|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02807 |
PLN02807 |
diaminohydroxyphosphoribosylaminopyrimidine deaminase |
64-422 |
0e+00 |
|
diaminohydroxyphosphoribosylaminopyrimidine deaminase
Pssm-ID: 215433 [Multi-domain] Cd Length: 380 Bit Score: 552.46 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 449441472 64 GGHSVRCvnviQGVHCDVDDEVYMRRSLEIARKAIGHTSPNPMVGCVIVKNGEIVGEGFHPKAGQPHAEVFALREAGSLA 143
Cdd:PLN02807 17 RRTSVRC----SARAAGDDDSFYMRRCVELARKAIGCTSPNPMVGCVIVKDGRIVGEGFHPKAGQPHAEVFALRDAGDLA 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 449441472 144 ENATAYVTLEPCNHYGRTPPCTEALIKAKVKRVVVGMVDPNPIVASKGVQRLRDAGIDVTVSIEEDSCKKLNEAYIHQIL 223
Cdd:PLN02807 93 ENATAYVSLEPCNHYGRTPPCTEALIKAKVKRVVVGMVDPNPIVASKGIERLRDAGIEVTVGVEEELCRKLNEAFIHRML 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 449441472 224 TGKPLLTLRYTLSLNGCFLDQVGKGAAEAGGYYSQLLQEYNAVIISpPSSSEEFEIPSSNEHGAKQPLWIIL-SSPDGLI 302
Cdd:PLN02807 173 TGKPFVTLRYSMSMNGCLLNQIGEGADDAGGYYSQLLQEYDAVILS-SALADADPLPLSQEAGAKQPLRIIIaRSESSPL 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 449441472 303 TVPRITDP-TTKVVIFTNKEVVV----SEREIETVVLDQLNMNNILNYCQSQGLNSVMWDVRAKLGVHEELIKEGIEEKL 377
Cdd:PLN02807 252 QIPSLREEsAAKVLVLADKESSAepvlRRKGVEVVVLNQINLDSILDLCYQRGLCSVLLDLRGNVGGLESLLKDALEDKL 331
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 449441472 378 LQKVVVEVLPQWSESQS-ETWFKSMAENLKLKCLEPRMCGPSVVLE 422
Cdd:PLN02807 332 LQKVVVEVLPFWSGSQGqSIASFGGSQSFKLKRLTSREVGGSVVLE 377
|
|
| RibD1 |
COG0117 |
Riboflavin biosynthesis protein RibD, pyrimidine deaminase domain [Coenzyme transport and ... |
84-240 |
1.45e-96 |
|
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: 291.96 E-value: 1.45e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 449441472 84 EVYMRRSLEIARKAIGHTSPNPMVGCVIVKNGEIVGEGFHPKAGQPHAEVFALREAGSLAENATAYVTLEPCNHYGRTPP 163
Cdd:COG0117 1 ERYMRRALELARRGLGTTSPNPLVGCVIVKDGRIVGEGYHQRAGGPHAEVNALAQAGEAARGATLYVTLEPCSHHGRTPP 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 449441472 164 CTEALIKAKVKRVVVGMVDPNPIVASKGVQRLRDAGIDVTVSIEEDSCKKLNEAYIHQILTGKPLLTLRYTLSLNGC 240
Cdd:COG0117 81 CADALIEAGIKRVVIAMLDPNPLVAGKGIARLRAAGIEVEVGVLEEEARALNRGFLKRMRTGRPFVTLKLAMSLDGK 157
|
|
| eubact_ribD |
TIGR00326 |
riboflavin biosynthesis protein RibD; This model describes the ribD protein as found in ... |
87-421 |
2.70e-90 |
|
