|
Name |
Accession |
Description |
Interval |
E-value |
| RibD1 |
COG0117 |
Riboflavin biosynthesis protein RibD, pyrimidine deaminase domain [Coenzyme transport and ... |
8-311 |
1.06e-62 |
|
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: 202.98 E-value: 1.06e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490246498 8 HHWMRRALLLARRQAGRTWPNPTVGCCIVRDGHLLGEAVHAGPGHPHAEAAVLLALAAhriDPAGATAYITLEPCHHQGR 87
Cdd:COG0117 1 ERYMRRALELARRGLGTTSPNPLVGCVIVKDGRIVGEGYHQRAGGPHAEVNALAQAGE---AARGATLYVTLEPCSHHGR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490246498 88 TAPCSRALAEAGISRVVYAAPDDTPRHPGGGGAWLRENSVEVQPGVFGNLARELNHPFFETSSDSEPHLTLKLAMSADGA 167
Cdd:COG0117 78 TPPCADALIEAGIKRVVIAMLDPNPLVAGKGIARLRAAGIEVEVGVLEEEARALNRGFLKRMRTGRPFVTLKLAMSLDGK 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490246498 168 LARRAGRieavaERAITGQRTRRRVHRMRAGANAVIVGAATARADHPRLDVReLVDGSWSGVQPQPVVLAGRHPL----- 242
Cdd:COG0117 158 IATANGE-----SQWITGEEARADVHRLRARSDAILVGIGTVLADDPSLTVR-LPGGENPPRRVVVDDLLLRPPPalllv 231
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1490246498 243 ETGEVPGRALIMAGADGPRLPGSLRVLRATTRPGGRLDWESVLALLLAEGCGILLVEGGASVAADLLAE 311
Cdd:COG0117 232 ANDAALIIVTVTADAAAALAALAAEAGVVLLLVGGLLLLALLLLLLLLLLLLLLLLLLLGGGGGLAAAA 300
|
|
| eubact_ribD |
TIGR00326 |
riboflavin biosynthesis protein RibD; This model describes the ribD protein as found in ... |
11-355 |
1.62e-55 |
|
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: 185.42 E-value: 1.62e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490246498 11 MRRALLLARRQAGRTWPNPTVGCCIVRDGHLLGEAVHAGPGHPHAEAAVLLALAAHridPAGATAYITLEPCHHQGRTAP 90
Cdd:TIGR00326 1 MNRALDLAKKGQGTTHPNPLVGCVIVKNGEIVGEGAHQKAGEPHAEVHALRQAGEN---AKGATAYVTLEPCSHQGRTPP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490246498 91 CSRALAEAGISRVVYAAPDDTPRHPGGGGAWLRENSVEVQPGVFGNLARELNHPFFETSSDSEPHLTLKLAMSADGALAR 170
Cdd:TIGR00326 78 CAEAIIEAGIKKVVVSMQDPNPLVAGRGAERLKQAGIEVTFGILKEEAERLNKGFLKRMRTGLPYVQLKLAASLDGKIAT 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490246498 171 RAGrieavAERAITGQRTRRRVHRMRAGANAVIVGAATARADHPRLDVRelvdgsWSGVQPQP--VVLAGRH--PLETGE 246
Cdd:TIGR00326 158 ASG-----ESKWITSEAARTDAQQLRAQSDAILVGGGTVKADNPALTAR------LDEATEQPlrVVLDTQLriPEFAKL 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490246498 247 VPGRALIMAGADGPRLPGSLRVLRATTRPGGRLDWESVLALLLAEGCGILLVEGGASVAADLLAERPPHRIHLYLAACGF 326
