|
Name |
Accession |
Description |
Interval |
E-value |
| RibD1 |
COG0117 |
Riboflavin biosynthesis protein RibD, pyrimidine deaminase domain [Coenzyme transport and ... |
1-307 |
3.21e-122 |
|
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: 353.98 E-value: 3.21e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1745509151 1 MRRCIQLAKNGLCNVSPNPMVGAVIVCEGQIIGEGYHIRCGEAHAEVNAIRSVKDpsLLKHSTIYVSLEPCSHHGKTPPC 80
Cdd:COG0117 4 MRRALELARRGLGTTSPNPLVGCVIVKDGRIVGEGYHQRAGGPHAEVNALAQAGE--AARGATLYVTLEPCSHHGRTPPC 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1745509151 81 ADLIIEKQIPRIVIGCQDPFSKVAGKGIQKLRDAGCEVIVGVLEPECRELIRKFITFHTLHRPYIVLKWAESADGFIDLE 160
Cdd:COG0117 82 ADALIEAGIKRVVIAMLDPNPLVAGKGIARLRAAGIEVEVGVLEEEARALNRGFLKRMRTGRPFVTLKLAMSLDGKIATA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1745509151 161 RteGQPVILSTPLTSMLVHKKRAESDAIMVGTRTALLDNPALTVRNWYGHNPVRIVMDRNHSLPQTSHLSDNSVSTLVFT 240
Cdd:COG0117 162 N--GESQWITGEEARADVHRLRARSDAILVGIGTVLADDPSLTVRLPGGENPPRRVVVDDLLLRPPPALLLVANDAALII 239
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1745509151 241 EHPRSGKENLEYITLNYQTDILPQILSALYQRNLQSLMVEGGRILLESFIRSGIWDEVIIEKSDKLL 307
Cdd:COG0117 240 VTVTADAAAALAALAAEAGVVLLLVGGLLLLALLLLLLLLLLLLLLLLLLLGGGGGLAAAALLAALL 306
|
|
| eubact_ribD |
TIGR00326 |
riboflavin biosynthesis protein RibD; This model describes the ribD protein as found in ... |
1-314 |
3.13e-96 |
|
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: 289.04 E-value: 3.13e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1745509151 1 MRRCIQLAKNGLCNVSPNPMVGAVIVCEGQIIGEGYHIRCGEAHAEVNAIRSVKDPslLKHSTIYVSLEPCSHHGKTPPC 80
Cdd:TIGR00326 1 MNRALDLAKKGQGTTHPNPLVGCVIVKNGEIVGEGAHQKAGEPHAEVHALRQAGEN--AKGATAYVTLEPCSHQGRTPPC 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1745509151 81 ADLIIEKQIPRIVIGCQDPFSKVAGKGIQKLRDAGCEVIVGVLEPECRELIRKFITFHTLHRPYIVLKWAESADGFIDLE 160
Cdd:TIGR00326 79 AEAIIEAGIKKVVVSMQDPNPLVAGRGAERLKQAGIEVTFGILKEEAERLNKGFLKRMRTGLPYVQLKLAASLDGKIATA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1745509151 161 RTEGQpvILSTPLTSMLVHKKRAESDAIMVGTRTALLDNPALTVRnWYG--HNPVRIVMDRNHSLPQTSHLSDNSVSTLV 238
Cdd:TIGR00326 159 SGESK--WITSEAARTDAQQLRAQSDAILVGGGTVKADNPALTAR-LDEatEQPLRVVLDTQLRIPEFAKLIPQIAPTWI 235
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1745509151 239 FTEH--PRSGKENLEYITLNYQTDILPQILSALYQRNLQSLMVEGGRILLESFIRSGIWDEVIIEKSDKLLySGVKAP 314
Cdd:TIGR00326 236 FTTArdKKKRLEAFEVNIFPLEKVTIREVMTQLGKRGINSVLVEGGPNLLGSFLDEGLVDELIIYIAPKLL-GGTHAP 312
|
|
| ribD |
PRK10786 |
bifunctional diaminohydroxyphosphoribosylaminopyrimidine deaminase/5-amino-6- ... |
1-307 |
7.60e-66 |
|
bifunctional diaminohydroxyphosphoribosylaminopyrimidine deaminase/5-amino-6-(5-phosphoribosylamino)uracil reductase RibD;
Pssm-ID: 182729 [Multi-domain] Cd Length: 367 Bit Score: 211.93 E-value: 7.60e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1745509151 1 MRRCIQLAKNGLCNVSPNPMVGAVIVCEGQIIGEGYHIRCGEAHAEVNAIRSVKDPSllKHSTIYVSLEPCSHHGKTPPC 80
Cdd:PRK10786 7 MARALKLAQRGRFTTHPNPNVGCVIVKDGEIVGEGYHQRAGEPHAEVHALRMAGEKA--KGATAYVTLEPCSHHGRTPPC 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1745509151 81 ADLIIEKQIPRIVIGCQDPFSKVAGKGIQKLRDAGCEVIVGVLEPECRELIRKFITFHTLHRPYIVLKWAESADGFIDLE 160
Cdd:PRK10786 85 CDALIAAGVARVVAAMQDPNPQVAGRGLYRLQQAGIDVSHGLMMSEAEALNKGFLKRMRTGFPYIQLKLGASLDGRTAMA 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1745509151 161 RTEGQPVilSTPLTSMLVHKKRAESDAIMVGTRTALLDNPALTVRnW----------YGH----NPVRIVMDR-NHSLPQ 225
Cdd:PRK10786 165 SGESQWI--TSPQARRDVQRLRAQSHAILTSSATVLADDPALTVR-WseldaqtqalYPQenlrQPVRIVIDSqNRVTPE 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1745509151 226 TSHLSDNSVSTLVFT-EHPRSGKENLEYITL---NYQTDiLPQILSALYQRNLQSLMVEGGRILLESFIRSGIWDEVIIE 301
Cdd:PRK10786 242 HRIVQQPGETWLARTqEDSREWPETVRTLLLpehNGHLD-LVVLMMQLGKQQINSIWVEAGPTLAGALLQAGLVDELIVY 320
|
....*.
