|
Name |
Accession |
Description |
Interval |
E-value |
| FAD_synthase |
cd23948 |
FAD synthase; FAD synthase (FMN:ATP adenylyl transferase (FMNAT); FAD pyrophosphorylase; ... |
320-498 |
7.81e-109 |
|
FAD synthase; FAD synthase (FMN:ATP adenylyl transferase (FMNAT); FAD pyrophosphorylase; Flavin adenine dinucleotide synthase (FADS); EC 2.7.7.2) is involved in the biochemical pathway for converting riboflavin into FAD. By sequence comparison, bacterial and eukaryotic FMNAT enzymes belong to two different protein superfamilies and apparently utilize different sets of active-site residues to accomplish the same chemistry. This subfamily includes eukaryotic FMNATs, which are members of the 3'-phosphoadenosine 5'-phosphosulfate (PAPS) reductase-like family belonging to the adenine nucleotide alpha hydrolase superfamily, which has conserved motifs different from those of nucleotidylyl transferases.
Pssm-ID: 467513 [Multi-domain] Cd Length: 179 Bit Score: 321.78 E-value: 7.81e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782205059 320 KVANALKTIETALDQYSAGEICVGFNGGKDCTALLHLYYAALKRRYPEGKDKVKALYIRIVSPFPEMERFLQDTIKRYDL 399
Cdd:cd23948 1 KVKSALEVIEEALDKYGPEEIAISFNGGKDCTVLLHLLRAALKRKYPSPLTPLKALYIKSPDPFPEVEEFVEDTAKRYNL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782205059 400 EIFSVEGSIRQALSEVQERRPELRAVCMGTRRSDPYSHTLTPMCLTDPGWPDYMRVNPLLDWTYHDIWSFLRTLYVPYCI 479
Cdd:cd23948 81 DLITIDGPMKEGLEELLKEHPIIKAVFMGTRRTDPHGENLKPFSPTDPGWPQFMRVNPILDWSYHDVWEFLRTLNLPYCS 160
|
170
....*....|....*....
gi 1782205059 480 LYDKGYTSLGSMDNTCRNP 498
Cdd:cd23948 161 LYDQGYTSLGSVDNTLPNP 179
|
|
| cinA |
cd00885 |
Competence-damaged protein. CinA is the first gene in the competence- inducible (cin) operon ... |
48-215 |
7.90e-54 |
|
Competence-damaged protein. CinA is the first gene in the competence- inducible (cin) operon and is thought to be specifically required at some stage in the process of transformation. This domain is closely related to a domain, found in a variety of proteins involved in biosynthesis of molybdopterin cofactor, where the domain is presumed to bind molybdopterin.
Pssm-ID: 238450 [Multi-domain] Cd Length: 170 Bit Score: 179.22 E-value: 7.90e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782205059 48 TAAILIIGDEILKGHTVDTNSAFLLRALRKLGVCVQRVTVIPDQQEVISKEVALLAPQYTHLLTSGGIGPTHDDVTFEGV 127
Cdd:cd00885 1 TAEIIAIGDELLSGQIVDTNAAFLAKELAELGIEVYRVTVVGDDEDRIAEALRRASERADLVITTGGLGPTHDDLTREAV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782205059 128 AMAFEEELHAHPELTRLVEEFFGVVDREN--AAMKLAMVPRSAKL---NYGTdpqtgqplrYPLVSVR----NVYIFPGI 198
Cdd:cd00885 81 AKAFGRPLVLDEEALERIEARFARRGREMteANLKQAMLPEGATLlpnPVGT---------APGFSVEhngkNVFLLPGV 151
|
170
....*....|....*...
gi 1782205059 199 PSLLERAF-NGLEHLFAG 215
Cdd:cd00885 152 PSEMKPMLeEEVLPRLRE 169
|
|
| CinA |
COG1058 |
ADP-ribose pyrophosphatase domain of DNA damage- and competence-inducible protein CinA ... |
48-289 |
3.00e-52 |
|
ADP-ribose pyrophosphatase domain of DNA damage- and competence-inducible protein CinA [Replication, recombination and repair];
Pssm-ID: 440678 Cd Length: 249 Bit Score: 178.00 E-value: 3.00e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782205059 48 TAAILIIGDEILKGHTVDTNSAFLLRALRKLGVCVQRVTVIPDQQEVISKEVALLAPQYTHLLTSGGIGPTHDDVTFEGV 127
Cdd:COG1058 1 KAEIITIGDELLSGRIVDTNAAWLARELAELGIDVYRITTVGDDPERIVEALREALARADLVITTGGLGPTPDDLTREAV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782205059 128 AMAFEEELHAHPELTRLVEEFFGVVDRE--NAAMKLAMVPRSAKL---NYGTdpqtgqplrYPLVSVRN----VYIFPGI 198
Cdd:COG1058 81 AEALGVPLVLDPEALALIEERFAKRGREmtENNLKQALLPEGAELlpnPVGT---------APGFSIENngkvVIFLPGV 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782205059 199 PSLLERAF-NGLEHLFA--GSGTTFHTREV-FVDADEALIAPVLTRLQAGWgKRVALGSYPDwlSNYHRVRLVLDSDISE 274
Cdd:COG1058 152 PSEMKPMFeEEVLPRLKklFSGEPIVSRTLrTFGIGESDLAELLEDLEARF-PNVTIGSYPS--DGEVRLRLTARGTDEE 228
|
250
....*....|....*
gi 1782205059 275 EVEKARAQLLEEMPK 289
Cdd:COG1058 229 EAEAALEALEEELRE 243
|
|
| PAPS_reduct |
pfam01507 |
Phosphoadenosine phosphosulfate reductase family; This domain is found in phosphoadenosine ... |
339-494 |
8.48e-29 |
|
Phosphoadenosine phosphosulfate reductase family; This domain is found in phosphoadenosine phosphosulfate (PAPS) reductase enzymes or PAPS sulfotransferase. PAPS reductase is part of the adenine nucleotide alpha hydrolases superfamily also including N type ATP PPases and ATP sulphurylases. The enzyme uses thioredoxin as an electron donor for the reduction of PAPS to phospho-adenosine-phosphate (PAP). It is also found in NodP nodulation protein P from Rhizobium which has ATP sulfurylase activity (sulfate adenylate transferase).
