|
Name |
Accession |
Description |
Interval |
E-value |
| ribD |
PRK10786 |
bifunctional diaminohydroxyphosphoribosylaminopyrimidine deaminase/5-amino-6- ... |
6-368 |
7.44e-147 |
|
bifunctional diaminohydroxyphosphoribosylaminopyrimidine deaminase/5-amino-6-(5-phosphoribosylamino)uracil reductase RibD;
Pssm-ID: 182729 [Multi-domain] Cd Length: 367 Bit Score: 419.94 E-value: 7.44e-147
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233478 6 DRAMMARAVQLAWRGRYSTHPNPRVGCVIAKGDLIVGEGWHERAGEAHAEVRALSQAGHEARGATAYVTLEPCSHYGRTP 85
Cdd:PRK10786 3 DEFYMARALKLAQRGRFTTHPNPNVGCVIVKDGEIVGEGYHQRAGEPHAEVHALRMAGEKAKGATAYVTLEPCSHHGRTP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233478 86 PCARALIDAGVAHVFAATKDPNPSVSGRGLDMLREAGIRVTEGVMADEASRLNPGFMKRMNTGRPWVRLKMAASLDGRTA 165
Cdd:PRK10786 83 PCCDALIAAGVARVVAAMQDPNPQVAGRGLYRLQQAGIDVSHGLMMSEAEALNKGFLKRMRTGFPYIQLKLGASLDGRTA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233478 166 MASGESQWITGPEARADVQRLRAISDAILTGVGTVLADDPSLTVRRDEMGDIGDATDPS---RQPLRVIADRDARTPATA 242
Cdd:PRK10786 163 MASGESQWITSPQARRDVQRLRAQSHAILTSSATVLADDPALTVRWSELDAQTQALYPQenlRQPVRIVIDSQNRVTPEH 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233478 243 RILQGGnvqvfcASSTLASGPAQDLA-ALGVSLTGVAWKDNGVDVAELLDALGELGINELLVEAGPTLAGTFIGENLVDE 321
Cdd:PRK10786 243 RIVQQP------GETWLARTQEDSREwPETVRTLLLPEHNGHLDLVVLMMQLGKQQINSIWVEAGPTLAGALLQAGLVDE 316
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 504233478 322 LWLYQAPVFLGSTGRPTAHLP-LETMADKVQWKVLDRRQVGEDQRLIL 368
Cdd:PRK10786 317 LIVYIAPKLLGSDARGLCTLPgLEKLADAPQFKFSEIRHVGPDVCLHL 364
|
|
| eubact_ribD |
TIGR00326 |
riboflavin biosynthesis protein RibD; This model describes the ribD protein as found in ... |
10-367 |
1.57e-143 |
|
riboflavin biosynthesis protein RibD; This model describes the ribD protein as found in Escherichia coli. The N-terminal domain includes the conserved zinc-binding site region captured in the model dCMP_cyt_deam and shared by proteins such as cytosine deaminase, mammalian apolipoprotein B mRNA editing protein, blasticidin-S deaminase, and Bacillus subtilis competence protein comEB. The C-terminal domain is homologous to the full length of yeast HTP reductase, a protein required for riboflavin biosynthesis. A number of archaeal proteins believed related to riboflavin biosynthesis contain only this C-terminal domain and are not found as full-length matches to this model. [Biosynthesis of cofactors, prosthetic groups, and carriers, Riboflavin, FMN, and FAD]
Pssm-ID: 273015 [Multi-domain] Cd Length: 344 Bit Score: 410.37 E-value: 1.57e-143
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233478 10 MARAVQLAWRGRYSTHPNPRVGCVIAKGDLIVGEGWHERAGEAHAEVRALSQAGHEARGATAYVTLEPCSHYGRTPPCAR 89
Cdd:TIGR00326 1 MNRALDLAKKGQGTTHPNPLVGCVIVKNGEIVGEGAHQKAGEPHAEVHALRQAGENAKGATAYVTLEPCSHQGRTPPCAE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233478 90 ALIDAGVAHVFAATKDPNPSVSGRGLDMLREAGIRVTEGVMADEASRLNPGFMKRMNTGRPWVRLKMAASLDGRTAMASG 169
Cdd:TIGR00326 81 AIIEAGIKKVVVSMQDPNPLVAGRGAERLKQAGIEVTFGILKEEAERLNKGFLKRMRTGLPYVQLKLAASLDGKIATASG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233478 170 ESQWITGPEARADVQRLRAISDAILTGVGTVLADDPSLTVRRDEMgdigdatdpSRQPLRVIADRDARTPATARILQGgn 249
Cdd:TIGR00326 161 ESKWITSEAARTDAQQLRAQSDAILVGGGTVKADNPALTARLDEA---------TEQPLRVVLDTQLRIPEFAKLIPQ-- 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233478 250 vqvfcASSTLASGPAQDLAALGVSLTGVAWKDNGVDVAELLDALGELGINELLVEAGPTLAGTFIGENLVDELWLYQAPV 329
Cdd:TIGR00326 230 -----IAPTWIFTTARDKKKRLEAFEVNIFPLEKVTIREVMTQLGKRGINSVLVEGGPNLLGSFLDEGLVDELIIYIAPK 304
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 504233478 330 FLGSTGRPT--AHLPLETMADKVQWKVLDRRQVGEDQRLI 367
Cdd:TIGR00326 305 LLGGTHAPGlcSEPGFQKMADALNFKFLEINQIGPDILLT 344
|
|
| RibD1 |
COG0117 |
Riboflavin biosynthesis protein RibD, pyrimidine deaminase domain [Coenzyme transport and ... |
7-328 |
1.72e-135 |
|
Riboflavin biosynthesis protein RibD, pyrimidine deaminase domain [Coenzyme transport and metabolism]; Riboflavin biosynthesis protein RibD, pyrimidine deaminase domain is part of the Pathway/BioSystem: Riboflavin/FAD biosynthesis
Pssm-ID: 439887 [Multi-domain] Cd Length: 311 Bit Score: 388.65 E-value: 1.72e-135