Cdd:TIGR00326 227 IPQIAPTWIFTTARDKKKRLEAFEVNIFPLEKVTIREVMTQLGKRGINSVLVEGGPNLLGSFLDEGLVDELIIYIAPKLL 306
|
330 340 350
....*....|....*....|....*....|....*
gi 1490246498 327 G----PGSVKLPGGLRLDD--RYETLRARRLGSDV 355
Cdd:TIGR00326 307 GgthaPGLCSEPGFQKMADalNFKFLEINQIGPDI 341
|
|
| ribD |
PRK10786 |
bifunctional diaminohydroxyphosphoribosylaminopyrimidine deaminase/5-amino-6- ... |
6-360 |
7.14e-38 |
|
bifunctional diaminohydroxyphosphoribosylaminopyrimidine deaminase/5-amino-6-(5-phosphoribosylamino)uracil reductase RibD;
Pssm-ID: 182729 [Multi-domain] Cd Length: 367 Bit Score: 139.52 E-value: 7.14e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490246498 6 SDHHWMRRALLLARRQAGRTWPNPTVGCCIVRDGHLLGEAVHAGPGHPHAEAavllalaaHRIDPAG-----ATAYITLE 80
Cdd:PRK10786 2 QDEFYMARALKLAQRGRFTTHPNPNVGCVIVKDGEIVGEGYHQRAGEPHAEV--------HALRMAGekakgATAYVTLE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490246498 81 PCHHQGRTAPCSRALAEAGISRVVYAAPDDTPRHPGGGGAWLRENSVEVQPGVFGNLARELNHPFFETSSDSEPHLTLKL 160
Cdd:PRK10786 74 PCSHHGRTPPCCDALIAAGVARVVAAMQDPNPQVAGRGLYRLQQAGIDVSHGLMMSEAEALNKGFLKRMRTGFPYIQLKL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490246498 161 AMSADGALARRAGRieavaERAITGQRTRRRVHRMRAGANAVIVGAATARADHPRLDVR--ELvDGSWSGVQP-----QP 233
Cdd:PRK10786 154 GASLDGRTAMASGE-----SQWITSPQARRDVQRLRAQSHAILTSSATVLADDPALTVRwsEL-DAQTQALYPqenlrQP 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490246498 234 V-VLAGRHPLETGE-----VPGRALIM-AGADGPRLPGSLRVLRaTTRPGGRLDWESVLALLLAEGCGILLVEGGASVAA 306
Cdd:PRK10786 228 VrIVIDSQNRVTPEhrivqQPGETWLArTQEDSREWPETVRTLL-LPEHNGHLDLVVLMMQLGKQQINSIWVEAGPTLAG 306
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 1490246498 307 DLLAERPPHRIHLYLAACGFGP---GSVKLPGGLRLDD--RYETLRARRLGSDVEWVLR 360
Cdd:PRK10786 307 ALLQAGLVDELIVYIAPKLLGSdarGLCTLPGLEKLADapQFKFSEIRHVGPDVCLHLV 365
|
|
| Riboflavin_deaminase-reductase |
cd01284 |
Riboflavin-specific deaminase. Riboflavin biosynthesis protein RibD ... |
11-125 |
1.99e-30 |
|
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: 112.33 E-value: 1.99e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490246498 11 MRRALLLARRQAGRTWPNPTVGCCIVRD-GHLLGEAVHAGPGHPHAEAAVLLALAahRIDPAGATAYITLEPCHHQGRTA 89
Cdd:cd01284 1 MRRALELAEKGRGLTSPNPPVGCVIVDDdGEIVGEGYHRKAGGPHAEVNALASAG--EKLARGATLYVTLEPCSHHGKTP 78
|
90 100 110
....*....|....*....|....*....|....*.