Pssm-ID: 396201 [Multi-domain] Cd Length: 173 Bit Score: 112.00 E-value: 8.48e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782205059 339 EICVGFNGGKDCTALLHLyyaALKRRYPegkdkVKALYIRIVSPFPEMERFLQDTIKRYDLEI---------------FS 403
Cdd:pfam01507 1 ELVVSFSGGKDSLVLLHL---ASKAFPP-----GPVIFIDTGYEFPETYEFVDELEEKYGLNLkvylpedsfaeginpEG 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782205059 404 VEGSIRQALSEVQERRPELR--------AVCMGTRRSDPYSHTLTPMCLTDPGWPDYMRVNPLLDWTYHDIWSFLRTLYV 475
Cdd:pfam01507 73 IPSSLYRRCCRLRKVEPLKRalkelgfdAWFTGLRRDESPSRAKLPIVSIDGDFPKVIKVFPLLNWTETDVWQYILANNV 152
|
170
....*....|....*....
gi 1782205059 476 PYCILYDKGYTSLGSMDNT 494
Cdd:pfam01507 153 PYNPLYDQGYRSIGCYPCT 171
|
|
| PRK01215 |
PRK01215 |
nicotinamide mononucleotide deamidase-related protein; |
48-241 |
3.19e-26 |
|
nicotinamide mononucleotide deamidase-related protein;
Pssm-ID: 179250 [Multi-domain] Cd Length: 264 Bit Score: 107.79 E-value: 3.19e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782205059 48 TAAILIIGDEILKGHTVDTNSAFLLRALRKLGVCVQRVTVIPDQQEVISKEVALLAPQYTHLLTSGGIGPTHDDVTFEGV 127
Cdd:PRK01215 5 FAWIITIGNELLIGRTVNTNASWIARRLTYLGYTVRRITVVMDDIEEIVSAFREAIDRADVVVSTGGLGPTYDDKTNEGF 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782205059 128 AMAFEEELHAHPELTRLVEEFFgvvDRENAAM-----KLAMVPRSAKlnygtdpqtgqPLRYP-------LVSVRN--VY 193
Cdd:PRK01215 85 AKALGVELELNEDALRMILEKY---EKRGIPLtperkKMAMMPPGAV-----------PLENPvgtapgiLIEHGGkdIV 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1782205059 194 IFPGIPSLLERAF-NGLEHLFAGSGTTFHTREVFV--DADEALIAPVLTRL 241
Cdd:PRK01215 151 ALPGVPREMEAIFeNFVEPLLKNRPPLKYYEDSILveGVMESDLAPYVKEL 201
|
|
| MoCF_biosynth |
pfam00994 |
Probable molybdopterin binding domain; This domain is found a variety of proteins involved in ... |
50-150 |
1.61e-24 |
|
Probable molybdopterin binding domain; This domain is found a variety of proteins involved in biosynthesis of molybdopterin cofactor. The domain is presumed to bind molybdopterin. The structure of this domain is known, and it forms an alpha/beta structure. In the known structure of Gephyrin this domain mediates trimerization.
Pssm-ID: 425979 [Multi-domain] Cd Length: 143 Bit Score: 99.25 E-value: 1.61e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782205059 50 AILIIGDEILKGHTVDTNSAFLLRALRKLGVCVQRVTVIPDQQEVISKEVALLAPQYTHLLTSGGIGPTHDDVTFEGVAM 129
Cdd:pfam00994 1 AIITTGDELLPGQIRDTNGPLLAALLREAGAEVIRYGIVPDDPEAIKEALRAAAEEADVVITTGGTGPGPDDVTPEALAE 80
|
90 100
....*....|....*....|.
gi 1782205059 130 AFEEELHAHPELTRLVEEFFG 150
Cdd:pfam00994 81 LGGRELPGFEELFRGVSLKPG 101
|
|
| MoCF_biosynth |
smart00852 |
Probable molybdopterin binding domain; This domain is found a variety of proteins involved in ... |
50-209 |
1.80e-22 |
|
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: 93.04 E-value: 1.80e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782205059 50 AILIIGDEILKGHTVDTNSAFLLRA-LRKLGVCVQRVTVI--PDQQEVISKEVALLAPQYTHLLTSGGIGPTHDDVTFEG 126
Cdd:smart00852 1 AIISTGDELLSGGQIRDSNGPMLAAlLRELGIEVVRVVVVggPDDPEAIREALREALAEADVVITTGGTGPGPDDLTPEA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782205059 127 VAMAFEEELhahpeltrlveEFFGVvdrenaAMKLAMVPRSAKLNYGTDPqtGQPLRYPlvsvrnVYIFPGIPSLLERAF 206
Cdd:smart00852 81 LAELGGREL-----------LGHGV------AMRPGGPPGPLANLSGTAP--GVRGKKP------VFGLPGNPVAALVMF 135
|
...
gi 1782205059 207 NGL 209
Cdd:smart00852 136 EEL 138
|
|
| cinA_nterm |
TIGR00200 |
competence/damage-inducible protein CinA N-terminal domain; cinA is a DNA damage- or ... |
49-239 |
5.30e-16 |
|
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: 79.95 E-value: 5.30e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782205059 49 AAILIIGDEILKGHTVDTNSAFLLRALRKLGVCVQRVTVIPDQQEVISKEVALLAPQYTHLLTSGGIGPTHDDVTFEGVA 128
Cdd:TIGR00200 3 AEIISVGDELLLGQIVNTNAQWLADFLAHQGLPLSRRTTVGDNPERLKTIIRIASERADVLIFNGGLGPTSDDLTAETIA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782205059 129 MAFEEELHAHPELTRLVEEFFGVVDRENAA--MKLAMVPRSAKL---NYGTDPQ--TGQPLRYPLvsvrnvYIFPGIPSL 201
Cdd:TIGR00200 83 TAKGEPLVLNEAWLKEIERYFHETGRVMAPnnRKQALLPAGAEFlanPVGTAPGmfAVQLNRCLM------LFTPGVPSE 156
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1782205059 202 LERAFNG-----LEHLFAGSGTTFHTREVFVDADEALIAPVLT 239
Cdd:TIGR00200 157 FRVMVEHealprLRERFSLPQPIVSLVLRFFGIGESQLEADLA 199
|
|
| CysD |
COG0175 |
3'-phosphoadenosine 5'-phosphosulfate sulfotransferase (PAPS reductase)/FAD synthetase or ... |
322-489 |
1.42e-14 |
|
3'-phosphoadenosine 5'-phosphosulfate sulfotransferase (PAPS reductase)/FAD synthetase or related enzyme [Amino acid transport and metabolism, Coenzyme transport and metabolism]; 3'-phosphoadenosine 5'-phosphosulfate sulfotransferase (PAPS reductase)/FAD synthetase or related enzyme is part of the Pathway/BioSystem: Cysteine biosynthesis
Pssm-ID: 439945 [Multi-domain] Cd Length: 232 Bit Score: 73.34 E-value: 1.42e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782205059 322 ANALKTIETALDQYsAGEICVGFNGGKDCTALLHLyyaALKRrypegKDKVKALYI---RIvspFPEMERFLQDTIKRYD 398
Cdd:COG0175 19 AEAIEILREAAAEF-GGRVVVSSSGGKDSTVLLHL---AAKF-----KPPIPVLFLdtgYE---FPETYEFRDRLAERLG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782205059 399 LEI--FSVEGSIRQALSEVQERRPE-LRAVCMGTRRSDPYSHTLTPM----CLT------------------DPGwPDYM 453
Cdd:COG0175 87 LDLivVRPEDAFAEQLAEFGPPLFYrDPRWCCKIRKVEPLKRALAGYdfdaWITglrrdesptrakepvvewDPV-GGLI 165
|
170 180 190
....*....|....*....|....*....|....*.