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: 277.10 E-value: 2.70e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 449441472 87 MRRSLEIARKAIGHTSPNPMVGCVIVKNGEIVGEGFHPKAGQPHAEVFALREAGSLAENATAYVTLEPCNHYGRTPPCTE 166
Cdd:TIGR00326 1 MNRALDLAKKGQGTTHPNPLVGCVIVKNGEIVGEGAHQKAGEPHAEVHALRQAGENAKGATAYVTLEPCSHQGRTPPCAE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 449441472 167 ALIKAKVKRVVVGMVDPNPIVASKGVQRLRDAGIDVTVSIEEDSCKKLNEAYIHQILTGKPLLTLRYTLSLNGCFLDQVG 246
Cdd:TIGR00326 81 AIIEAGIKKVVVSMQDPNPLVAGRGAERLKQAGIEVTFGILKEEAERLNKGFLKRMRTGLPYVQLKLAASLDGKIATASG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 449441472 247 KG---AAEAGGYYSQLLQ-EYNAVIISppSSSEEFEIPSSNEHGAK---QPLWIILSSPDGLITVPRITDPTTKVVIFTN 319
Cdd:TIGR00326 161 ESkwiTSEAARTDAQQLRaQSDAILVG--GGTVKADNPALTARLDEateQPLRVVLDTQLRIPEFAKLIPQIAPTWIFTT 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 449441472 320 KEVVVSERE---IETVVLDQLNMNNILNYCQSQGLNSVMWDVRAKLgvHEELIKEGieekLLQKVVVEVLPQWSESQ--- 393
Cdd:TIGR00326 239 ARDKKKRLEafeVNIFPLEKVTIREVMTQLGKRGINSVLVEGGPNL--LGSFLDEG----LVDELIIYIAPKLLGGThap 312
|
330 340 350
....*....|....*....|....*....|.
gi 449441472 394 ---SETWFKSMAENLKLKCLEPRMCGPSVVL 421
Cdd:TIGR00326 313 glcSEPGFQKMADALNFKFLEINQIGPDILL 343
|
|
| Riboflavin_deaminase-reductase |
cd01284 |
Riboflavin-specific deaminase. Riboflavin biosynthesis protein RibD ... |
87-199 |
4.06e-64 |
|
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: 201.31 E-value: 4.06e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 449441472 87 MRRSLEIARKAIGHTSPNPMVGCVIVK-NGEIVGEGFHPKAGQPHAEVFALREAG-SLAENATAYVTLEPCNHYGRTPPC 164
Cdd:cd01284 1 MRRALELAEKGRGLTSPNPPVGCVIVDdDGEIVGEGYHRKAGGPHAEVNALASAGeKLARGATLYVTLEPCSHHGKTPPC 80
|
90 100 110
....*....|....*....|....*....|....*
gi 449441472 165 TEALIKAKVKRVVVGMVDPNPIVASKGVQRLRDAG 199
Cdd:cd01284 81 VDAIIEAGIKRVVVGVRDPNPLVAGKGAERLRAAG 115
|
|
| dCMP_cyt_deam_1 |
pfam00383 |
Cytidine and deoxycytidylate deaminase zinc-binding region; |
82-179 |
4.12e-25 |
|
Cytidine and deoxycytidylate deaminase zinc-binding region;
Pssm-ID: 395307 [Multi-domain] Cd Length: 100 Bit Score: 98.53 E-value: 4.12e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 449441472 82 DDEVYMRRSLEIARKAigHTSPNPMVGCVIVK-NGEIVGEGFHPK-AGQP---HAEVFALREAGSL-----AENATAYVT 151
Cdd:pfam00383 1 WDEYFMRLALKAAKRA--YPYSNFPVGAVIVKkDGEIIATGYNGEnAGYDptiHAERNAIRQAGKRgegvrLEGATLYVT 78
|
90 100
....*....|....*....|....*...