gi 1490246498 90 PCSRALAEAGISRVVYAAPDDTPRHPGGGGAWLREN 125
Cdd:cd01284 79 PCVDAIIEAGIKRVVVGVRDPNPLVAGKGAERLRAA 114
|
|
| RibD_C |
pfam01872 |
RibD C-terminal domain; The function of this domain is not known, but it is thought to be ... |
154-355 |
1.18e-17 |
|
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: 80.12 E-value: 1.18e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490246498 154 PHLTLKLAMSADGALARRAGrieavAERAITGQRTRRRVHRMRAGANAVIVGAATARADHPRLDVReLVDGSWSGVQPQP 233
Cdd:pfam01872 1 PYVILKFAISLDGKIAAAGG-----SSQWITGEEARADVHQLRAEADAILVGRGTVRADNPSLTVR-WVKGRAAERQPPR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490246498 234 VVLA--GRHPLETGEVPGRALIMAGADGPRLPGSLRVLRATtrpggRLDWESVLALLLAEGCGILLVEGGASVAADLLAE 311
Cdd:pfam01872 75 VVVDstLRVPLDARVLNDDAPTLVATTEPADKEKVEKLKVL-----RVDLKELLRELKERGIRSLLVEGGATLAGSLLRA 149
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1490246498 312 RPPHRIHLYLAACGFGPGSVKLPGGLRLDD-RYETLRARRLGSDV 355
Cdd:pfam01872 150 GLVDELRLYIAPKLLGGGGRTLFGGEGFLAlKLKLVSSEAIGNGV 194
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| RibD1 |
COG0117 |
Riboflavin biosynthesis protein RibD, pyrimidine deaminase domain [Coenzyme transport and ... |
8-311 |
1.06e-62 |
|
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: 202.98 E-value: 1.06e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490246498 8 HHWMRRALLLARRQAGRTWPNPTVGCCIVRDGHLLGEAVHAGPGHPHAEAAVLLALAAhriDPAGATAYITLEPCHHQGR 87
Cdd:COG0117 1 ERYMRRALELARRGLGTTSPNPLVGCVIVKDGRIVGEGYHQRAGGPHAEVNALAQAGE---AARGATLYVTLEPCSHHGR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490246498 88 TAPCSRALAEAGISRVVYAAPDDTPRHPGGGGAWLRENSVEVQPGVFGNLARELNHPFFETSSDSEPHLTLKLAMSADGA 167
Cdd:COG0117 78 TPPCADALIEAGIKRVVIAMLDPNPLVAGKGIARLRAAGIEVEVGVLEEEARALNRGFLKRMRTGRPFVTLKLAMSLDGK 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490246498 168 LARRAGRieavaERAITGQRTRRRVHRMRAGANAVIVGAATARADHPRLDVReLVDGSWSGVQPQPVVLAGRHPL----- 242
Cdd:COG0117 158 IATANGE-----SQWITGEEARADVHRLRARSDAILVGIGTVLADDPSLTVR-LPGGENPPRRVVVDDLLLRPPPalllv 231
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1490246498 243 ETGEVPGRALIMAGADGPRLPGSLRVLRATTRPGGRLDWESVLALLLAEGCGILLVEGGASVAADLLAE 311
Cdd:COG0117 232 ANDAALIIVTVTADAAAALAALAAEAGVVLLLVGGLLLLALLLLLLLLLLLLLLLLLLLGGGGGLAAAA 300
|
|
| eubact_ribD |
TIGR00326 |
riboflavin biosynthesis protein RibD; This model describes the ribD protein as found in ... |
11-355 |
1.62e-55 |
|
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: 185.42 E-value: 1.62e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490246498 11 MRRALLLARRQAGRTWPNPTVGCCIVRDGHLLGEAVHAGPGHPHAEAAVLLALAAHridPAGATAYITLEPCHHQGRTAP 90
Cdd:TIGR00326 1 MNRALDLAKKGQGTTHPNPLVGCVIVKNGEIVGEGAHQKAGEPHAEVHALRQAGEN---AKGATAYVTLEPCSHQGRTPP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490246498 91 CSRALAEAGISRVVYAAPDDTPRHPGGGGAWLRENSVEVQPGVFGNLARELNHPFFETSSDSEPHLTLKLAMSADGALAR 170
