssm-ID: 179629 [Multi-domain]  Cd Length: 396  Bit Score: 68.57  E-value: 2.06e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2102663963  14 GDEILRGQIIDTNTSYLAKRLQASGIKLRKVTVILDIVDEIAKTVLDFSKEYSIVFTSGGVGPTHDDVTYEAIAKGLGLK 93
Cdd:PRK03673   10 GDEVLHGQIVDTNAAWLADFFFHQGLPLSRRNTVGDNLDALVAILRERSQHADVLIVNGGLGPTSDDLSALAAATAAGEG 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2102663963  94 LEQHEELVDIYLNLF--------PNHKKEAQrltiVPRPCELIY--VYSPKKYAIvKVKNIYML--PGSPKYFELSI-DT 160
Cdd:PRK03673   90 LVLHEEWLAEMERFFaergrvmaPSNRKQAE----LPASAEMIDnpVGTACGFAL-QLNRCLMFftPGVPSEFKVMVeQE 164

                         170
                  ....*....|.
gi 2102663963 161 IIPQLKGNIPL 171
Cdd:PRK03673  165 ILPRLRERFSL 175
MoaB COG0521
Molybdopterin biosynthesis enzyme MoaB/MogA [Coenzyme transport and metabolism]; Molybdopterin ...
 7-165 5.70e-11

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: 60.90  E-value: 5.70e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2102663963   7 TAGLIVIGDEILRGQIIDTNTSYLAKRLQASGIKLRKVTVILDIVDEIAKTVLDF--SKEYSIVFTSGGVGPTHDDVTYE 84
Cdd:COG0521    11 RIAVLTVSDRRSRGEREDTSGPALVELLEEAGHEVVARRIVPDDKDAIRAALRELidDEGVDLVLTTGGTGLSPRDVTPE 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2102663963  85 AIakglglkleqhEELVDiylnlfpnhkKEaqrltiVPRPCELIYVYSPKKY--------AIVKVKN---IYMLPGSPKY 153
Cdd:COG0521    91 AT-----------RPLLD----------KE------LPGFGELFRALSLEEIgpsailsrAVAGIRGgtlIFNLPGSPGA 143

                         170
                  ....*....|..
gi 2102663963 154 FELSIDTIIPQL 165
Cdd:COG0521   144 VREALEAILPEL 155
PRK08557 PRK08557
hypothetical protein; Provisional
 241-431 4.36e-09

hypothetical protein; Provisional


Pssm-ID: 181465 [Multi-domain]  Cd Length: 417  Bit Score: 58.23  E-value: 4.36e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2102663963 241 KIRNL--KDGFSYYQAETVLKDAENEVHI--KYAVDILQQCYKMYKPE--EIFISFNGGKDCTVVLHLAACItklqnISS 314
Cdd:PRK08557  133 KIKDLslKKELDFEKIEDYLEKNKERIEKleENSLSILKDYIEKYKNKgyAINASFSGGKDSSVSTLLAKEV-----IPD 207

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2102663963 315 LLCLYV-IAEPFPEVDSFVEKAVQYYDLELI------------KKKYPMR-----LALCSLLNEKTNIKASLMGMRKGD- 375
Cdd:PRK08557  208 LEVIFIdTGLEYPETINYVKDFAKKYDLNLDtldgdnfwenleKEGIPTKdnrwcNSACKLMPLKEYLKKKYGNKKVLTi 287

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2102663963 376 PGSENLEAFTPTDPNW-------PNLIRVNPILNWSYDQVWKFLLKHNVPYCPLYDKGYTSLG 431
Cdd:PRK08557  288 DGSRKYESFTRANLDYerksgfiDFQTNVFPILDWNSLDIWSYIYLNDILYNPLYDKGFERIG 350
PRK13795 PRK13795
hypothetical protein; Provisional
 279-431 6.76e-09

hypothetical protein; Provisional


Pssm-ID: 237510 [Multi-domain]  Cd Length: 636  Bit Score: 58.08  E-value: 6.76e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2102663963 279 KMYKPeeIFISFNGGKDCTVVLHLAAcitklqniSSLLCLYVI-----AEpFPEVDSFVEKAVQYYDLELIKKKY----- 348
Cdd:PRK13795  241 KYNLP--VSVSFSGGKDSLVVLDLAR--------EALKDFKAFfnntgLE-FPETVENVKEVAEEYGIELIEADAgdafw 309

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2102663963 349 --------PMR----------LALCSLLNEKTNIKASLM--GMRKgdpgsenLEAFT-----PTDPN-W-PNLIRVNPIL 401
Cdd:PRK13795  310 ravekfgpPARdyrwcckvckLGPITRAIKENFPKGCLTfvGQRK-------YESFSrakspRVWRNpWvPNQIGASPIQ 382