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233478 7 RAMMARAVQLAWRGRYSTHPNPRVGCVIAKGDLIVGEGWHERAGEAHAEVRALSQAGHEARGATAYVTLEPCSHYGRTPP 86
Cdd:COG0117 1 ERYMRRALELARRGLGTTSPNPLVGCVIVKDGRIVGEGYHQRAGGPHAEVNALAQAGEAARGATLYVTLEPCSHHGRTPP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233478 87 CARALIDAGVAHVFAATKDPNPSVSGRGLDMLREAGIRVTEGVMADEASRLNPGFMKRMNTGRPWVRLKMAASLDGRTAM 166
Cdd:COG0117 81 CADALIEAGIKRVVIAMLDPNPLVAGKGIARLRAAGIEVEVGVLEEEARALNRGFLKRMRTGRPFVTLKLAMSLDGKIAT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233478 167 ASGESQWITGPEARADVQRLRAISDAILTGVGTVLADDPSLTVRRDEMGdigdatdpsRQPLRVIADRDARTPATARILQ 246
Cdd:COG0117 161 ANGESQWITGEEARADVHRLRARSDAILVGIGTVLADDPSLTVRLPGGE---------NPPRRVVVDDLLLRPPPALLLV 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233478 247 GGNVQVFCAssTLASGPAQDLAALGVSLTGVAWKDNGVDVAELLDALGELGINELLVEAGPTLAGTFIGENLVDELWLYQ 326
Cdd:COG0117 232 ANDAALIIV--TVTADAAAALAALAAEAGVVLLLVGGLLLLALLLLLLLLLLLLLLLLLLLGGGGGLAAAALLAALLLDL 309
|
..
gi 504233478 327 AP 328
Cdd:COG0117 310 LL 311
|
|
| Riboflavin_deaminase-reductase |
cd01284 |
Riboflavin-specific deaminase. Riboflavin biosynthesis protein RibD ... |
10-122 |
1.23e-54 |
|
Riboflavin-specific deaminase. Riboflavin biosynthesis protein RibD (Diaminohydroxyphosphoribosylaminopyrimidine deaminase) catalyzes the deamination of 2,5-diamino-6-ribosylamino-4(3H)-pyrimidinone 5'-phosphate, which is an intermediate step in the biosynthesis of riboflavin.The ribG gene of Bacillus subtilis and the ribD gene of E. coli are bifunctional and contain this deaminase domain and a reductase domain which catalyzes the subsequent reduction of the ribosyl side chain.
Pssm-ID: 238611 [Multi-domain] Cd Length: 115 Bit Score: 175.50 E-value: 1.23e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233478 10 MARAVQLAWRGRYSTHPNPRVGCVIAKGD-LIVGEGWHERAGEAHAEVRALSQAGHE-ARGATAYVTLEPCSHYGRTPPC 87
Cdd:cd01284 1 MRRALELAEKGRGLTSPNPPVGCVIVDDDgEIVGEGYHRKAGGPHAEVNALASAGEKlARGATLYVTLEPCSHHGKTPPC 80
|
90 100 110
....*....|....*....|....*....|....*
gi 504233478 88 ARALIDAGVAHVFAATKDPNPSVSGRGLDMLREAG 122
Cdd:cd01284 81 VDAIIEAGIKRVVVGVRDPNPLVAGKGAERLRAAG 115
|
|
| RibD_C |
pfam01872 |
RibD C-terminal domain; The function of this domain is not known, but it is thought to be ... |
150-363 |
4.45e-52 |
|
RibD C-terminal domain; The function of this domain is not known, but it is thought to be involved in riboflavin biosynthesis. This domain is found in the C terminus of RibD/RibG, in combination with pfam00383, as well as in isolation in some archaebacterial proteins. This family appears to be related to pfam00186.
Pssm-ID: 396444 Cd Length: 196 Bit Score: 171.79 E-value: 4.45e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233478 150 PWVRLKMAASLDGRTAMASGESQWITGPEARADVQRLRAISDAILTGVGTVLADDPSLTVRRdemgdiGDATDPSRQPLR 229
Cdd:pfam01872 1 PYVILKFAISLDGKIAAAGGSSQWITGEEARADVHQLRAEADAILVGRGTVRADNPSLTVRW------VKGRAAERQPPR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233478 230 VIADRDARTPATARILQGGNVQVFCASSTLASGPAQDLAALgvsltgvawkdnGVDVAELLDALGELGINELLVEAGPTL 309
Cdd:pfam01872 75 VVVDSTLRVPLDARVLNDDAPTLVATTEPADKEKVEKLKVL------------RVDLKELLRELKERGIRSLLVEGGATL 142
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 504233478 310 AGTFIGENLVDELWLYQAPVFLGSTGRPtahLPLETMADKVQWKVLDRRQVGED 363
Cdd:pfam01872 143 AGSLLRAGLVDELRLYIAPKLLGGGGRT---LFGGEGFLALKLKLVSSEAIGNG 193
|
|
|
|
Name |
Accession |
Description |
Interval |
E-value |
| ribD |
PRK10786 |
bifunctional diaminohydroxyphosphoribosylaminopyrimidine deaminase/5-amino-6- ... |
6-368 |
7.44e-147 |
|
bifunctional diaminohydroxyphosphoribosylaminopyrimidine deaminase/5-amino-6-(5-phosphoribosylamino)uracil reductase RibD;
Pssm-ID: 182729 [Multi-domain] Cd Length: 367 Bit Score: 419.94 E-value: 7.44e-147
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233478 6 DRAMMARAVQLAWRGRYSTHPNPRVGCVIAKGDLIVGEGWHERAGEAHAEVRALSQAGHEARGATAYVTLEPCSHYGRTP 85
Cdd:PRK10786 3 DEFYMARALKLAQRGRFTTHPNPNVGCVIVKDGEIVGEGYHQRAGEPHAEVHALRMAGEKAKGATAYVTLEPCSHHGRTP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233478 86 PCARALIDAGVAHVFAATKDPNPSVSGRGLDMLREAGIRVTEGVMADEASRLNPGFMKRMNTGRPWVRLKMAASLDGRTA 165
Cdd:PRK10786 83 PCCDALIAAGVARVVAAMQDPNPQVAGRGLYRLQQAGIDVSHGLMMSEAEALNKGFLKRMRTGFPYIQLKLGASLDGRTA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233478 166 MASGESQWITGPEARADVQRLRAISDAILTGVGTVLADDPSLTVRRDEMGDIGDATDPS---RQPLRVIADRDARTPATA 242