gi 1782205059 454 RVNPLLDWTYHDIWSFLRTLYVPYCILYDKGYTSLG 489
Cdd:COG0175 166 KVNPLADWTELDVWAYIRREDLPYNPLYDQGYPSIG 201
|
|
| APS_reduc |
TIGR00424 |
5'-adenylylsulfate reductase, thioredoxin-independent; This enzyme, involved in the ... |
285-500 |
7.52e-13 |
|
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: 70.43 E-value: 7.52e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782205059 285 EEMPKGSVVPLVTDPVSIATEEVYTLVNSGTPLGDKVANA--LKTIETALDQYsAGEICVGFNGGKDcTALLHlyYAALK 362
Cdd:TIGR00424 62 EPKRNESIVPSAATTVAPEVEEKVVEVEDFEKLAKKLENAspLEIMDKALEKF-GNDIAIAFSGAED-VALIE--YAHLT 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782205059 363 ------------RRYPEGK---DKVKALY-IRIVSPFPEMERfLQDTIKRYDLEIFSVEGsiRQALSEVQERRP------ 420
Cdd:TIGR00424 138 grpfrvfsldtgRLNPETYrffDAVEKQYgIRIEYMFPDAVE-VQALVRSKGLFSFYEDG--HQECCRVRKVRPlrralk 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782205059 421 ELRAVCMGTRR-SDPYSHTLTPMCLTDP-------GWPDYMRVNPLLDWTYHDIWSFLRTLYVPYCILYDKGYTSLGSmd 492
Cdd:TIGR00424 215 GLKAWITGQRKdQSPGTRSEIPVVQVDPvfegldgGVGSLVKWNPVANVEGKDVWNFLRTMDVPVNTLHAQGYVSIGC-- 292
|
....*...
gi 1782205059 493 NTCRNPAL 500
Cdd:TIGR00424 293 EPCTRPVL 300
|
|
| PLN02309 |
PLN02309 |
5'-adenylylsulfate reductase |
279-500 |
4.64e-09 |
|
5'-adenylylsulfate reductase
Pssm-ID: 215175 [Multi-domain] Cd Length: 457 Bit Score: 58.65 E-value: 4.64e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782205059 279 ARAQLLEEMPKGSVVPLVTDPVSIATEEVYTLVNSGTpLGDKVANA--LKTIETALDQYSAGeICVGFNGGKDcTALLHl 356
Cdd:PLN02309 52 AKPLNAQPAARQAMIPSAATAVAEVPEEEGEVEDFEK-LAKELENAspLEIMDKALEKFGND-IAIAFSGAED-VALIE- 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782205059 357 yYAALKRRY------------PEGK---DKVKALY-IRIVSPFPEMERfLQDTIKRYDLEIFSVEGsiRQALSEVQERRP 420
Cdd:PLN02309 128 -YAHLTGRPfrvfsldtgrlnPETYrlfDAVEKHYgIRIEYMFPDAVE-VQALVRNKGLFSFYEDG--HQECCRVRKVRP 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782205059 421 ------ELRAVCMGTRRSD-PYSHTLTPMCLTDP-------GWPDYMRVNPLLDWTYHDIWSFLRTLYVPYCILYDKGYT 486
Cdd:PLN02309 204 lrralkGLRAWITGQRKDQsPGTRAEVPVVQVDPvfegldgGPGSLVKWNPLANVTGNEVWNFLRTMDVPVNSLHAQGYV 283
|
250
....*....|....
gi 1782205059 487 SLGSmdNTCRNPAL 500
Cdd:PLN02309 284 SIGC--EPCTRPVL 295
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| FAD_synthase |
cd23948 |
FAD synthase; FAD synthase (FMN:ATP adenylyl transferase (FMNAT); FAD pyrophosphorylase; ... |
320-498 |
7.81e-109 |
|
FAD synthase; FAD synthase (FMN:ATP adenylyl transferase (FMNAT); FAD pyrophosphorylase; Flavin adenine dinucleotide synthase (FADS); EC 2.7.7.2) is involved in the biochemical pathway for converting riboflavin into FAD. By sequence comparison, bacterial and eukaryotic FMNAT enzymes belong to two different protein superfamilies and apparently utilize different sets of active-site residues to accomplish the same chemistry. This subfamily includes eukaryotic FMNATs, which are members of the 3'-phosphoadenosine 5'-phosphosulfate (PAPS) reductase-like family belonging to the adenine nucleotide alpha hydrolase superfamily, which has conserved motifs different from those of nucleotidylyl transferases.
Pssm-ID: 467513 [Multi-domain] Cd Length: 179 Bit Score: 321.78 E-value: 7.81e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782205059 320 KVANALKTIETALDQYSAGEICVGFNGGKDCTALLHLYYAALKRRYPEGKDKVKALYIRIVSPFPEMERFLQDTIKRYDL 399
Cdd:cd23948 1 KVKSALEVIEEALDKYGPEEIAISFNGGKDCTVLLHLLRAALKRKYPSPLTPLKALYIKSPDPFPEVEEFVEDTAKRYNL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782205059 400 EIFSVEGSIRQALSEVQERRPELRAVCMGTRRSDPYSHTLTPMCLTDPGWPDYMRVNPLLDWTYHDIWSFLRTLYVPYCI 479
Cdd:cd23948 81 DLITIDGPMKEGLEELLKEHPIIKAVFMGTRRTDPHGENLKPFSPTDPGWPQFMRVNPILDWSYHDVWEFLRTLNLPYCS 160
|
170
....*....|....*....
gi 1782205059 480 LYDKGYTSLGSMDNTCRNP 498
Cdd:cd23948 161 LYDQGYTSLGSVDNTLPNP 179
|
|
| cinA |
cd00885 |
Competence-damaged protein. CinA is the first gene in the competence- inducible (cin) operon ... |
48-215 |
7.90e-54 |
|
Competence-damaged protein. CinA is the first gene in the competence- inducible (cin) operon and is thought to be specifically required at some stage in the process of transformation. This domain is closely related to a domain, found in a variety of proteins involved in biosynthesis of molybdopterin cofactor, where the domain is presumed to bind molybdopterin.