Cdd:TIGR00326 78 CAEAIIEAGIKKVVVSMQDPNPLVAGRGAERLKQAGIEVTFGILKEEAERLNKGFLKRMRTGLPYVQLKLAASLDGKIAT 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490246498 171 RAGrieavAERAITGQRTRRRVHRMRAGANAVIVGAATARADHPRLDVRelvdgsWSGVQPQP--VVLAGRH--PLETGE 246
Cdd:TIGR00326 158 ASG-----ESKWITSEAARTDAQQLRAQSDAILVGGGTVKADNPALTAR------LDEATEQPlrVVLDTQLriPEFAKL 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490246498 247 VPGRALIMAGADGPRLPGSLRVLRATTRPGGRLDWESVLALLLAEGCGILLVEGGASVAADLLAERPPHRIHLYLAACGF 326
Cdd:TIGR00326 227 IPQIAPTWIFTTARDKKKRLEAFEVNIFPLEKVTIREVMTQLGKRGINSVLVEGGPNLLGSFLDEGLVDELIIYIAPKLL 306
|
330 340 350
....*....|....*....|....*....|....*
gi 1490246498 327 G----PGSVKLPGGLRLDD--RYETLRARRLGSDV 355
Cdd:TIGR00326 307 GgthaPGLCSEPGFQKMADalNFKFLEINQIGPDI 341
|
|
| ribD |
PRK10786 |
bifunctional diaminohydroxyphosphoribosylaminopyrimidine deaminase/5-amino-6- ... |
6-360 |
7.14e-38 |
|
bifunctional diaminohydroxyphosphoribosylaminopyrimidine deaminase/5-amino-6-(5-phosphoribosylamino)uracil reductase RibD;
Pssm-ID: 182729 [Multi-domain] Cd Length: 367 Bit Score: 139.52 E-value: 7.14e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490246498 6 SDHHWMRRALLLARRQAGRTWPNPTVGCCIVRDGHLLGEAVHAGPGHPHAEAavllalaaHRIDPAG-----ATAYITLE 80
Cdd:PRK10786 2 QDEFYMARALKLAQRGRFTTHPNPNVGCVIVKDGEIVGEGYHQRAGEPHAEV--------HALRMAGekakgATAYVTLE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490246498 81 PCHHQGRTAPCSRALAEAGISRVVYAAPDDTPRHPGGGGAWLRENSVEVQPGVFGNLARELNHPFFETSSDSEPHLTLKL 160
Cdd:PRK10786 74 PCSHHGRTPPCCDALIAAGVARVVAAMQDPNPQVAGRGLYRLQQAGIDVSHGLMMSEAEALNKGFLKRMRTGFPYIQLKL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490246498 161 AMSADGALARRAGRieavaERAITGQRTRRRVHRMRAGANAVIVGAATARADHPRLDVR--ELvDGSWSGVQP-----QP 233
Cdd:PRK10786 154 GASLDGRTAMASGE-----SQWITSPQARRDVQRLRAQSHAILTSSATVLADDPALTVRwsEL-DAQTQALYPqenlrQP 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490246498 234 V-VLAGRHPLETGE-----VPGRALIM-AGADGPRLPGSLRVLRaTTRPGGRLDWESVLALLLAEGCGILLVEGGASVAA 306
Cdd:PRK10786 228 VrIVIDSQNRVTPEhrivqQPGETWLArTQEDSREWPETVRTLL-LPEHNGHLDLVVLMMQLGKQQINSIWVEAGPTLAG 306
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 1490246498 307 DLLAERPPHRIHLYLAACGFGP---GSVKLPGGLRLDD--RYETLRARRLGSDVEWVLR 360
Cdd:PRK10786 307 ALLQAGLVDELIVYIAPKLLGSdarGLCTLPGLEKLADapQFKFSEIRHVGPDVCLHLV 365
|
|
| PLN02807 |
PLN02807 |
diaminohydroxyphosphoribosylaminopyrimidine deaminase |
2-168 |
1.66e-36 |
|
diaminohydroxyphosphoribosylaminopyrimidine deaminase
Pssm-ID: 215433 [Multi-domain] Cd Length: 380 Bit Score: 136.06 E-value: 1.66e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490246498 2 EGSASDHHWMRRALLLARRQAGRTWPNPTVGCCIVRDGHLLGEAVHAGPGHPHAEAAVLLALAahriDPA-GATAYITLE 80
Cdd:PLN02807 27 AAGDDDSFYMRRCVELARKAIGCTSPNPMVGCVIVKDGRIVGEGFHPKAGQPHAEVFALRDAG----DLAeNATAYVSLE 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490246498 81 PCHHQGRTAPCSRALAEAGISRVVYAAPDDTPRHPGGGGAWLRENSVEVQPGVFGNLARELNHPFFETSSDSEPHLTLKL 160
Cdd:PLN02807 103 PCNHYGRTPPCTEALIKAKVKRVVVGMVDPNPIVASKGIERLRDAGIEVTVGVEEELCRKLNEAFIHRMLTGKPFVTLRY 182
|
....*...