Cdd:PRK10786 163 MASGESQWITSPQARRDVQRLRAQSHAILTSSATVLADDPALTVRWSELDAQTQALYPQenlRQPVRIVIDSQNRVTPEH 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233478 243 RILQGGnvqvfcASSTLASGPAQDLA-ALGVSLTGVAWKDNGVDVAELLDALGELGINELLVEAGPTLAGTFIGENLVDE 321
Cdd:PRK10786 243 RIVQQP------GETWLARTQEDSREwPETVRTLLLPEHNGHLDLVVLMMQLGKQQINSIWVEAGPTLAGALLQAGLVDE 316
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 504233478 322 LWLYQAPVFLGSTGRPTAHLP-LETMADKVQWKVLDRRQVGEDQRLIL 368
Cdd:PRK10786 317 LIVYIAPKLLGSDARGLCTLPgLEKLADAPQFKFSEIRHVGPDVCLHL 364
|
|
| eubact_ribD |
TIGR00326 |
riboflavin biosynthesis protein RibD; This model describes the ribD protein as found in ... |
10-367 |
1.57e-143 |
|
riboflavin biosynthesis protein RibD; This model describes the ribD protein as found in Escherichia coli. The N-terminal domain includes the conserved zinc-binding site region captured in the model dCMP_cyt_deam and shared by proteins such as cytosine deaminase, mammalian apolipoprotein B mRNA editing protein, blasticidin-S deaminase, and Bacillus subtilis competence protein comEB. The C-terminal domain is homologous to the full length of yeast HTP reductase, a protein required for riboflavin biosynthesis. A number of archaeal proteins believed related to riboflavin biosynthesis contain only this C-terminal domain and are not found as full-length matches to this model. [Biosynthesis of cofactors, prosthetic groups, and carriers, Riboflavin, FMN, and FAD]
Pssm-ID: 273015 [Multi-domain] Cd Length: 344 Bit Score: 410.37 E-value: 1.57e-143
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233478 10 MARAVQLAWRGRYSTHPNPRVGCVIAKGDLIVGEGWHERAGEAHAEVRALSQAGHEARGATAYVTLEPCSHYGRTPPCAR 89
Cdd:TIGR00326 1 MNRALDLAKKGQGTTHPNPLVGCVIVKNGEIVGEGAHQKAGEPHAEVHALRQAGENAKGATAYVTLEPCSHQGRTPPCAE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233478 90 ALIDAGVAHVFAATKDPNPSVSGRGLDMLREAGIRVTEGVMADEASRLNPGFMKRMNTGRPWVRLKMAASLDGRTAMASG 169
Cdd:TIGR00326 81 AIIEAGIKKVVVSMQDPNPLVAGRGAERLKQAGIEVTFGILKEEAERLNKGFLKRMRTGLPYVQLKLAASLDGKIATASG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233478 170 ESQWITGPEARADVQRLRAISDAILTGVGTVLADDPSLTVRRDEMgdigdatdpSRQPLRVIADRDARTPATARILQGgn 249
Cdd:TIGR00326 161 ESKWITSEAARTDAQQLRAQSDAILVGGGTVKADNPALTARLDEA---------TEQPLRVVLDTQLRIPEFAKLIPQ-- 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233478 250 vqvfcASSTLASGPAQDLAALGVSLTGVAWKDNGVDVAELLDALGELGINELLVEAGPTLAGTFIGENLVDELWLYQAPV 329
Cdd:TIGR00326 230 -----IAPTWIFTTARDKKKRLEAFEVNIFPLEKVTIREVMTQLGKRGINSVLVEGGPNLLGSFLDEGLVDELIIYIAPK 304
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 504233478 330 FLGSTGRPT--AHLPLETMADKVQWKVLDRRQVGEDQRLI 367
Cdd:TIGR00326 305 LLGGTHAPGlcSEPGFQKMADALNFKFLEINQIGPDILLT 344
|
|
| RibD1 |
COG0117 |
Riboflavin biosynthesis protein RibD, pyrimidine deaminase domain [Coenzyme transport and ... |
7-328 |
1.72e-135 |
|
Riboflavin biosynthesis protein RibD, pyrimidine deaminase domain [Coenzyme transport and metabolism]; Riboflavin biosynthesis protein RibD, pyrimidine deaminase domain is part of the Pathway/BioSystem: Riboflavin/FAD biosynthesis
Pssm-ID: 439887 [Multi-domain] Cd Length: 311 Bit Score: 388.65 E-value: 1.72e-135
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233478 7 RAMMARAVQLAWRGRYSTHPNPRVGCVIAKGDLIVGEGWHERAGEAHAEVRALSQAGHEARGATAYVTLEPCSHYGRTPP 86
Cdd:COG0117 1 ERYMRRALELARRGLGTTSPNPLVGCVIVKDGRIVGEGYHQRAGGPHAEVNALAQAGEAARGATLYVTLEPCSHHGRTPP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233478 87 CARALIDAGVAHVFAATKDPNPSVSGRGLDMLREAGIRVTEGVMADEASRLNPGFMKRMNTGRPWVRLKMAASLDGRTAM 166
Cdd:COG0117 81 CADALIEAGIKRVVIAMLDPNPLVAGKGIARLRAAGIEVEVGVLEEEARALNRGFLKRMRTGRPFVTLKLAMSLDGKIAT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233478 167 ASGESQWITGPEARADVQRLRAISDAILTGVGTVLADDPSLTVRRDEMGdigdatdpsRQPLRVIADRDARTPATARILQ 246
Cdd:COG0117 161 ANGESQWITGEEARADVHRLRARSDAILVGIGTVLADDPSLTVRLPGGE---------NPPRRVVVDDLLLRPPPALLLV 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233478 247 GGNVQVFCAssTLASGPAQDLAALGVSLTGVAWKDNGVDVAELLDALGELGINELLVEAGPTLAGTFIGENLVDELWLYQ 326
Cdd:COG0117 232 ANDAALIIV--TVTADAAAALAALAAEAGVVLLLVGGLLLLALLLLLLLLLLLLLLLLLLLGGGGGLAAAALLAALLLDL 309
|
..