gi 449441472 152 LEPCNHygrtppCTEALIKAKVKRVVVG 179
Cdd:pfam00383 79 LEPCGM------CAQAIIESGIKRVVFG 100
|
|
|
|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02807 |
PLN02807 |
diaminohydroxyphosphoribosylaminopyrimidine deaminase |
64-422 |
0e+00 |
|
diaminohydroxyphosphoribosylaminopyrimidine deaminase
Pssm-ID: 215433 [Multi-domain] Cd Length: 380 Bit Score: 552.46 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 449441472 64 GGHSVRCvnviQGVHCDVDDEVYMRRSLEIARKAIGHTSPNPMVGCVIVKNGEIVGEGFHPKAGQPHAEVFALREAGSLA 143
Cdd:PLN02807 17 RRTSVRC----SARAAGDDDSFYMRRCVELARKAIGCTSPNPMVGCVIVKDGRIVGEGFHPKAGQPHAEVFALRDAGDLA 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 449441472 144 ENATAYVTLEPCNHYGRTPPCTEALIKAKVKRVVVGMVDPNPIVASKGVQRLRDAGIDVTVSIEEDSCKKLNEAYIHQIL 223
Cdd:PLN02807 93 ENATAYVSLEPCNHYGRTPPCTEALIKAKVKRVVVGMVDPNPIVASKGIERLRDAGIEVTVGVEEELCRKLNEAFIHRML 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 449441472 224 TGKPLLTLRYTLSLNGCFLDQVGKGAAEAGGYYSQLLQEYNAVIISpPSSSEEFEIPSSNEHGAKQPLWIIL-SSPDGLI 302
Cdd:PLN02807 173 TGKPFVTLRYSMSMNGCLLNQIGEGADDAGGYYSQLLQEYDAVILS-SALADADPLPLSQEAGAKQPLRIIIaRSESSPL 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 449441472 303 TVPRITDP-TTKVVIFTNKEVVV----SEREIETVVLDQLNMNNILNYCQSQGLNSVMWDVRAKLGVHEELIKEGIEEKL 377
Cdd:PLN02807 252 QIPSLREEsAAKVLVLADKESSAepvlRRKGVEVVVLNQINLDSILDLCYQRGLCSVLLDLRGNVGGLESLLKDALEDKL 331
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 449441472 378 LQKVVVEVLPQWSESQS-ETWFKSMAENLKLKCLEPRMCGPSVVLE 422
Cdd:PLN02807 332 LQKVVVEVLPFWSGSQGqSIASFGGSQSFKLKRLTSREVGGSVVLE 377
|
|
| RibD1 |
COG0117 |
Riboflavin biosynthesis protein RibD, pyrimidine deaminase domain [Coenzyme transport and ... |
84-240 |
1.45e-96 |
|
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: 291.96 E-value: 1.45e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 449441472 84 EVYMRRSLEIARKAIGHTSPNPMVGCVIVKNGEIVGEGFHPKAGQPHAEVFALREAGSLAENATAYVTLEPCNHYGRTPP 163
Cdd:COG0117 1 ERYMRRALELARRGLGTTSPNPLVGCVIVKDGRIVGEGYHQRAGGPHAEVNALAQAGEAARGATLYVTLEPCSHHGRTPP 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 449441472 164 CTEALIKAKVKRVVVGMVDPNPIVASKGVQRLRDAGIDVTVSIEEDSCKKLNEAYIHQILTGKPLLTLRYTLSLNGC 240
Cdd:COG0117 81 CADALIEAGIKRVVIAMLDPNPLVAGKGIARLRAAGIEVEVGVLEEEARALNRGFLKRMRTGRPFVTLKLAMSLDGK 157
|
|
| eubact_ribD |
TIGR00326 |
riboflavin biosynthesis protein RibD; This model describes the ribD protein as found in ... |
87-421 |
2.70e-90 |
|
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: 277.10 E-value: 2.70e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 449441472 87 MRRSLEIARKAIGHTSPNPMVGCVIVKNGEIVGEGFHPKAGQPHAEVFALREAGSLAENATAYVTLEPCNHYGRTPPCTE 166
Cdd:TIGR00326 1 MNRALDLAKKGQGTTHPNPLVGCVIVKNGEIVGEGAHQKAGEPHAEVHALRQAGENAKGATAYVTLEPCSHQGRTPPCAE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 449441472 167 ALIKAKVKRVVVGMVDPNPIVASKGVQRLRDAGIDVTVSIEEDSCKKLNEAYIHQILTGKPLLTLRYTLSLNGCFLDQVG 246
Cdd:TIGR00326 81 AIIEAGIKKVVVSMQDPNPLVAGRGAERLKQAGIEVTFGILKEEAERLNKGFLKRMRTGLPYVQLKLAASLDGKIATASG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 449441472 247 KG---AAEAGGYYSQLLQ-EYNAVIISppSSSEEFEIPSSNEHGAK---QPLWIILSSPDGLITVPRITDPTTKVVIFTN 319
Cdd:TIGR00326 161 ESkwiTSEAARTDAQQLRaQSDAILVG--GGTVKADNPALTARLDEateQPLRVVLDTQLRIPEFAKLIPQIAPTWIFTT 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 449441472 320 KEVVVSERE---IETVVLDQLNMNNILNYCQSQGLNSVMWDVRAKLgvHEELIKEGieekLLQKVVVEVLPQWSESQ--- 393
Cdd:TIGR00326 239 ARDKKKRLEafeVNIFPLEKVTIREVMTQLGKRGINSVLVEGGPNL--LGSFLDEG----LVDELIIYIAPKLLGGThap 312
|
330 340 350
....*....|....*....|....*....|.