gi 1490246498 161 AMSADGAL 168
Cdd:PLN02807 183 SMSMNGCL 190
|
|
| Riboflavin_deaminase-reductase |
cd01284 |
Riboflavin-specific deaminase. Riboflavin biosynthesis protein RibD ... |
11-125 |
1.99e-30 |
|
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: 112.33 E-value: 1.99e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490246498 11 MRRALLLARRQAGRTWPNPTVGCCIVRD-GHLLGEAVHAGPGHPHAEAAVLLALAahRIDPAGATAYITLEPCHHQGRTA 89
Cdd:cd01284 1 MRRALELAEKGRGLTSPNPPVGCVIVDDdGEIVGEGYHRKAGGPHAEVNALASAG--EKLARGATLYVTLEPCSHHGKTP 78
|
90 100 110
....*....|....*....|....*....|....*.
gi 1490246498 90 PCSRALAEAGISRVVYAAPDDTPRHPGGGGAWLREN 125
Cdd:cd01284 79 PCVDAIIEAGIKRVVVGVRDPNPLVAGKGAERLRAA 114
|
|
| RibD |
COG1985 |
Pyrimidine reductase, riboflavin biosynthesis [Coenzyme transport and metabolism]; Pyrimidine ... |
154-363 |
1.55e-24 |
|
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: 99.46 E-value: 1.55e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490246498 154 PHLTLKLAMSADGALARRAGRieavaERAITGQRTRRRVHRMRAGANAVIVGAATARADHPRLDVRelvdGSWSGVQPQP 233
Cdd:COG1985 4 PYVTLKLAMSLDGKIATADGE-----SKWITGEAARRDVHRLRARADAILVGAGTVLADDPSLTVR----LPGLGRQPLR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490246498 234 VVLAGRHPLETG----EVPGRALIMAGADGPrlPGSLRVLRA------TTRPGGRLDWESVLALLLAEGCGILLVEGGAS 303
Cdd:COG1985 75 VVVDSSLRLPPDarlfDDAAPTLVLTTEAAD--AERRAALEAagaeviVLPGDGRVDLAALLAALAERGIRSVLVEGGPT 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1490246498 304 VAADLLAERPPHRIHLYLAAC---GFGPGSVKLPGGLRLDD--RYETLRARRLGSDVEWVLRRRD 363
Cdd:COG1985 153 LAGSFLAAGLVDELILYIAPKllgGDGPTLVGGPGLETLADapRLRLVSVRRLGDDLLLRYRPRR 217
|
|
| RibD_C |
pfam01872 |
RibD C-terminal domain; The function of this domain is not known, but it is thought to be ... |
154-355 |
1.18e-17 |
|
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: 80.12 E-value: 1.18e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490246498 154 PHLTLKLAMSADGALARRAGrieavAERAITGQRTRRRVHRMRAGANAVIVGAATARADHPRLDVReLVDGSWSGVQPQP 233
Cdd:pfam01872 1 PYVILKFAISLDGKIAAAGG-----SSQWITGEEARADVHQLRAEADAILVGRGTVRADNPSLTVR-WVKGRAAERQPPR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490246498 234 VVLA--GRHPLETGEVPGRALIMAGADGPRLPGSLRVLRATtrpggRLDWESVLALLLAEGCGILLVEGGASVAADLLAE 311
Cdd:pfam01872 75 VVVDstLRVPLDARVLNDDAPTLVATTEPADKEKVEKLKVL-----RVDLKELLRELKERGIRSLLVEGGATLAGSLLRA 149
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1490246498 312 RPPHRIHLYLAACGFGPGSVKLPGGLRLDD-RYETLRARRLGSDV 355
Cdd:pfam01872 150 GLVDELRLYIAPKLLGGGGRTLFGGEGFLAlKLKLVSSEAIGNGV 194
|
|
| ribD_Cterm |
TIGR00227 |
riboflavin-specific deaminase C-terminal domain; Eubacterial riboflavin-specific deaminases ... |
154-355 |
1.62e-16 |
|