gi 504233478 327 AP 328
Cdd:COG0117 310 LL 311
|
|
| RibD |
COG1985 |
Pyrimidine reductase, riboflavin biosynthesis [Coenzyme transport and metabolism]; Pyrimidine ... |
147-371 |
3.34e-86 |
|
Pyrimidine reductase, riboflavin biosynthesis [Coenzyme transport and metabolism]; Pyrimidine reductase, riboflavin biosynthesis is part of the Pathway/BioSystem: Riboflavin/FAD biosynthesis
Pssm-ID: 441588 Cd Length: 217 Bit Score: 259.71 E-value: 3.34e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233478 147 TGRPWVRLKMAASLDGRTAMASGESQWITGPEARADVQRLRAISDAILTGVGTVLADDPSLTVRRDEMGdigdatdpsRQ 226
Cdd:COG1985 1 TGRPYVTLKLAMSLDGKIATADGESKWITGEAARRDVHRLRARADAILVGAGTVLADDPSLTVRLPGLG---------RQ 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233478 227 PLRVIADRDARTPATARILQ-GGNVQVFCASSTlASGPAQDLAALGVSLTgVAWKDNGVDVAELLDALGELGINELLVEA 305
Cdd:COG1985 72 PLRVVVDSSLRLPPDARLFDdAAPTLVLTTEAA-DAERRAALEAAGAEVI-VLPGDGRVDLAALLAALAERGIRSVLVEG 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 504233478 306 GPTLAGTFIGENLVDELWLYQAPVFLGSTGRPTAHLP-LETMADKVQWKVLDRRQVGEDQRLILARH 371
Cdd:COG1985 150 GPTLAGSFLAAGLVDELILYIAPKLLGGDGPTLVGGPgLETLADAPRLRLVSVRRLGDDLLLRYRPR 216
|
|
| PLN02807 |
PLN02807 |
diaminohydroxyphosphoribosylaminopyrimidine deaminase |
4-363 |
6.68e-65 |
|
diaminohydroxyphosphoribosylaminopyrimidine deaminase
Pssm-ID: 215433 [Multi-domain] Cd Length: 380 Bit Score: 210.78 E-value: 6.68e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233478 4 DRDRAMMARAVQLAWRGRYSTHPNPRVGCVIAKGDLIVGEGWHERAGEAHAEVRALSQAGHEARGATAYVTLEPCSHYGR 83
Cdd:PLN02807 30 DDDSFYMRRCVELARKAIGCTSPNPMVGCVIVKDGRIVGEGFHPKAGQPHAEVFALRDAGDLAENATAYVSLEPCNHYGR 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233478 84 TPPCARALIDAGVAHVFAATKDPNPSVSGRGLDMLREAGIRVTEGVMADEASRLNPGFMKRMNTGRPWVRLKMAASLDGR 163
Cdd:PLN02807 110 TPPCTEALIKAKVKRVVVGMVDPNPIVASKGIERLRDAGIEVTVGVEEELCRKLNEAFIHRMLTGKPFVTLRYSMSMNGC 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233478 164 TAMASGESqwitGPEARADVQRLRAISDAILTGvGTVLADDPSLTVRrdEMGdigdatdpSRQPLRVIADRDARTPATAR 243
Cdd:PLN02807 190 LLNQIGEG----ADDAGGYYSQLLQEYDAVILS-SALADADPLPLSQ--EAG--------AKQPLRIIIARSESSPLQIP 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233478 244 IL---QGGNVQVFCASSTLAsgpAQDLAALGVSLTGVawkdNGVDVAELLDALGELGINELLVEA-GPT-----LAGTFI 314
Cdd:PLN02807 255 SLreeSAAKVLVLADKESSA---EPVLRRKGVEVVVL----NQINLDSILDLCYQRGLCSVLLDLrGNVgglesLLKDAL 327
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 504233478 315 GENLVDELWLYQAPVFLGSTGRPTAhlpLETMADKVQWKVLDRRQVGED 363
Cdd:PLN02807 328 EDKLLQKVVVEVLPFWSGSQGQSIA---SFGGSQSFKLKRLTSREVGGS 373
|
|
| ribD_Cterm |
TIGR00227 |
riboflavin-specific deaminase C-terminal domain; Eubacterial riboflavin-specific deaminases ... |
148-363 |
1.23e-63 |
|
riboflavin-specific deaminase C-terminal domain; Eubacterial riboflavin-specific deaminases have a zinc-binding domain recognized by the dCMP_cyt_deam model toward the N-terminus and this domain toward the C-terminus. Yeast HTP reductase, a riboflavin-biosynthetic enzyme, and several archaeal proteins believed related to riboflavin biosynthesis consist only of this domain and lack the dCMP_cyt_deam domain.