gi 449441472 394 ---SETWFKSMAENLKLKCLEPRMCGPSVVL 421
Cdd:TIGR00326 313 glcSEPGFQKMADALNFKFLEINQIGPDILL 343
|
|
| ribD |
PRK10786 |
bifunctional diaminohydroxyphosphoribosylaminopyrimidine deaminase/5-amino-6- ... |
83-239 |
9.67e-66 |
|
bifunctional diaminohydroxyphosphoribosylaminopyrimidine deaminase/5-amino-6-(5-phosphoribosylamino)uracil reductase RibD;
Pssm-ID: 182729 [Multi-domain] Cd Length: 367 Bit Score: 214.24 E-value: 9.67e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 449441472 83 DEVYMRRSLEIARKAIGHTSPNPMVGCVIVKNGEIVGEGFHPKAGQPHAEVFALREAGSLAENATAYVTLEPCNHYGRTP 162
Cdd:PRK10786 3 DEFYMARALKLAQRGRFTTHPNPNVGCVIVKDGEIVGEGYHQRAGEPHAEVHALRMAGEKAKGATAYVTLEPCSHHGRTP 82
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 449441472 163 PCTEALIKAKVKRVVVGMVDPNPIVASKGVQRLRDAGIDVTVSIEEDSCKKLNEAYIHQILTGKPLLTLRYTLSLNG 239
Cdd:PRK10786 83 PCCDALIAAGVARVVAAMQDPNPQVAGRGLYRLQQAGIDVSHGLMMSEAEALNKGFLKRMRTGFPYIQLKLGASLDG 159
|
|
| Riboflavin_deaminase-reductase |
cd01284 |
Riboflavin-specific deaminase. Riboflavin biosynthesis protein RibD ... |
87-199 |
4.06e-64 |
|
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: 201.31 E-value: 4.06e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 449441472 87 MRRSLEIARKAIGHTSPNPMVGCVIVK-NGEIVGEGFHPKAGQPHAEVFALREAG-SLAENATAYVTLEPCNHYGRTPPC 164
Cdd:cd01284 1 MRRALELAEKGRGLTSPNPPVGCVIVDdDGEIVGEGYHRKAGGPHAEVNALASAGeKLARGATLYVTLEPCSHHGKTPPC 80
|
90 100 110
....*....|....*....|....*....|....*
gi 449441472 165 TEALIKAKVKRVVVGMVDPNPIVASKGVQRLRDAG 199
Cdd:cd01284 81 VDAIIEAGIKRVVVGVRDPNPLVAGKGAERLRAAG 115
|
|
| dCMP_cyt_deam_1 |
pfam00383 |
Cytidine and deoxycytidylate deaminase zinc-binding region; |
82-179 |
4.12e-25 |
|
Cytidine and deoxycytidylate deaminase zinc-binding region;
Pssm-ID: 395307 [Multi-domain] Cd Length: 100 Bit Score: 98.53 E-value: 4.12e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 449441472 82 DDEVYMRRSLEIARKAigHTSPNPMVGCVIVK-NGEIVGEGFHPK-AGQP---HAEVFALREAGSL-----AENATAYVT 151
Cdd:pfam00383 1 WDEYFMRLALKAAKRA--YPYSNFPVGAVIVKkDGEIIATGYNGEnAGYDptiHAERNAIRQAGKRgegvrLEGATLYVT 78
|
90 100
....*....|....*....|....*...