Pssm-ID: 238450 [Multi-domain] Cd Length: 170 Bit Score: 179.22 E-value: 7.90e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782205059 48 TAAILIIGDEILKGHTVDTNSAFLLRALRKLGVCVQRVTVIPDQQEVISKEVALLAPQYTHLLTSGGIGPTHDDVTFEGV 127
Cdd:cd00885 1 TAEIIAIGDELLSGQIVDTNAAFLAKELAELGIEVYRVTVVGDDEDRIAEALRRASERADLVITTGGLGPTHDDLTREAV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782205059 128 AMAFEEELHAHPELTRLVEEFFGVVDREN--AAMKLAMVPRSAKL---NYGTdpqtgqplrYPLVSVR----NVYIFPGI 198
Cdd:cd00885 81 AKAFGRPLVLDEEALERIEARFARRGREMteANLKQAMLPEGATLlpnPVGT---------APGFSVEhngkNVFLLPGV 151
|
170
....*....|....*...
gi 1782205059 199 PSLLERAF-NGLEHLFAG 215
Cdd:cd00885 152 PSEMKPMLeEEVLPRLRE 169
|
|
| CinA |
COG1058 |
ADP-ribose pyrophosphatase domain of DNA damage- and competence-inducible protein CinA ... |
48-289 |
3.00e-52 |
|
ADP-ribose pyrophosphatase domain of DNA damage- and competence-inducible protein CinA [Replication, recombination and repair];
Pssm-ID: 440678 Cd Length: 249 Bit Score: 178.00 E-value: 3.00e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782205059 48 TAAILIIGDEILKGHTVDTNSAFLLRALRKLGVCVQRVTVIPDQQEVISKEVALLAPQYTHLLTSGGIGPTHDDVTFEGV 127
Cdd:COG1058 1 KAEIITIGDELLSGRIVDTNAAWLARELAELGIDVYRITTVGDDPERIVEALREALARADLVITTGGLGPTPDDLTREAV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782205059 128 AMAFEEELHAHPELTRLVEEFFGVVDRE--NAAMKLAMVPRSAKL---NYGTdpqtgqplrYPLVSVRN----VYIFPGI 198
Cdd:COG1058 81 AEALGVPLVLDPEALALIEERFAKRGREmtENNLKQALLPEGAELlpnPVGT---------APGFSIENngkvVIFLPGV 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782205059 199 PSLLERAF-NGLEHLFA--GSGTTFHTREV-FVDADEALIAPVLTRLQAGWgKRVALGSYPDwlSNYHRVRLVLDSDISE 274
Cdd:COG1058 152 PSEMKPMFeEEVLPRLKklFSGEPIVSRTLrTFGIGESDLAELLEDLEARF-PNVTIGSYPS--DGEVRLRLTARGTDEE 228
|
250
....*....|....*
gi 1782205059 275 EVEKARAQLLEEMPK 289
Cdd:COG1058 229 EAEAALEALEEELRE 243
|
|
| PAPS_reduct |
pfam01507 |
Phosphoadenosine phosphosulfate reductase family; This domain is found in phosphoadenosine ... |
339-494 |
8.48e-29 |
|
Phosphoadenosine phosphosulfate reductase family; This domain is found in phosphoadenosine phosphosulfate (PAPS) reductase enzymes or PAPS sulfotransferase. PAPS reductase is part of the adenine nucleotide alpha hydrolases superfamily also including N type ATP PPases and ATP sulphurylases. The enzyme uses thioredoxin as an electron donor for the reduction of PAPS to phospho-adenosine-phosphate (PAP). It is also found in NodP nodulation protein P from Rhizobium which has ATP sulfurylase activity (sulfate adenylate transferase).
Pssm-ID: 396201 [Multi-domain] Cd Length: 173 Bit Score: 112.00 E-value: 8.48e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782205059 339 EICVGFNGGKDCTALLHLyyaALKRRYPegkdkVKALYIRIVSPFPEMERFLQDTIKRYDLEI---------------FS 403
Cdd:pfam01507 1 ELVVSFSGGKDSLVLLHL---ASKAFPP-----GPVIFIDTGYEFPETYEFVDELEEKYGLNLkvylpedsfaeginpEG 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782205059 404 VEGSIRQALSEVQERRPELR--------AVCMGTRRSDPYSHTLTPMCLTDPGWPDYMRVNPLLDWTYHDIWSFLRTLYV 475
Cdd:pfam01507 73 IPSSLYRRCCRLRKVEPLKRalkelgfdAWFTGLRRDESPSRAKLPIVSIDGDFPKVIKVFPLLNWTETDVWQYILANNV 152
|
170
....*....|....*....
gi 1782205059 476 PYCILYDKGYTSLGSMDNT 494
Cdd:pfam01507 153 PYNPLYDQGYRSIGCYPCT 171
|
|
| PRK01215 |
PRK01215 |
nicotinamide mononucleotide deamidase-related protein; |
48-241 |
3.19e-26 |
|
nicotinamide mononucleotide deamidase-related protein;
Pssm-ID: 179250 [Multi-domain] Cd Length: 264 Bit Score: 107.79 E-value: 3.19e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782205059 48 TAAILIIGDEILKGHTVDTNSAFLLRALRKLGVCVQRVTVIPDQQEVISKEVALLAPQYTHLLTSGGIGPTHDDVTFEGV 127
Cdd:PRK01215 5 FAWIITIGNELLIGRTVNTNASWIARRLTYLGYTVRRITVVMDDIEEIVSAFREAIDRADVVVSTGGLGPTYDDKTNEGF 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782205059 128 AMAFEEELHAHPELTRLVEEFFgvvDRENAAM-----KLAMVPRSAKlnygtdpqtgqPLRYP-------LVSVRN--VY 193
Cdd:PRK01215 85 AKALGVELELNEDALRMILEKY---EKRGIPLtperkKMAMMPPGAV-----------PLENPvgtapgiLIEHGGkdIV 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1782205059 194 IFPGIPSLLERAF-NGLEHLFAGSGTTFHTREVFV--DADEALIAPVLTRL 241
Cdd:PRK01215 151 ALPGVPREMEAIFeNFVEPLLKNRPPLKYYEDSILveGVMESDLAPYVKEL 201
|
|
| MoCF_biosynth |
pfam00994 |
Probable molybdopterin binding domain; This domain is found a variety of proteins involved in ... |
50-150 |
1.61e-24 |
|
Probable molybdopterin binding domain; This domain is found a variety of proteins involved in biosynthesis of molybdopterin cofactor. The domain is presumed to bind molybdopterin. The structure of this domain is known, and it forms an alpha/beta structure. In the known structure of Gephyrin this domain mediates trimerization.