                         170       180       190
                  ....*....|....*....|....*....|
gi 2102663963 402 NWSYDQVWKFLLKHNVPYCPLYDKGYTSLG 431
Cdd:PRK13795  383 DWTALEVWLYIFWRKLPYNPLYERGFDRIG 412
MoeA cd00887
MoeA family. Members of this family are involved in biosynthesis of the molybdenum cofactor ...
 9-88 1.17e-07

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: 53.65  E-value: 1.17e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2102663963   9 GLIVIGDEIL-------RGQIIDTNTSYLAKRLQASGIKLRKVTVILDIVDEIAKTVLDFSKEYSIVFTSGGVGPTHDDV 81
Cdd:cd00887   172 AIISTGDELVepgeplaPGQIYDSNSYMLAALLRELGAEVVDLGIVPDDPEALREALEEALEEADVVITSGGVSVGDYDF 251


                  ....*..
gi 2102663963  82 TYEAIAK 88
Cdd:cd00887   252 VKEVLEE 258
MoeA COG0303
Molybdopterin Mo-transferase (molybdopterin biosynthesis) [Coenzyme transport and metabolism]; ...
 4-94 2.86e-07

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: 52.40  E-value: 2.86e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2102663963   4 TVY---TAGLIVIGDEIL-------RGQIIDTNTSYLAKRLQASGIKLRKVTVILDIVDEIAKTVLDFSKEYSIVFTSGG 73
Cdd:COG0303   168 PVYrrpRVAILSTGDELVepgeplgPGQIYDSNSYMLAALLREAGAEVVDLGIVPDDPEALRAALREALAEADLVITSGG 247

                          90       100
                  ....*....|....*....|.
gi 2102663963  74 VGPTHDDVTYEAIAKgLGLKL 94
Cdd:COG0303   248 VSVGDYDLVKEALEE-LGAEV 267
moaC PRK03604
bifunctional molybdenum cofactor biosynthesis protein MoaC/MogA; Provisional
 8-87 7.12e-07

bifunctional molybdenum cofactor biosynthesis protein MoaC/MogA; Provisional


Pssm-ID: 235138 [Multi-domain]  Cd Length: 312  Bit Score: 50.71  E-value: 7.12e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2102663963   8 AGLIVIGDEILRGQIIDTNTSYLAKRLQASGIKLRKVTVILDIVDEIAKTVLDF-SKEYSIVFTSG--GVGPThdDVTYE 84
Cdd:PRK03604  158 AAVLVLSDSIAAGTKEDRSGKLIVEGLEEAGFEVSHYTIIPDEPAEIAAAVAAWiAEGYALIITTGgtGLGPR--DVTPE 235


                  ...
gi 2102663963  85 AIA 87
Cdd:PRK03604  236 ALA 238
APS_reduc TIGR00424
5'-adenylylsulfate reductase, thioredoxin-independent; This enzyme, involved in the ...
 344-438 1.44e-06

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: 50.40  E-value: 1.44e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2102663963 344 IKKKYPMRLALCSLlnektniKASLMGMRKG-DPGSENLEAFTPTDPNWP-------NLIRVNPILNWSYDQVWKFLLKH 415
Cdd:TIGR00424 203 VRKVRPLRRALKGL-------KAWITGQRKDqSPGTRSEIPVVQVDPVFEgldggvgSLVKWNPVANVEGKDVWNFLRTM 275

                          90       100
                  ....*....|....*....|...
gi 2102663963 416 NVPYCPLYDKGYTSLGTKSTTKP 438
Cdd:TIGR00424 276 DVPVNTLHAQGYVSIGCEPCTRP 298
PRK13794 PRK13794
hypothetical protein; Provisional
 283-431 1.67e-06

hypothetical protein; Provisional


Pssm-ID: 237509 [Multi-domain]  Cd Length: 479  Bit Score: 50.44  E-value: 1.67e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2102663963 283 PEEIFISFNGGKDCTVVLhlaacitklqnissLLCLYVIAEP-----------FPEVDSFVEKAVQYYDLELIK------ 345
Cdd:PRK13794  247 NKPVTVAYSGGKDSLATL--------------LLALKALGINfpvlfndtgleFPETLENVEDVEKHYGLEIIRtkseef 312

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2102663963 346 ----KKY--PMRLA-----LCSLLNEKTNIKA-------SLMGMRKGDPGSENLEAFTPTDPNWPNLIRVNPILNWSYDQ 407
Cdd:PRK13794  313 weklEEYgpPARDNrwcseVCKLEPLGKLIDEkyegeclSFVGQRKYESFNRSKKPRIWRNPYIKKQILAAPILHWTAMH 392

                         170       180
                  ....*....|....*....|....
gi 2102663963 408 VWKFLLKHNVPYCPLYDKGYTSLG 431
Cdd:PRK13794  393 VWIYLFREKAPYNKLYEQGFDRIG 416
Sulfate_adenylyltransferase_2 cd23946
Sulfate adenylyltransferase subunit 2; Sulfate adenylyltransferase subunits 1 and 2 form ATP ...
 258-423 8.11e-06