Pssm-ID: 129330 [Multi-domain] Cd Length: 216 Bit Score: 202.23 E-value: 1.23e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233478 148 GRPWVRLKMAASLDGRTAMASGESQWITGPEARADVQRLRAISDAILTGVGTVLADDPSLTVRRDEMgdigdatDPSRQP 227
Cdd:TIGR00227 1 GRPYVILKYAMSLDGKIATASGESSWITSEEARRDVHQLRAQSDAILVGSGTVLADDPRLTVRWVEL-------DELRNP 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233478 228 LRVIADRDARTPATARILQGGNVQVFCASSTLASGPAQDLAALGVSLtgVAWKDNGVDVAELLDALGELGINELLVEAGP 307
Cdd:TIGR00227 74 VRVVLDSRLRVPPTARLLNDDAPTWVATSEPADEEKVKELEDFGVEV--LVLETKRVDLKKLMEILYEEGIRSVMVEGGG 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 504233478 308 TLAGTFIGENLVDELWLYQAPVFLGSTGRPT--AHLPLETMADKVQWKVLDRRQVGED 363
Cdd:TIGR00227 152 TLNGSLLKEGLVDELIVYIAPKLLGGRDAPTlvDGEGFQKMADAPNLELKEIYQIGED 209
|
|
| Riboflavin_deaminase-reductase |
cd01284 |
Riboflavin-specific deaminase. Riboflavin biosynthesis protein RibD ... |
10-122 |
1.23e-54 |
|
Riboflavin-specific deaminase. Riboflavin biosynthesis protein RibD (Diaminohydroxyphosphoribosylaminopyrimidine deaminase) catalyzes the deamination of 2,5-diamino-6-ribosylamino-4(3H)-pyrimidinone 5'-phosphate, which is an intermediate step in the biosynthesis of riboflavin.The ribG gene of Bacillus subtilis and the ribD gene of E. coli are bifunctional and contain this deaminase domain and a reductase domain which catalyzes the subsequent reduction of the ribosyl side chain.
Pssm-ID: 238611 [Multi-domain] Cd Length: 115 Bit Score: 175.50 E-value: 1.23e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233478 10 MARAVQLAWRGRYSTHPNPRVGCVIAKGD-LIVGEGWHERAGEAHAEVRALSQAGHE-ARGATAYVTLEPCSHYGRTPPC 87
Cdd:cd01284 1 MRRALELAEKGRGLTSPNPPVGCVIVDDDgEIVGEGYHRKAGGPHAEVNALASAGEKlARGATLYVTLEPCSHHGKTPPC 80
|
90 100 110
....*....|....*....|....*....|....*
gi 504233478 88 ARALIDAGVAHVFAATKDPNPSVSGRGLDMLREAG 122
Cdd:cd01284 81 VDAIIEAGIKRVVVGVRDPNPLVAGKGAERLRAAG 115
|
|
| RibD_C |
pfam01872 |
RibD C-terminal domain; The function of this domain is not known, but it is thought to be ... |
150-363 |
4.45e-52 |
|
RibD C-terminal domain; The function of this domain is not known, but it is thought to be involved in riboflavin biosynthesis. This domain is found in the C terminus of RibD/RibG, in combination with pfam00383, as well as in isolation in some archaebacterial proteins. This family appears to be related to pfam00186.
Pssm-ID: 396444 Cd Length: 196 Bit Score: 171.79 E-value: 4.45e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233478 150 PWVRLKMAASLDGRTAMASGESQWITGPEARADVQRLRAISDAILTGVGTVLADDPSLTVRRdemgdiGDATDPSRQPLR 229
Cdd:pfam01872 1 PYVILKFAISLDGKIAAAGGSSQWITGEEARADVHQLRAEADAILVGRGTVRADNPSLTVRW------VKGRAAERQPPR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233478 230 VIADRDARTPATARILQGGNVQVFCASSTLASGPAQDLAALgvsltgvawkdnGVDVAELLDALGELGINELLVEAGPTL 309
Cdd:pfam01872 75 VVVDSTLRVPLDARVLNDDAPTLVATTEPADKEKVEKLKVL------------RVDLKELLRELKERGIRSLLVEGGATL 142
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 504233478 310 AGTFIGENLVDELWLYQAPVFLGSTGRPtahLPLETMADKVQWKVLDRRQVGED 363
Cdd:pfam01872 143 AGSLLRAGLVDELRLYIAPKLLGGGGRT---LFGGEGFLALKLKLVSSEAIGNG 193
|
|
| PRK05625 |
PRK05625 |
5-amino-6-(5-phosphoribosylamino)uracil reductase; Validated |
149-338 |
6.13e-38 |
|
5-amino-6-(5-phosphoribosylamino)uracil reductase; Validated
Pssm-ID: 180169 Cd Length: 217 Bit Score: 135.37 E-value: 6.13e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233478 149 RPWVRLKMAASLDGRTAMASGESQwITGPEARADVQRLRAISDAILTGVGTVLADDPSLTVRRDEMGDigdatdpSRQPL 228
Cdd:PRK05625 2 RPYVIVNAAMSADGKLATKTRYSR-ISGPEDFDRVHELRAEVDAVMVGIGTVLADDPSLTVHRYAAGK-------PENPI 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233478 229 RVIADRDARTPATARILQGGNVQVFCASSTLASGPAQDLAALGVSLtgVAWKDNGVDVAELLDALGELGINELLVEAGPT 308
Cdd:PRK05625 74 RVVVDSSARTPPDARILDGPAKTIVAVSEAAPSEKVEELEKKGAEV--IVAGGERVDLPDLLEDLYERGIKRLMVEGGGT 151
|
170 180 190
....*....|....*....|....*....|
gi 504233478 309 LAGTFIGENLVDELWLYQAPVFLGSTGRPT 338
Cdd:PRK05625 152 LIWSMFKEGLVDEVRVTVGPKIIGGKDAPT 181
|
|
| rib_reduct_arch |
TIGR01508 |
2,5-diamino-6-hydroxy-4-(5-phosphoribosylamino)pyrimidine 1'-reductase, archaeal; This model ... |
150-338 |
1.22e-34 |
|
2,5-diamino-6-hydroxy-4-(5-phosphoribosylamino)pyrimidine 1'-reductase, archaeal; This model represents a specific reductase of riboflavin biosynthesis in the Archaea, diaminohydroxyphosphoribosylaminopyrimidine reductase. It should not be confused with bacterial 5-amino-6-(5-phosphoribosylamino)uracil reductase. The intermediate 2,5-diamino-6-hydroxy-4-(5-phosphoribosylamino)pyrimidine in riboflavin biosynthesis is reduced first, and then deaminated, in both Archaea and Fungi, opposite the order in Bacteria. The subsequent deaminase is not presently known and is not closely homologous to the deaminase domain (3.5.4.26) fused to the reductase domain (1.1.1.193) similar to this protein but found in most bacteria.