Pssm-ID: 425979 [Multi-domain] Cd Length: 143 Bit Score: 99.25 E-value: 1.61e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782205059 50 AILIIGDEILKGHTVDTNSAFLLRALRKLGVCVQRVTVIPDQQEVISKEVALLAPQYTHLLTSGGIGPTHDDVTFEGVAM 129
Cdd:pfam00994 1 AIITTGDELLPGQIRDTNGPLLAALLREAGAEVIRYGIVPDDPEAIKEALRAAAEEADVVITTGGTGPGPDDVTPEALAE 80
|
90 100
....*....|....*....|.
gi 1782205059 130 AFEEELHAHPELTRLVEEFFG 150
Cdd:pfam00994 81 LGGRELPGFEELFRGVSLKPG 101
|
|
| MoCF_biosynth |
smart00852 |
Probable molybdopterin binding domain; This domain is found a variety of proteins involved in ... |
50-209 |
1.80e-22 |
|
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: 93.04 E-value: 1.80e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782205059 50 AILIIGDEILKGHTVDTNSAFLLRA-LRKLGVCVQRVTVI--PDQQEVISKEVALLAPQYTHLLTSGGIGPTHDDVTFEG 126
Cdd:smart00852 1 AIISTGDELLSGGQIRDSNGPMLAAlLRELGIEVVRVVVVggPDDPEAIREALREALAEADVVITTGGTGPGPDDLTPEA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782205059 127 VAMAFEEELhahpeltrlveEFFGVvdrenaAMKLAMVPRSAKLNYGTDPqtGQPLRYPlvsvrnVYIFPGIPSLLERAF 206
Cdd:smart00852 81 LAELGGREL-----------LGHGV------AMRPGGPPGPLANLSGTAP--GVRGKKP------VFGLPGNPVAALVMF 135
|
...
gi 1782205059 207 NGL 209
Cdd:smart00852 136 EEL 138
|
|
| PRK03670 |
PRK03670 |
competence damage-inducible protein A; Provisional |
49-285 |
3.20e-22 |
|
competence damage-inducible protein A; Provisional
Pssm-ID: 167581 Cd Length: 252 Bit Score: 96.02 E-value: 3.20e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782205059 49 AAILIIGDEILKGHTVDTNSAFLLRALRKLGVCVQRVTVIPDQQEVISKEV-ALLAPQYTHLLTSGGIGPTHDDVTFEGV 127
Cdd:PRK03670 3 AEIITVGDELLTGNTVDSNSAFIAQKLTEKGYWVRRITTVGDDVEEIKSVVlEILSRKPEVLVISGGLGPTHDDVTMLAV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782205059 128 AMAFEEELHAHPELTRLVEEFF------GVVDR---ENAAMKLAMVPRSAK-LNYGTDPQTGQPLRYPLVsvrNVYIFPG 197
Cdd:PRK03670 83 AEALGRELVLCEDCLERIKEFYeelykkGLIDDptlNEARKKMAYLPEGAEpLENTEGAAPGAYIEHKGT---KIFVLPG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782205059 198 IP----SLLERAFngLEHLfaGSGtTFHTREVFVD-ADEALIAPVLTrlQAGWGKRVALGSYPDWLSNYhrVRLVLDSDI 272
Cdd:PRK03670 160 MPremkAMLEKEV--LPRL--GER-KFVQKKFLAEiTDESKLAPILE--EALERFNVKIHSSPKGFGKY--IGIIIFAED 230
|
250
....*....|...
gi 1782205059 273 SEEVEKARAQLLE 285
Cdd:PRK03670 231 EEEIEKAVEFMEE 243
|
|
| PRK00549 |
PRK00549 |
competence damage-inducible protein A; Provisional |
49-207 |
1.53e-16 |
|
competence damage-inducible protein A; Provisional
Pssm-ID: 234789 [Multi-domain] Cd Length: 414 Bit Score: 81.76 E-value: 1.53e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782205059 49 AAILIIGDEILKGHTVDTNSAFLLRALRKLGVCVQRVTVIPDQQEVIsKEVALLAPQYTHLL-TSGGIGPTHDDVTFEGV 127
Cdd:PRK00549 3 AEIIAVGTELLLGQIVNTNAQFLSEKLAELGIDVYHQTVVGDNPERL-LSALEIAEERSDLIiTTGGLGPTKDDLTKETV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782205059 128 AMAFEEELHAHPELTRLVEEFFGVVDRENAA--MKLAMVPRSAKL---NYGTDPqtGQplrypLVSVRNV-YI-FPGIPS 200
Cdd:PRK00549 82 AKFLGRELVLDEEALAKIEDYFAKRGREMTEnnRKQALIPEGATVlpnPVGTAP--GM-----IIEVDGKtYIvLPGPPS 154
|
....*..
gi 1782205059 201 LLERAFN 207
Cdd:PRK00549 155 ELKPMFE 161
|
|
| cinA_nterm |
TIGR00200 |
competence/damage-inducible protein CinA N-terminal domain; cinA is a DNA damage- or ... |
49-239 |
5.30e-16 |
|
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: 79.95 E-value: 5.30e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782205059 49 AAILIIGDEILKGHTVDTNSAFLLRALRKLGVCVQRVTVIPDQQEVISKEVALLAPQYTHLLTSGGIGPTHDDVTFEGVA 128
Cdd:TIGR00200 3 AEIISVGDELLLGQIVNTNAQWLADFLAHQGLPLSRRTTVGDNPERLKTIIRIASERADVLIFNGGLGPTSDDLTAETIA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782205059 129 MAFEEELHAHPELTRLVEEFFGVVDRENAA--MKLAMVPRSAKL---NYGTDPQ--TGQPLRYPLvsvrnvYIFPGIPSL 201
Cdd:TIGR00200 83 TAKGEPLVLNEAWLKEIERYFHETGRVMAPnnRKQALLPAGAEFlanPVGTAPGmfAVQLNRCLM------LFTPGVPSE 156
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1782205059 202 LERAFNG-----LEHLFAGSGTTFHTREVFVDADEALIAPVLT 239
Cdd:TIGR00200 157 FRVMVEHealprLRERFSLPQPIVSLVLRFFGIGESQLEADLA 199
|
|
| PAPS_reductase-like_YbdN |
cd23947 |
uncharacterized phosphoadenosine phosphosulfate reductase-like proteins, similar to ... |
340-491 |
1.87e-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: 75.12 E-value: 1.87e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782205059 340 ICVGFNGGKDCTALLHLYYAALKRRypegKDKVKALYIRIVSPFPEMERFLQDTIKRYDLEIFSVEGSIRQALSEVQE-- 417
Cdd:cd23947 15 VIVSFSGGKDSLVLLHLALEALRRL----RKDVYVVFIDTGIEFPETIDFVEKLAETLGLDVEAARPPLFLEWLTSNFqp 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782205059 418 -------------------------------RRPELRAVCM--GTRRSDPYSHTLTPMCLTDPGW-----PDYMRVNPLL 459
Cdd:cd23947 91 qwdpiwdnpppprdyrwccdelklepftkwlKEKKPEGVLLlvGIRADESLNRAKRPRVYRKYGWrnstlPGQIVAYPIK 170
|
170 180 190
....*....|....*....|....*....|..