Sulfate adenylyltransferase subunit 2; Sulfate adenylyltransferase subunits 1 and 2 form ATP sulfurylase (ATPS) that catalyzes the adenylation of sulfate producing adenosine 5'-phosphosulfate (APS) and diphosphate, the first enzymatic step in the sulfur assimilation pathway. APS synthesis involves the formation of a high-energy phosphoric-sulfuric acid anhydride bond driven by GTP hydrolysis by CysN, coupled to ATP hydrolysis by CysD. CysD belongs to the ATP pyrophosphatase (ATP PPase) family of proteins, members of which include PAPS reductase, GMP synthetase, asparagine synthetase, and NAD(+) synthetase. This subunit is responsible for directly forming APS under control of the G protein. A modified version of the P loop (PP-loop), the fingerprint peptide of mononucleotide-binding proteins, is present in the active site of the protein, which appears to be a positively charged cleft containing a number of conserved arginine and lysine residues.


Pssm-ID: 467511  Cd Length: 214  Bit Score: 46.72  E-value: 8.11e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2102663963 258 LKDAENEvhikyAVDILQQCYKMYKPEEIFISFngGKDCTVVLHLAAcITKLQNISSLLCLYV-IAEPFPEVDSFVEKAV 336
Cdd:cd23946     2 LRQLEAE-----SIHIIREVAAEFSNPVMLYSI--GKDSSVMLHLAR-KAFYPGKPPFPLLHVdTTWKFREMIEFRDRVA 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2102663963 337 QYYDLELIKKKYPMRLAL------------CSLLN--------EKTNIKASLMGMRKGDPGS---ENLEAFTPTDPNW-- 391
Cdd:cd23946    74 KEYGLDLIVHVNPDGVEAginpfthgsakhTDIMKteglkqalDKYGFDAAFGGARRDEEKSrakERVYSFRDSNHRWdp 153

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 2102663963 392 ----PNL-------------IRVNPILNWSYDQVWKFLLKHNVPYCPLY 423
Cdd:cd23946   154 knqrPELwnqyngrvkkgesIRVFPLSNWTELDIWQYIYLENIPIVPLY 202
PLN02309 PLN02309
5'-adenylylsulfate reductase
 344-438 1.24e-05

5'-adenylylsulfate reductase


Pssm-ID: 215175 [Multi-domain]  Cd Length: 457  Bit Score: 47.48  E-value: 1.24e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2102663963 344 IKKKYPMRLALCSLlnektniKASLMGMRKGD-PGSENLEAFTPTDPNWP-------NLIRVNPILNWSYDQVWKFLLKH 415
Cdd:PLN02309  198 VRKVRPLRRALKGL-------RAWITGQRKDQsPGTRAEVPVVQVDPVFEgldggpgSLVKWNPLANVTGNEVWNFLRTM 270

                          90       100
                  ....*....|....*....|...
gi 2102663963 416 NVPYCPLYDKGYTSLGTKSTTKP 438
Cdd:PLN02309  271 DVPVNSLHAQGYVSIGCEPCTRP 293
PRK14498 PRK14498
putative molybdopterin biosynthesis protein MoeA/LysR substrate binding-domain-containing ...
 5-91 2.37e-05

putative molybdopterin biosynthesis protein MoeA/LysR substrate binding-domain-containing protein; Provisional


Pssm-ID: 237732 [Multi-domain]  Cd Length: 633  Bit Score: 46.75  E-value: 2.37e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2102663963   5 VY---TAGLIVIGDEILR-------GQIIDTNTSYLAKRLQASGIklrkVTVILDIV----DEIAKTVLDFSKEYSIVFT 70
Cdd:PRK14498  183 VYkkpRVGIISTGDELVEpgeplkpGKIYDVNSYTLAAAVEEAGG----EPVRYGIVpddeEELEAALRKALKECDLVLL 258

                          90       100
                  ....*....|....*....|....*
gi 2102663963  71 SG----GVGpthdDVTYEAIAKgLG 91
Cdd:PRK14498  259 SGgtsaGAG----DVTYRVIEE-LG 278
MoeA_like cd03522
MoeA_like. This domain is similar to a domain found in a variety of proteins involved in ...
 7-86 8.25e-04

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: 41.38  E-value: 8.25e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2102663963   7 TAGLIVIGDEILRGQIIDTNTSYLAKRLQASGIKLRKVTVILDIVDEIAKTVLDFSKEYS--IVFTSGG-VGPthDDVTY 83
Cdd:cd03522   161 RVGLIVTGSEVYGGRIEDKFGPVLRARLAALGVELVEQVIVPHDEAAIAAAIAEALEAGAelLILTGGAsVDP--DDVTP 238


                  ...
gi 2102663963  84 EAI 86
Cdd:cd03522   239 AAI 241
 
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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