Pssm-ID: 130572 Cd Length: 210 Bit Score: 126.84 E-value: 1.22e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233478 150 PWVRLKMAASLDGRTAMASGESQwITGPEARADVQRLRAISDAILTGVGTVLADDPSLTVrrdemgdigDATDPSRQPLR 229
Cdd:TIGR01508 1 PYVIVNVAMSLDGKLATINRDSR-ISCEEDLIRVHEIRAEVDAIMVGIGTVLADDPRLTV---------KKIKSDRNPVR 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233478 230 VIADRDARTPATARILQGGNVQVFCASSTLASGPAQDLAALGVSLtgVAWKDNGVDVAELLDALGELGINELLVEAGPTL 309
Cdd:TIGR01508 71 VVVDSKLRVPLNARILNKDAKTIIATSEDEPEEKVEELEDKGVEV--VKFGEGRVDLKKLLDILYDKGVRRLMVEGGGTL 148
|
170 180
....*....|....*....|....*....
gi 504233478 310 AGTFIGENLVDELWLYQAPVFLGSTGRPT 338
Cdd:TIGR01508 149 IWSLFKENLVDEISVYIAPKIFGGRDAPT 177
|
|
| PRK14719 |
PRK14719 |
bifunctional RNAse/5-amino-6-(5-phosphoribosylamino)uracil reductase; Provisional |
113-338 |
4.11e-24 |
|
bifunctional RNAse/5-amino-6-(5-phosphoribosylamino)uracil reductase; Provisional
Pssm-ID: 237801 [Multi-domain] Cd Length: 360 Bit Score: 101.55 E-value: 4.11e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233478 113 RGL---DMLREAGIRVTEGVMADEASrLNPGFMKRMNTGR-------PWVRLKMAASLDGRTAMASGESQwITGPEARAD 182
Cdd:PRK14719 94 RGIkvnNLIRKEIIKYSRGDLKDIES-LYPYISRRININSdlsdimlPYVISNVGMTLDGKLATIENDSR-ISGENDLKR 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233478 183 VQRLRAISDAILTGVGTVLADDPSLTVRRDEmgdigdaTDPSRQPLRVIADRDARTPATARILQGgNVQVFCASSTLASG 262
Cdd:PRK14719 172 VHEIRKDVDAIMVGIGTVLKDDPRLTVHKIN-------ASPKDNPLRIVVDSNLKIPLNARVLNK-DAKTVIATTTPISD 243
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233478 263 PAQD----LAALGVSL--TGVawkdNGVDVAELLDALGELGINELLVEAGPTLAGTFIGENLVDELWLYQAPVFLGSTGR 336
Cdd:PRK14719 244 EKEEkirkLKEMGITVlqAGV----QKVDLRKIMNEIYKMGINKILLEGGGTLNWGMFKENLINEVRVYIAPKVFGGANS 319
|
..
gi 504233478 337 PT 338
Cdd:PRK14719 320 PT 321
|
|
| TadA |
COG0590 |
tRNA(Arg) A34 adenosine deaminase TadA [Translation, ribosomal structure and biogenesis]; tRNA ... |
4-137 |
4.06e-18 |
|
tRNA(Arg) A34 adenosine deaminase TadA [Translation, ribosomal structure and biogenesis]; tRNA(Arg) A34 adenosine deaminase TadA is part of the Pathway/BioSystem: Pyrimidine salvagetRNA modification
Pssm-ID: 440355 [Multi-domain] Cd Length: 148 Bit Score: 80.16 E-value: 4.06e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233478 4 DRDRAMMARAVQLAWRGRYS-THPnprVGCVIAKGDLIVGEGWHERAGE----AHAEVRALSQAG-----HEARGATAYV 73
Cdd:COG0590 2 EDDEEFMRRALELARKAVAEgEVP---VGAVLVKDGEIIARGHNRVETLndptAHAEILAIRAAArklgnWRLSGCTLYV 78
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 504233478 74 TLEPCshygrtPPCARALIDAGVAHVFAATKDPNPSVSGRGLDMLREA----GIRVTEGVMADEASRL 137
Cdd:COG0590 79 TLEPC------PMCAGAIVWARIGRVVYGASDPKAGAAGSIYDLLADPrlnhRVEVVGGVLAEECAAL 140
|
|
| dCMP_cyt_deam_1 |
pfam00383 |
Cytidine and deoxycytidylate deaminase zinc-binding region; |
6-102 |
8.59e-18 |
|
Cytidine and deoxycytidylate deaminase zinc-binding region;
Pssm-ID: 395307 [Multi-domain] Cd Length: 100 Bit Score: 77.73 E-value: 8.59e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233478 6 DRAMMARAVQLAWRGRysTHPNPRVGCVIAKGD-LIVGEGWH-ERAG---EAHAEVRALSQA-----GHEARGATAYVTL 75
Cdd:pfam00383 2 DEYFMRLALKAAKRAY--PYSNFPVGAVIVKKDgEIIATGYNgENAGydpTIHAERNAIRQAgkrgeGVRLEGATLYVTL 79
|
90 100
....*....|....*....|....*..