gi 1782205059 460 DWTYHDIWSFLRTLYVPYCILYDKGYTSLGSM 491
Cdd:cd23947 171 DWSVEDVWLYILRHGLPYNPLYDLGFDRGGCL 202
|
|
| CysD |
COG0175 |
3'-phosphoadenosine 5'-phosphosulfate sulfotransferase (PAPS reductase)/FAD synthetase or ... |
322-489 |
1.42e-14 |
|
3'-phosphoadenosine 5'-phosphosulfate sulfotransferase (PAPS reductase)/FAD synthetase or related enzyme [Amino acid transport and metabolism, Coenzyme transport and metabolism]; 3'-phosphoadenosine 5'-phosphosulfate sulfotransferase (PAPS reductase)/FAD synthetase or related enzyme is part of the Pathway/BioSystem: Cysteine biosynthesis
Pssm-ID: 439945 [Multi-domain] Cd Length: 232 Bit Score: 73.34 E-value: 1.42e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782205059 322 ANALKTIETALDQYsAGEICVGFNGGKDCTALLHLyyaALKRrypegKDKVKALYI---RIvspFPEMERFLQDTIKRYD 398
Cdd:COG0175 19 AEAIEILREAAAEF-GGRVVVSSSGGKDSTVLLHL---AAKF-----KPPIPVLFLdtgYE---FPETYEFRDRLAERLG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782205059 399 LEI--FSVEGSIRQALSEVQERRPE-LRAVCMGTRRSDPYSHTLTPM----CLT------------------DPGwPDYM 453
Cdd:COG0175 87 LDLivVRPEDAFAEQLAEFGPPLFYrDPRWCCKIRKVEPLKRALAGYdfdaWITglrrdesptrakepvvewDPV-GGLI 165
|
170 180 190
....*....|....*....|....*....|....*.
gi 1782205059 454 RVNPLLDWTYHDIWSFLRTLYVPYCILYDKGYTSLG 489
Cdd:COG0175 166 KVNPLADWTELDVWAYIRREDLPYNPLYDQGYPSIG 201
|
|
| molyb_syn |
TIGR00177 |
molybdenum cofactor synthesis domain; The Drosophila protein cinnamon, the Arabidopsis protein ... |
47-144 |
2.08e-13 |
|
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: 67.73 E-value: 2.08e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782205059 47 VTAAILIIGDEILKGHT-------VDTNSAFLLRALRKLGVCVQRVTVIPDQQEVISKEVALLAPQYTHLLTSGGIGPTH 119
Cdd:TIGR00177 1 PRVAVISVGDELVEGGQplepgqiYDSNGPLLAALLQEAGFNVVRLGIVPDDPEEIREILRKAVDEADVVLTTGGTGVGP 80
|
90 100
....*....|....*....|....*
gi 1782205059 120 DDVTFEGVAMAFEEELHAHPELTRL 144
Cdd:TIGR00177 81 RDVTPEALEELGEKEIPGFGEFRML 105
|
|
| APS_reduc |
TIGR00424 |
5'-adenylylsulfate reductase, thioredoxin-independent; This enzyme, involved in the ... |
285-500 |
7.52e-13 |
|
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: 70.43 E-value: 7.52e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782205059 285 EEMPKGSVVPLVTDPVSIATEEVYTLVNSGTPLGDKVANA--LKTIETALDQYsAGEICVGFNGGKDcTALLHlyYAALK 362
Cdd:TIGR00424 62 EPKRNESIVPSAATTVAPEVEEKVVEVEDFEKLAKKLENAspLEIMDKALEKF-GNDIAIAFSGAED-VALIE--YAHLT 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782205059 363 ------------RRYPEGK---DKVKALY-IRIVSPFPEMERfLQDTIKRYDLEIFSVEGsiRQALSEVQERRP------ 420
Cdd:TIGR00424 138 grpfrvfsldtgRLNPETYrffDAVEKQYgIRIEYMFPDAVE-VQALVRSKGLFSFYEDG--HQECCRVRKVRPlrralk 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782205059 421 ELRAVCMGTRR-SDPYSHTLTPMCLTDP-------GWPDYMRVNPLLDWTYHDIWSFLRTLYVPYCILYDKGYTSLGSmd 492
Cdd:TIGR00424 215 GLKAWITGQRKdQSPGTRSEIPVVQVDPvfegldgGVGSLVKWNPVANVEGKDVWNFLRTMDVPVNTLHAQGYVSIGC-- 292
|
....*...
gi 1782205059 493 NTCRNPAL 500
Cdd:TIGR00424 293 EPCTRPVL 300
|
|
| PAPS_reductase |
cd23945 |
Phosphoadenylyl-sulfate reductase (thioredoxin); Phosphoadenosine phosphosulfate (PAPS) ... |
383-489 |
1.93e-11 |
|
Phosphoadenylyl-sulfate reductase (thioredoxin); Phosphoadenosine phosphosulfate (PAPS) reductase (or PAPS sulfotransferase EC 1.8.4.8) is part of the adenine nucleotide alpha hydrolase superfamily that also includes N-type ATP PPases and ATP sulfurylases. A highly modified version of the P loop, the fingerprint peptide of mononucleotide-binding proteins, is present in the active site of the protein, which appears to be a positively charged cleft containing a number of conserved arginine and lysine residues. Although PAPS reductase has no ATPase activity, it shows a striking similarity to the structure of the ATP pyrophosphatase (ATP PPase) domain of GMP synthetase, indicating that both enzyme families have evolved from a common ancestral nucleotide-binding fold. The enzyme uses thioredoxin as an electron donor for the reduction of PAPS to phospho-adenosine-phosphate (PAP).