gi 449441472 152 LEPCNHygrtppCTEALIKAKVKRVVVG 179
Cdd:pfam00383 79 LEPCGM------CAQAIIESGIKRVVFG 100
|
|
| TadA |
COG0590 |
tRNA(Arg) A34 adenosine deaminase TadA [Translation, ribosomal structure and biogenesis]; tRNA ... |
82-214 |
5.07e-20 |
|
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: 85.94 E-value: 5.07e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 449441472 82 DDEVYMRRSLEIARKAI---GHtspnPmVGCVIVKNGEIVGEGF-------HPKAgqpHAEVFALREAGSLAEN-----A 146
Cdd:COG0590 3 DDEEFMRRALELARKAVaegEV----P-VGAVLVKDGEIIARGHnrvetlnDPTA---HAEILAIRAAARKLGNwrlsgC 74
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 449441472 147 TAYVTLEPCnhygrtPPCTEALIKAKVKRVVVGMVDPNPIVASKGVQRLRDA----GIDVTVSIEEDSCKKL 214
Cdd:COG0590 75 TLYVTLEPC------PMCAGAIVWARIGRVVYGASDPKAGAAGSIYDLLADPrlnhRVEVVGGVLAEECAAL 140
|
|
| MafB19-deam |
pfam14437 |
MafB19-like deaminase; A member of the nucleic acid/nucleotide deaminase superfamily ... |
82-221 |
2.29e-17 |
|
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: 78.33 E-value: 2.29e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 449441472 82 DDEVYMRRSLEIARKAIGHTSPNpmVGCVIVKNGEIVGEGFHPKAGQ----PHAEVFALREA-----GSLAENATAYVTL 152
Cdd:pfam14437 2 NHEKWFRKALGLAEKAYDAGEVP--IGAVIVKDGKVIARGYNRKELNadttAHAEILAIQQAakklgSWRLDDATLYVTL 79
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 449441472 153 EPCnhygrtPPCTEALIKAKVKRVVVGMVDPNPIVASKGVQRLRDAGIDVTVSIEEDSCKKLNEAYIHQ 221
Cdd:pfam14437 80 EPC------PMCAGAIVQAGLKSLVYGAGNPKGGAVGSVLNKLVIVLWNHRVELVEEDCSEILKGFFKK 142
|
|
| PRK10860 |
PRK10860 |
tRNA-specific adenosine deaminase; Provisional |
76-221 |
4.33e-17 |
|
tRNA-specific adenosine deaminase; Provisional
Pssm-ID: 182786 [Multi-domain] Cd Length: 172 Bit Score: 78.31 E-value: 4.33e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 449441472 76 GVHCDVD----DEVYMRRSLEIARKAIGHTS-PnpmVGCVIVKNGEIVGEGFHPKAGQ----PHAEVFALREAGSLAEN- 145
Cdd:PRK10860 2 GVFFLSEvefsHEYWMRHALTLAKRAWDEREvP---VGAVLVHNNRVIGEGWNRPIGRhdptAHAEIMALRQGGLVLQNy 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 449441472 146 ----ATAYVTLEPCNHygrtppCTEALIKAKVKRVVVGMVDPNPIVASKGVQRLRDAG----IDVTVSIEEDSCKKLNEA 217
Cdd:PRK10860 79 rlldATLYVTLEPCVM------CAGAMVHSRIGRLVFGARDAKTGAAGSLMDVLHHPGmnhrVEITEGVLADECAALLSD 152
|
....
gi 449441472 218 YIHQ 221
Cdd:PRK10860 153 FFRM 156
|
|
| nucleoside_deaminase |
cd01285 |
Nucleoside deaminases include adenosine, guanine and cytosine deaminases. These enzymes are Zn ... |
87-184 |
9.81e-17 |
|
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: 75.35 E-value: 9.81e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 449441472 87 MRRSLEIARKAIGHTSpNPmVGCVIVKN-GEIVGEGfHPKAGQP-----HAEVFALREAGS-----LAENATAYVTLEPC 155
Cdd:cd01285 1 MRLAIELARKALAEGE-VP-FGAVIVDDdGKVIARG-HNRVEQDgdptaHAEIVAIRNAARrlgsyLLSGCTLYTTLEPC 77
|
90 100
....*....|....*....|....*....