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: 77.43 E-value: 1.62e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490246498 154 PHLTLKLAMSADGALARRAGRieavaERAITGQRTRRRVHRMRAGANAVIVGAATARADHPRLDVRElvDGSWSGVQPQP 233
Cdd:TIGR00227 3 PYVILKYAMSLDGKIATASGE-----SSWITSEEARRDVHQLRAQSDAILVGSGTVLADDPRLTVRW--VELDELRNPVR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490246498 234 VVLAGRH--PLETGEVPGRALIMAGADGPRLPGSLRVLRATTR----PG-GRLDWESVLALLLAEGCGILLVEGGASVAA 306
Cdd:TIGR00227 76 VVLDSRLrvPPTARLLNDDAPTWVATSEPADEEKVKELEDFGVevlvLEtKRVDLKKLMEILYEEGIRSVMVEGGGTLNG 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1490246498 307 DLLAERPPHRIHLYLAACGFG----PGSVKLPGGLRLDD--RYETLRARRLGSDV 355
Cdd:TIGR00227 156 SLLKEGLVDELIVYIAPKLLGgrdaPTLVDGEGFQKMADapNLELKEIYQIGEDI 210
|
|
| dCMP_cyt_deam_1 |
pfam00383 |
Cytidine and deoxycytidylate deaminase zinc-binding region; |
7-106 |
1.57e-12 |
|
Cytidine and deoxycytidylate deaminase zinc-binding region;
Pssm-ID: 395307 [Multi-domain] Cd Length: 100 Bit Score: 63.09 E-value: 1.57e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490246498 7 DHHWMRRALLLARRqaGRTWPNPTVGCCIVR-DGHLLGEAVHAGPG------HPHAEAAVLLALAAHRIDPAGATAYITL 79
Cdd:pfam00383 2 DEYFMRLALKAAKR--AYPYSNFPVGAVIVKkDGEIIATGYNGENAgydptiHAERNAIRQAGKRGEGVRLEGATLYVTL 79
|
90 100
....*....|....*....|....*..
gi 1490246498 80 EPCHHqgrtapCSRALAEAGISRVVYA 106
Cdd:pfam00383 80 EPCGM------CAQAIIESGIKRVVFG 100
|
|
| deoxycytidylate_deaminase |
cd01286 |
Deoxycytidylate deaminase domain. Deoxycytidylate deaminase catalyzes the deamination of dCMP ... |
7-108 |
6.76e-11 |
|
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: 59.21 E-value: 6.76e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490246498 7 DHHWMRRALLLARRQagrTWPNPTVGCCIVRDGHLLGEAVHAGP---------GHPHAEAAVLLALAAHR---------- 67
Cdd:cd01286 1 DEYFMAIARLAALRS---TCPRRQVGAVIVKDKRIISTGYNGSPsglphcaevGCERDDLPSGEDQKCCRtvhaeqnail 77
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 1490246498 68 ------IDPAGATAYITLEPCHHqgrtapCSRALAEAGISRVVYAAP 108
Cdd:cd01286 78 qaarhgVSLEGATLYVTLFPCIE------CAKLIIQAGIKKVVYAEP 118
|
|
| ComEB |
COG2131 |
Deoxycytidylate deaminase [Nucleotide transport and metabolism]; |
7-108 |
1.06e-10 |
|
Deoxycytidylate deaminase [Nucleotide transport and metabolism];
Pssm-ID: 441734 [Multi-domain] Cd Length: 154 Bit Score: 59.47 E-value: 1.06e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490246498 7 DHHWMRRALLLARRQagrTWPNPTVGCCIVRDGHLLG----EAVHAGP-----GHPHAEAAVLLALA------------- 64
Cdd:COG2131 9 DEYFMEIAKLVALRS---TCLRRQVGAVIVKDKRILAtgynGAPSGLPhcdevGCLREKLGIPSGERgeccrtvhaeqna 85
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 1490246498 65 -----AHRIDPAGATAYITLEPCHHqgrtapCSRALAEAGISRVVYAAP 108
Cdd:COG2131 86 ilqaaRHGVSTEGATLYVTHFPCLE------CAKMIIQAGIKRVVYLED 128