Pssm-ID: 467510 [Multi-domain] Cd Length: 183 Bit Score: 63.00 E-value: 1.93e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782205059 383 FPEMERFLQDTIKRYDLEIFSVEGSIRQALSEVQE-------------------RRPE--------LRAVCMGTRRSDPY 435
Cdd:cd23945 51 FPETYDLIDEVEARYGLNIEVYFPEGTEAEEEALEgglnefyledeerydccrkRKPFplalallgVKAWITGRRRDQSP 130
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 1782205059 436 SHTLTPMCLTDPGWPdYMRVNPLLDWTYHDIWSFLRTLYVPYCILYDKGYTSLG 489
Cdd:cd23945 131 TRANLPIVEVDEEGG-LVKINPLADWTWEDVWAYIREHDLPYNPLHDQGYPSIG 183
|
|
| MoCF_BD |
cd00758 |
MoCF_BD: molybdenum cofactor (MoCF) binding domain (BD). This domain is found a variety of ... |
49-138 |
2.41e-11 |
|
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: 61.21 E-value: 2.41e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782205059 49 AAILIIGDEILKGHTVDTNSAFLLRALRKLGVCVQRVTVIPDQQEVISKEVALLAPQYTHLLTSGGIGPTHDDVTFEGVA 128
Cdd:cd00758 2 VAIVTVSDELSQGQIEDTNGPALEALLEDLGCEVIYAGVVPDDADSIRAALIEASREADLVLTTGGTGVGRRDVTPEALA 81
|
90
....*....|
gi 1782205059 129 MAFEEELHAH 138
Cdd:cd00758 82 ELGEREAHGK 91
|
|
| PRK03673 |
PRK03673 |
nicotinamide mononucleotide deamidase-related protein YfaY; |
51-170 |
1.75e-10 |
|
nicotinamide mononucleotide deamidase-related protein YfaY;
Pssm-ID: 179629 [Multi-domain] Cd Length: 396 Bit Score: 62.79 E-value: 1.75e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782205059 51 ILIIGDEILKGHTVDTNSAFLLRALRKLGVCVQRVTVIPDQqevISKEVALLAPQYTH---LLTSGGIGPTHDDVTFEGV 127
Cdd:PRK03673 6 MLSTGDEVLHGQIVDTNAAWLADFFFHQGLPLSRRNTVGDN---LDALVAILRERSQHadvLIVNGGLGPTSDDLSALAA 82
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 1782205059 128 AMAFEEELHAHPELTRLVEEFFGVVDRENAA--MKLAMVPRSAKL 170
Cdd:PRK03673 83 ATAAGEGLVLHEEWLAEMERFFAERGRVMAPsnRKQAELPASAEM 127
|
|
| PLN02309 |
PLN02309 |
5'-adenylylsulfate reductase |
279-500 |
4.64e-09 |
|
5'-adenylylsulfate reductase
Pssm-ID: 215175 [Multi-domain] Cd Length: 457 Bit Score: 58.65 E-value: 4.64e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782205059 279 ARAQLLEEMPKGSVVPLVTDPVSIATEEVYTLVNSGTpLGDKVANA--LKTIETALDQYSAGeICVGFNGGKDcTALLHl 356
Cdd:PLN02309 52 AKPLNAQPAARQAMIPSAATAVAEVPEEEGEVEDFEK-LAKELENAspLEIMDKALEKFGND-IAIAFSGAED-VALIE- 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782205059 357 yYAALKRRY------------PEGK---DKVKALY-IRIVSPFPEMERfLQDTIKRYDLEIFSVEGsiRQALSEVQERRP 420
Cdd:PLN02309 128 -YAHLTGRPfrvfsldtgrlnPETYrlfDAVEKHYgIRIEYMFPDAVE-VQALVRNKGLFSFYEDG--HQECCRVRKVRP 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782205059 421 ------ELRAVCMGTRRSD-PYSHTLTPMCLTDP-------GWPDYMRVNPLLDWTYHDIWSFLRTLYVPYCILYDKGYT 486
Cdd:PLN02309 204 lrralkGLRAWITGQRKDQsPGTRAEVPVVQVDPvfegldgGPGSLVKWNPLANVTGNEVWNFLRTMDVPVNSLHAQGYV 283
|
250
....*....|....
gi 1782205059 487 SLGSmdNTCRNPAL 500
Cdd:PLN02309 284 SIGC--EPCTRPVL 295
|
|
| MoaB |
COG0521 |
Molybdopterin biosynthesis enzyme MoaB/MogA [Coenzyme transport and metabolism]; Molybdopterin ... |
46-145 |
1.13e-07 |
|
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: 51.66 E-value: 1.13e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782205059 46 AVTAAILIIGDEILKGHTVDTNSAFLLRALRKLGVCVQRVTVIPDQQEVISKEV-ALLAPQYTHL-LTSGGIGPTHDDVT 123
Cdd:COG0521 9 PLRIAVLTVSDRRSRGEREDTSGPALVELLEEAGHEVVARRIVPDDKDAIRAALrELIDDEGVDLvLTTGGTGLSPRDVT 88
|
90 100
....*....|....*....|..
gi 1782205059 124 FEGVAMAFEEELHAHPELTRLV 145
Cdd:COG0521 89 PEATRPLLDKELPGFGELFRAL 110
|
|
| MogA_MoaB |
cd00886 |
MogA_MoaB family. Members of this family are involved in biosynthesis of the molybdenum ... |
47-135 |
1.46e-07 |
|
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: 50.94 E-value: 1.46e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782205059 47 VTAAILIIGDEILKGHTVDTNSAFLLRALRKLGVCVQRVTVIPDQQEVISKEVALLAPQYTH--LLTSGGIGPTHDDVTF 124
Cdd:cd00886 1 LRAAVLTVSDTRSAGEAEDRSGPALVELLEEAGHEVVAYEIVPDDKDEIREALIEWADEDGVdlILTTGGTGLAPRDVTP 80
|
90
....*....|.
gi 1782205059 125 EGVAMAFEEEL 135
Cdd:cd00886 81 EATRPLLDKEL 91
|
|
| PRK02090 |
PRK02090 |
phosphoadenylyl-sulfate reductase; |
453-489 |
3.30e-07 |
|
phosphoadenylyl-sulfate reductase;
Pssm-ID: 234997 Cd Length: 241 Bit Score: 51.38 E-value: 3.30e-07
10 20 30
....*....|....*....|....*....|....*..
gi 1782205059 453 MRVNPLLDWTYHDIWSFLRTLYVPYCILYDKGYTSLG 489
Cdd:PRK02090 170 FKINPLADWTNEDVWAYLKEHDLPYHPLVDQGYPSIG 206
|
|
| moaC |
PRK03604 |
bifunctional molybdenum cofactor biosynthesis protein MoaC/MogA; Provisional |
46-136 |
1.00e-06 |
|
bifunctional molybdenum cofactor biosynthesis protein MoaC/MogA; Provisional
Pssm-ID: 235138 [Multi-domain] Cd Length: 312 Bit Score: 50.71 E-value: 1.00e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782205059 46 AVTAAILIIGDEILKGHTVDTNSAFLLRALRKLGVCVQRVTVIPDQQEVISKEV-ALLAPQYTHLLTSG--GIGPThdDV 122
Cdd:PRK03604 155 RTSAAVLVLSDSIAAGTKEDRSGKLIVEGLEEAGFEVSHYTIIPDEPAEIAAAVaAWIAEGYALIITTGgtGLGPR--DV 232
|
90
....*....|....
