|
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
|
|
|