|
|
| TadA |
COG0590 |
tRNA(Arg) A34 adenosine deaminase TadA [Translation, ribosomal structure and biogenesis]; tRNA ... |
6-110 |
3.91e-09 |
|
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: 54.74 E-value: 3.91e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490246498 6 SDHHWMRRALLLARrQAGRT--WPnptVGCCIVRDGHLLGEAV-----------HA------------Gpghphaeaavl 60
Cdd:COG0590 3 DDEEFMRRALELAR-KAVAEgeVP---VGAVLVKDGEIIARGHnrvetlndptaHAeilairaaarklG----------- 67
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 1490246498 61 lalaahRIDPAGATAYITLEPChhqgrtaP-CSRALAEAGISRVVYAAPDD 110
Cdd:COG0590 68 ------NWRLSGCTLYVTLEPC-------PmCAGAIVWARIGRVVYGASDP 105
|
|
| nucleoside_deaminase |
cd01285 |
Nucleoside deaminases include adenosine, guanine and cytosine deaminases. These enzymes are Zn ... |
11-124 |
9.74e-07 |
|
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: 46.84 E-value: 9.74e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490246498 11 MRRALLLARrQAGRTWPNPtVGCCIVR-DGHLLGEAV------HAGPGHPHAEAAVLLALAAHRIDPAGATAYITLEPCh 83
Cdd:cd01285 1 MRLAIELAR-KALAEGEVP-FGAVIVDdDGKVIARGHnrveqdGDPTAHAEIVAIRNAARRLGSYLLSGCTLYTTLEPC- 77
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 1490246498 84 hqgrtAPCSRALAEAGISRVVYAAPDDTprhpGGGGAWLRE 124
Cdd:cd01285 78 -----PMCAGALLWARIKRVVYGASDPK----LGGIGFLIE 109
|
|
| PRK10860 |
PRK10860 |
tRNA-specific adenosine deaminase; Provisional |
1-116 |
1.28e-06 |
|
tRNA-specific adenosine deaminase; Provisional
Pssm-ID: 182786 [Multi-domain] Cd Length: 172 Bit Score: 47.88 E-value: 1.28e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490246498 1 MEGSASDHHWMRRALLLARR-QAGRTWPnptVGCCIVRDGHLLGEA------VHAGPGHPHAEAAVLLALAAHRIDPAGA 73
Cdd:PRK10860 7 SEVEFSHEYWMRHALTLAKRaWDEREVP---VGAVLVHNNRVIGEGwnrpigRHDPTAHAEIMALRQGGLVLQNYRLLDA 83
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 1490246498 74 TAYITLEPChhqgrtAPCSRALAEAGISRVVYAAPD----------DTPRHPG 116
Cdd:PRK10860 84 TLYVTLEPC------VMCAGAMVHSRIGRLVFGARDaktgaagslmDVLHHPG 130
|
|
| PRK05625 |
PRK05625 |
5-amino-6-(5-phosphoribosylamino)uracil reductase; Validated |
154-302 |
3.65e-06 |
|
5-amino-6-(5-phosphoribosylamino)uracil reductase; Validated
Pssm-ID: 180169 Cd Length: 217 Bit Score: 47.16 E-value: 3.65e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490246498 154 PHLTLKLAMSADGALARRAGrieavaERAITGQRTRRRVHRMRAGANAVIVGAATARADHPRLDVRELVDGswSGVQPQP 233
Cdd:PRK05625 3 PYVIVNAAMSADGKLATKTR------YSRISGPEDFDRVHELRAEVDAVMVGIGTVLADDPSLTVHRYAAG--KPENPIR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490246498 234 VVLAGRhpletGEVPGRALIMAGaDGPRL--------PGSLRVLRAT-----TRPGGRLDWESVLALLLAEGCGILLVEG 300
Cdd:PRK05625 75 VVVDSS-----ARTPPDARILDG-PAKTIvavseaapSEKVEELEKKgaeviVAGGERVDLPDLLEDLYERGIKRLMVEG 148
|
..