gi 1782205059 123 TFEGVAMAFEEELH 136
Cdd:PRK03604 233 TPEALAPLLERRLP 246
|
|
| PAPS_reductase |
TIGR02057 |
phosphoadenosine phosphosulfate reductase, thioredoxin dependent; Requiring thioredoxin as an ... |
391-489 |
1.53e-05 |
|
phosphoadenosine phosphosulfate reductase, thioredoxin dependent; Requiring thioredoxin as an electron donor, phosphoadenosine phosphosulfate reductase catalyzes the reduction of 3'-phosphoadenylylsulfate (PAPS) to sulfite and phospho-adenosine-phosphate (PAP). Found in enterobacteria, cyanobacteria, and yeast, PAPS reductase is related to a group of plant (TIGR00424) and bacterial (TIGR02055) enzymes preferring 5'-adenylylsulfate (APS) over PAPS as a substrate for reduction to sulfite. [Central intermediary metabolism, Sulfur metabolism]
Pssm-ID: 131112 Cd Length: 226 Bit Score: 46.37 E-value: 1.53e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782205059 391 QDTIKRYDlEIFSVEgSIRQALSEVqerrpELRAVCMGTRRSDPYSHTLTPMCLTDpGWPDYMRVNPLLDWTYHDIWSFL 470
Cdd:TIGR02057 106 QKDIEKYD-YIAKVE-PMQRALKEL-----NASAWFTGRRRDQGSARANLPVIEID-EQNGILKVNPLIDWTFEQVYQYL 177
|
90
....*....|....*....
gi 1782205059 471 RTLYVPYCILYDKGYTSLG 489
Cdd:TIGR02057 178 DAHNVPYNPLLDQGYRSIG 196
|
|
| MoeA |
COG0303 |
Molybdopterin Mo-transferase (molybdopterin biosynthesis) [Coenzyme transport and metabolism]; ... |
50-129 |
2.70e-05 |
|
Molybdopterin Mo-transferase (molybdopterin biosynthesis) [Coenzyme transport and metabolism]; Molybdopterin Mo-transferase (molybdopterin biosynthesis) is part of the Pathway/BioSystem: Molybdopterin biosynthesis
Pssm-ID: 440072 [Multi-domain] Cd Length: 401 Bit Score: 46.62 E-value: 2.70e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782205059 50 AILIIGDEIL-------KGHTVDTNSAFLLRALRKLGVCVQRVTVIPDQQEVISKEVALLAPQYTHLLTSGGIGP-THD- 120
Cdd:COG0303 176 AILSTGDELVepgeplgPGQIYDSNSYMLAALLREAGAEVVDLGIVPDDPEALRAALREALAEADLVITSGGVSVgDYDl 255
|
90
....*....|....*....
gi 1782205059 121 ----------DVTFEGVAM 129
Cdd:COG0303 256 vkealeelgaEVLFHKVAM 274
|
|
| MoeA |
cd00887 |
MoeA family. Members of this family are involved in biosynthesis of the molybdenum cofactor ... |
50-129 |
1.35e-04 |
|
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: 44.41 E-value: 1.35e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782205059 50 AILIIGDEIL-------KGHTVDTNSAFLLRALRKLGVCVQRVTVIPDQQEVISKEVALLAPQYTHLLTSGGIGP-THD- 120
Cdd:cd00887 172 AIISTGDELVepgeplaPGQIYDSNSYMLAALLRELGAEVVDLGIVPDDPEALREALEEALEEADVVITSGGVSVgDYDf 251
|
90
....*....|....*....
gi 1782205059 121 ----------DVTFEGVAM 129
Cdd:cd00887 252 vkevleelggEVLFHGVAM 270
|
|
| PRK08557 |
PRK08557 |
hypothetical protein; Provisional |
321-489 |
1.53e-04 |
|
hypothetical protein; Provisional
Pssm-ID: 181465 [Multi-domain] Cd Length: 417 Bit Score: 44.36 E-value: 1.53e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782205059 321 VANALKTIETALDQYSAG--EICVGFNGGKD---CTALLHlyyaalkrrypEGKDKVKALYIRIVSPFPEMERFLQDTIK 395
Cdd:PRK08557 163 EENSLSILKDYIEKYKNKgyAINASFSGGKDssvSTLLAK-----------EVIPDLEVIFIDTGLEYPETINYVKDFAK 231
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782205059 396 RYDLEIFSVEG---------------------SI--RQALSEVQERRPELRAVCM--GTRRSDPYSHTLTpmcltdpgwp 450
Cdd:PRK08557 232 KYDLNLDTLDGdnfwenlekegiptkdnrwcnSAckLMPLKEYLKKKYGNKKVLTidGSRKYESFTRANL---------- 301
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1782205059 451 DYMR----------VNPLLDWTYHDIWSFLRTLYVPYCILYDKGYTSLG 489
Cdd:PRK08557 302 DYERksgfidfqtnVFPILDWNSLDIWSYIYLNDILYNPLYDKGFERIG 350
|
|
| AANH-like |
cd01986 |
adenine nucleotide alpha hydrolase (AANH)-like proteins; This group of adenine nucleotide ... |
340-406 |
9.87e-04 |
|
adenine nucleotide alpha hydrolase (AANH)-like proteins; This group of adenine nucleotide alpha hydrolase (AANH)-like proteins includes N-type ATP PPases and ATP sulfurylases. The domain forms an alpha/beta/alpha fold which binds to adenosine nucleotide.
Pssm-ID: 467490 [Multi-domain] Cd Length: 74 Bit Score: 37.82 E-value: 9.87e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1782205059 340 ICVGFNGGKDCTALLHLYyaalkrRYPEGKDKVKALYIRIVSPFPEMERFLQDTIKRYDLEIFSVEG 406
Cdd:cd01986 1 VVVGYSGGKDSSVALHLA------SRLGRKAEVAVVHIDHGIGFKEEAESVASIARRSILKKLAEKG 61
|
|
| mogA |
PRK09417 |
molybdenum cofactor biosynthesis protein MogA; Provisional |
87-145 |
2.36e-03 |
|
molybdenum cofactor biosynthesis protein MogA; Provisional
Pssm-ID: 181837 [Multi-domain] Cd Length: 193 Bit Score: 39.17 E-value: 2.36e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1782205059 87 VIPDQQEVISKEVALLAPQY-THL-LTSGGIGPTHDDVTFEGVAMAFEEELHAHPELTRLV 145
Cdd:PRK09417 46 LIPDEQDLIEQTLIELVDEMgCDLvLTTGGTGPARRDVTPEATLAVADKEMPGFGEQMRQI 106
|
|
| |