gi 449441472 156 nhygrtPPCTEALIKAKVKRVVVGMVDPN 184
Cdd:cd01285 78 ------PMCAGALLWARIKRVVYGASDPK 100
|
|
| cytidine_deaminase-like |
cd00786 |
Cytidine and deoxycytidylate deaminase zinc-binding region. The family contains cytidine ... |
94-180 |
9.15e-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: 61.03 E-value: 9.15e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 449441472 94 ARKAIGHTSPNPMVGCVIVKN--GEIVGEG----FHPKAGQPHAEVFALREAGSLA--ENATAYVTLEPCNHygrtppCT 165
Cdd:cd00786 7 AADLGYAKESNFQVGACLVNKkdGGKVGRGcnieNAAYSMCNHAERTALFNAGSEGdtKGQMLYVALSPCGA------CA 80
|
90
....*....|....*
gi 449441472 166 EALIKAKVKRVVVGM 180
Cdd:cd00786 81 QLIIELGIKDVIVVL 95
|
|
| ComEB |
COG2131 |
Deoxycytidylate deaminase [Nucleotide transport and metabolism]; |
83-202 |
1.10e-11 |
|
Deoxycytidylate deaminase [Nucleotide transport and metabolism];
Pssm-ID: 441734 [Multi-domain] Cd Length: 154 Bit Score: 62.55 E-value: 1.10e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 449441472 83 DEVYMRRSLEIARKAighTSPNPMVGCVIVKNGEIVGEGF--HPKaGQP--------------------------HAEVF 134
Cdd:COG2131 9 DEYFMEIAKLVALRS---TCLRRQVGAVIVKDKRILATGYngAPS-GLPhcdevgclreklgipsgergeccrtvHAEQN 84
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 449441472 135 AL----REAGSLaENATAYVTLEPCNHygrtppCTEALIKAKVKRVVVgmVDPNPivASKGVQRLRDAGIDV 202
Cdd:COG2131 85 AIlqaaRHGVST-EGATLYVTHFPCLE------CAKMIIQAGIKRVVY--LEDYP--DELAKELLKEAGVEV 145
|
|
| deoxycytidylate_deaminase |
cd01286 |
Deoxycytidylate deaminase domain. Deoxycytidylate deaminase catalyzes the deamination of dCMP ... |
83-177 |
4.24e-10 |
|
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: 57.28 E-value: 4.24e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 449441472 83 DEVYMRRSLEIARKAighTSPNPMVGCVIVKNGEIVGEGF--------------HPKAGQP-----------HAEVFALR 137
Cdd:cd01286 1 DEYFMAIARLAALRS---TCPRRQVGAVIVKDKRIISTGYngspsglphcaevgCERDDLPsgedqkccrtvHAEQNAIL 77
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 449441472 138 EAGSL---AENATAYVTLEPCNHygrtppCTEALIKAKVKRVV 177
Cdd:cd01286 78 QAARHgvsLEGATLYVTLFPCIE------CAKLIIQAGIKKVV 114
|
|
| cd |
PHA02588 |
deoxycytidylate deaminase; Provisional |
82-215 |
2.03e-07 |
|
deoxycytidylate deaminase; Provisional
Pssm-ID: 222894 [Multi-domain] Cd Length: 168 Bit Score: 50.53 E-value: 2.03e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 449441472 82 DDEVYMRRSLEIARKAighTSPNPMVGCVIVKNGEIVGEGFH-PKAGQP------------------------------- 129
Cdd:PHA02588 2 KDSTYLQIAYLVSQES---KCVSWKVGAVIEKNGRIISTGYNgTPAGGVnccdhaneqgwlddegklkkehrpehsawss 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 449441472 130 ----HAE----VFALReAGSLAENATAYVTLEPCnhygrtPPCTEALIKAKVKRVVVG-MVDPNPIvasKGVQRLRDAGI 200
Cdd:PHA02588 79 kneiHAElnaiLFAAR-NGISIEGATMYVTASPC------PDCAKAIAQSGIKKLVYCeKYDRNGP---GWDDILRKSGI 148
|
170
....*....|....*
gi 449441472 201 DVtVSIEEDSCKKLN 215
Cdd:PHA02588 149 EV-IQIPKEELNKLN 162
|
|
|