gi 504233478 76 EPCSHygrtppCARALIDAGVAHVFAA 102
Cdd:pfam00383 80 EPCGM------CAQAIIESGIKRVVFG 100
|
|
| PRK14059 |
PRK14059 |
pyrimidine reductase family protein; |
144-339 |
8.59e-17 |
|
pyrimidine reductase family protein;
Pssm-ID: 184482 Cd Length: 251 Bit Score: 78.85 E-value: 8.59e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233478 144 RMNTGRPWVRLKMAASLDGrTAMASGESQWITGPEARADVQRLRAISDAILTGVGTVLADDPSLTV----RRDEMGDIGD 219
Cdd:PRK14059 25 PDGLDRPWLRANFVTSLDG-AATVDGRSGGLGGPADRRVFGLLRALADVVVVGAGTVRAENYGGVRlsaaARQQRQARGQ 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233478 220 ATDPsrqPLRVIAdRDARTPATARILQGGNVQ-VFCASSTLASGPAQDLAALGVSLTGVAWKDNGVDVAELLDALGELGI 298
Cdd:PRK14059 104 AEVP---PIAVVS-RSGDLDPDSRLFTETEVPpLVLTCAAAAADRRRRLAGLAEVADVVVAGPDTVDLAAAVAALAARGL 179
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 504233478 299 NELLVEAGPTLAGTFIGENLVDELWLYQAPVFLGSTGRPTA 339
Cdd:PRK14059 180 RRILCEGGPTLLGQLLAADLVDELCLTIAPVLAGGVARRIV 220
|
|
| ComEB |
COG2131 |
Deoxycytidylate deaminase [Nucleotide transport and metabolism]; |
4-125 |
1.29e-14 |
|
Deoxycytidylate deaminase [Nucleotide transport and metabolism];
Pssm-ID: 441734 [Multi-domain] Cd Length: 154 Bit Score: 70.64 E-value: 1.29e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233478 4 DRDRAMMARAVQLAWRgrySTHPNPRVGCVIAKGDLIVG---------------EGW------------HERAGEAHAEV 56
Cdd:COG2131 7 SWDEYFMEIAKLVALR---STCLRRQVGAVIVKDKRILAtgyngapsglphcdeVGClreklgipsgerGECCRTVHAEQ 83
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 504233478 57 RALSQA---GHEARGATAYVTLEPCSHygrtppCARALIDAGVAHVFAATKDPNPsvsgRGLDMLREAGIRV 125
Cdd:COG2131 84 NAILQAarhGVSTEGATLYVTHFPCLE------CAKMIIQAGIKRVVYLEDYPDE----LAKELLKEAGVEV 145
|
|
| deoxycytidylate_deaminase |
cd01286 |
Deoxycytidylate deaminase domain. Deoxycytidylate deaminase catalyzes the deamination of dCMP ... |
10-119 |
1.77e-13 |
|
Deoxycytidylate deaminase domain. Deoxycytidylate deaminase catalyzes the deamination of dCMP to dUMP, providing the nucleotide substrate for thymidylate synthase. The enzyme binds Zn++, which is required for catalytic activity. The activity of the enzyme is allosterically regulated by the ratio of dCTP to dTTP not only in eukaryotic cells but also in T-even phage-infected Escherichia coli, with dCTP acting as an activator and dTTP as an inhibitor.
Pssm-ID: 238613 [Multi-domain] Cd Length: 131 Bit Score: 66.91 E-value: 1.77e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233478 10 MARAVQLAWRgrySTHPNPRVGCVIAKGDLIVG--------------EGWHERAGE-----------AHAEVRALSQA-- 62
Cdd:cd01286 5 MAIARLAALR---STCPRRQVGAVIVKDKRIIStgyngspsglphcaEVGCERDDLpsgedqkccrtVHAEQNAILQAar 81
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 504233478 63 -GHEARGATAYVTLEPCSHygrtppCARALIDAGVAHVFAAtkDPNPSVSGRGLDMLR 119
Cdd:cd01286 82 hGVSLEGATLYVTLFPCIE------CAKLIIQAGIKKVVYA--EPYDDDDPAAAELLE 131
|
|
| PRK10860 |
PRK10860 |
tRNA-specific adenosine deaminase; Provisional |
5-144 |
4.84e-13 |
|
tRNA-specific adenosine deaminase; Provisional
Pssm-ID: 182786 [Multi-domain] Cd Length: 172 Bit Score: 66.75 E-value: 4.84e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233478 5 RDRAMMARAVQLAWRGrYSTHPNPrVGCVIAKGDLIVGEGWHERAGE----AHAEVRALSQAGHEARG-----ATAYVTL 75
Cdd:PRK10860 12 SHEYWMRHALTLAKRA-WDEREVP-VGAVLVHNNRVIGEGWNRPIGRhdptAHAEIMALRQGGLVLQNyrlldATLYVTL 89
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 504233478 76 EPCSHygrtppCARALIDAGVAHVFAATKDPNPSVSGRGLDMLREAG----IRVTEGVMADEASRLNPGFMKR 144
Cdd:PRK10860 90 EPCVM------CAGAMVHSRIGRLVFGARDAKTGAAGSLMDVLHHPGmnhrVEITEGVLADECAALLSDFFRM 156
|
|
| cytidine_deaminase-like |
cd00786 |
Cytidine and deoxycytidylate deaminase zinc-binding region. The family contains cytidine ... |
10-102 |
9.50e-12 |
|
Cytidine and deoxycytidylate deaminase zinc-binding region. The family contains cytidine deaminases, nucleoside deaminases, deoxycytidylate deaminases and riboflavin deaminases. Also included are the apoBec family of mRNA editing enzymes. All members are Zn dependent. The zinc ion in the active site plays a central role in the proposed catalytic mechanism, activating a water molecule to form a hydroxide ion that performs a nucleophilic attack on the substrate.