gi 1490246498 301 GA 302
Cdd:PRK05625 149 GG 150
|
|
| cd |
PHA02588 |
deoxycytidylate deaminase; Provisional |
72-129 |
1.57e-05 |
|
deoxycytidylate deaminase; Provisional
Pssm-ID: 222894 [Multi-domain] Cd Length: 168 Bit Score: 44.75 E-value: 1.57e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 1490246498 72 GATAYITLEPCHHqgrtapCSRALAEAGISRVVYAapDDTPRHPGGGGAWLRENSVEV 129
Cdd:PHA02588 101 GATMYVTASPCPD------CAKAIAQSGIKKLVYC--EKYDRNGPGWDDILRKSGIEV 150
|
|
| MafB19-deam |
pfam14437 |
MafB19-like deaminase; A member of the nucleic acid/nucleotide deaminase superfamily ... |
6-109 |
7.21e-05 |
|
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: 42.51 E-value: 7.21e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490246498 6 SDHHWMRRALLLARRQAGRTwpNPTVGCCIVRDGHLLGEA-----VHAGPG-HPHAEAAVLLALAAHRIDPAGATAYITL 79
Cdd:pfam14437 2 NHEKWFRKALGLAEKAYDAG--EVPIGAVIVKDGKVIARGynrkeLNADTTaHAEILAIQQAAKKLGSWRLDDATLYVTL 79
|
90 100 110
....*....|....*....|....*....|
gi 1490246498 80 EPChhqgrtAPCSRALAEAGISRVVYAAPD 109
Cdd:pfam14437 80 EPC------PMCAGAIVQAGLKSLVYGAGN 103
|
|
| cytidine_deaminase-like |
cd00786 |
Cytidine and deoxycytidylate deaminase zinc-binding region. The family contains cytidine ... |
16-106 |
8.28e-05 |
|
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: 41.00 E-value: 8.28e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490246498 16 LLARRQAGRTWPNPTVGCCIV--RDGHLLGEAVH----AGPGHPHAEAAVLLALAAHRiDPAGATAYITLEPCHHqgrta 89
Cdd:cd00786 5 LKAADLGYAKESNFQVGACLVnkKDGGKVGRGCNienaAYSMCNHAERTALFNAGSEG-DTKGQMLYVALSPCGA----- 78
|
90
....*....|....*..
gi 1490246498 90 pCSRALAEAGISRVVYA 106
Cdd:cd00786 79 -CAQLIIELGIKDVIVV 94
|
|
| rib_reduct_arch |
TIGR01508 |
2,5-diamino-6-hydroxy-4-(5-phosphoribosylamino)pyrimidine 1'-reductase, archaeal; This model ... |
154-327 |
1.17e-04 |
|
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: 42.87 E-value: 1.17e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490246498 154 PHLTLKLAMSADGALARRAGRIEavaeraITGQRTRRRVHRMRAGANAVIVGAATARADHPRLDV----------RELVD 223
Cdd:TIGR01508 1 PYVIVNVAMSLDGKLATINRDSR------ISCEEDLIRVHEIRAEVDAIMVGIGTVLADDPRLTVkkiksdrnpvRVVVD 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490246498 224 GSWSgVQPQPVVLAGrhpletgevPGRALIMAGADGPRLP-GSLRVLRATTRPGGRL--DWESVLALLLAEGCGILLVEG 300
Cdd:TIGR01508 75 SKLR-VPLNARILNK---------DAKTIIATSEDEPEEKvEELEDKGVEVVKFGEGrvDLKKLLDILYDKGVRRLMVEG 144
|
170 180
....*....|....*....|....*..
gi 1490246498 301 GASVAADLLAERPPHRIHLYLAACGFG 327
Cdd:TIGR01508 145 GGTLIWSLFKENLVDEISVYIAPKIFG 171
|
|
| |