Pssm-ID: 238406 [Multi-domain] Cd Length: 96 Bit Score: 60.64 E-value: 9.50e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233478 10 MARAVQLAWRGrYSTHPNPRVGCVI--AKGDLIVGEGWHER----AGEAHAEVRALSQAGHEA--RGATAYVTLEPCSHy 81
Cdd:cd00786 1 MTEALKAADLG-YAKESNFQVGACLvnKKDGGKVGRGCNIEnaaySMCNHAERTALFNAGSEGdtKGQMLYVALSPCGA- 78
|
90 100
....*....|....*....|.
gi 504233478 82 grtppCARALIDAGVAHVFAA 102
Cdd:cd00786 79 -----CAQLIIELGIKDVIVV 94
|
|
| MafB19-deam |
pfam14437 |
MafB19-like deaminase; A member of the nucleic acid/nucleotide deaminase superfamily ... |
4-118 |
2.66e-11 |
|
MafB19-like deaminase; A member of the nucleic acid/nucleotide deaminase superfamily prototyped by Neisseria MafB19. Members of this family are present in a wide phyletic range of bacteria and are predicted to function as toxins in bacterial polymorphic toxin systems.
Pssm-ID: 433953 [Multi-domain] Cd Length: 144 Bit Score: 61.00 E-value: 2.66e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233478 4 DRDRAMMARAVQLawRGRYSTHPNPrVGCVIAKGDLIVGEGWHERAGE----AHAEVRALSQA-----GHEARGATAYVT 74
Cdd:pfam14437 2 NHEKWFRKALGLA--EKAYDAGEVP-IGAVIVKDGKVIARGYNRKELNadttAHAEILAIQQAakklgSWRLDDATLYVT 78
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 504233478 75 LEPCshygrtPPCARALIDAGVAHVFAATKDPNPSVSGRGLDML 118
Cdd:pfam14437 79 LEPC------PMCAGAIVQAGLKSLVYGAGNPKGGAVGSVLNKL 116
|
|
| nucleoside_deaminase |
cd01285 |
Nucleoside deaminases include adenosine, guanine and cytosine deaminases. These enzymes are Zn ... |
10-112 |
2.00e-10 |
|
Nucleoside deaminases include adenosine, guanine and cytosine deaminases. These enzymes are Zn dependent and catalyze the deamination of nucleosides. The zinc ion in the active site plays a central role in the proposed catalytic mechanism, activating a water molecule to form a hydroxide ion that performs a nucleophilic attack on the substrate. The functional enzyme is a homodimer. Cytosine deaminase catalyzes the deamination of cytosine to uracil and ammonia and is a member of the pyrimidine salvage pathway. Cytosine deaminase is found in bacteria and fungi but is not present in mammals; for this reason, the enzyme is currently of interest for antimicrobial drug design and gene therapy applications against tumors. Some members of this family are tRNA-specific adenosine deaminases that generate inosine at the first position of their anticodon (position 34) of specific tRNAs; this modification is thought to enlarge the codon recognition capacity during protein synthesis. Other members of the family are guanine deaminases which deaminate guanine to xanthine as part of the utilization of guanine as a nitrogen source.
Pssm-ID: 238612 [Multi-domain] Cd Length: 109 Bit Score: 57.24 E-value: 2.00e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233478 10 MARAVQLAWRGR-YSTHPnprVGCVIAKGDL-IVGEGWHERAGE----AHAEVRALSQAG-----HEARGATAYVTLEPC 78
Cdd:cd01285 1 MRLAIELARKALaEGEVP---FGAVIVDDDGkVIARGHNRVEQDgdptAHAEIVAIRNAArrlgsYLLSGCTLYTTLEPC 77
|
90 100 110
....*....|....*....|....*....|....
gi 504233478 79 shygrtPPCARALIDAGVAHVFAATKDPNPSVSG 112
Cdd:cd01285 78 ------PMCAGALLWARIKRVVYGASDPKLGGIG 105
|
|
| cd |
PHA02588 |
deoxycytidylate deaminase; Provisional |
45-127 |
8.38e-07 |
|
deoxycytidylate deaminase; Provisional
Pssm-ID: 222894 [Multi-domain] Cd Length: 168 Bit Score: 48.60 E-value: 8.38e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233478 45 WHERaGEAHAEVRAL---SQAGHEARGATAYVTLEPCshygrtPPCARALIDAGVAHVFAATK-DPNPSvsgRGLDMLRE 120
Cdd:PHA02588 76 WSSK-NEIHAELNAIlfaARNGISIEGATMYVTASPC------PDCAKAIAQSGIKKLVYCEKyDRNGP---GWDDILRK 145
|
....*..
gi 504233478 121 AGIRVTE 127
Cdd:PHA02588 146 SGIEVIQ 152
|
|
| FolA |
COG0262 |
Dihydrofolate reductase [Coenzyme transport and metabolism]; Dihydrofolate reductase is part ... |
285-359 |
1.17e-05 |
|
Dihydrofolate reductase [Coenzyme transport and metabolism]; Dihydrofolate reductase is part of the Pathway/BioSystem: Folate biosynthesis
Pssm-ID: 440032 [Multi-domain] Cd Length: 168 Bit Score: 45.23 E-value: 1.17e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 504233478 285 DVAELLDALGELGINELLVEAGPTLAGTFIGENLVDELWLYQAPVFLGStGRPTahlpLETMADKVQWKVLDRRQ 359
Cdd:COG0262 90 DLEEALAALKAAGGKDIWVIGGGELYRQLLPAGLVDELYLTVVPVVLGE-GDRL----FPELDAPSRLELVESEA 159
|
|
|