gi 1745509151 302 KSDKLL 307
Cdd:PRK10786 321 IAPKLL 326
|
|
| Riboflavin_deaminase-reductase |
cd01284 |
Riboflavin-specific deaminase. Riboflavin biosynthesis protein RibD ... |
1-115 |
2.68e-53 |
|
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: 170.88 E-value: 2.68e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1745509151 1 MRRCIQLAKNGLCNVSPNPMVGAVIVC-EGQIIGEGYHIRCGEAHAEVNAIRSVKDpSLLKHSTIYVSLEPCSHHGKTPP 79
Cdd:cd01284 1 MRRALELAEKGRGLTSPNPPVGCVIVDdDGEIVGEGYHRKAGGPHAEVNALASAGE-KLARGATLYVTLEPCSHHGKTPP 79
|
90 100 110
....*....|....*....|....*....|....*.
gi 1745509151 80 CADLIIEKQIPRIVIGCQDPFSKVAGKGIQKLRDAG 115
Cdd:cd01284 80 CVDAIIEAGIKRVVVGVRDPNPLVAGKGAERLRAAG 115
|
|
| RibD_C |
pfam01872 |
RibD C-terminal domain; The function of this domain is not known, but it is thought to be ... |
143-300 |
3.66e-31 |
|
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: 116.33 E-value: 3.66e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1745509151 143 PYIVLKWAESADGFIDLERTEGQPviLSTPLTSMLVHKKRAESDAIMVGTRTALLDNPALTVRNW----YGHNPVRIVMD 218
Cdd:pfam01872 1 PYVILKFAISLDGKIAAAGGSSQW--ITGEEARADVHQLRAEADAILVGRGTVRADNPSLTVRWVkgraAERQPPRVVVD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1745509151 219 RNHSLPQTSHLSDNSVSTLVFTEHPRSGKENLEYITLNYQtdiLPQILSALYQRNLQSLMVEGGRILLESFIRSGIWDEV 298
Cdd:pfam01872 79 STLRVPLDARVLNDDAPTLVATTEPADKEKVEKLKVLRVD---LKELLRELKERGIRSLLVEGGATLAGSLLRAGLVDEL 155
|
..
gi 1745509151 299 II 300
Cdd:pfam01872 156 RL 157
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| RibD1 |
COG0117 |
Riboflavin biosynthesis protein RibD, pyrimidine deaminase domain [Coenzyme transport and ... |
1-307 |
3.21e-122 |
|
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: 353.98 E-value: 3.21e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1745509151 1 MRRCIQLAKNGLCNVSPNPMVGAVIVCEGQIIGEGYHIRCGEAHAEVNAIRSVKDpsLLKHSTIYVSLEPCSHHGKTPPC 80
Cdd:COG0117 4 MRRALELARRGLGTTSPNPLVGCVIVKDGRIVGEGYHQRAGGPHAEVNALAQAGE--AARGATLYVTLEPCSHHGRTPPC 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1745509151 81 ADLIIEKQIPRIVIGCQDPFSKVAGKGIQKLRDAGCEVIVGVLEPECRELIRKFITFHTLHRPYIVLKWAESADGFIDLE 160
Cdd:COG0117 82 ADALIEAGIKRVVIAMLDPNPLVAGKGIARLRAAGIEVEVGVLEEEARALNRGFLKRMRTGRPFVTLKLAMSLDGKIATA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1745509151 161 RteGQPVILSTPLTSMLVHKKRAESDAIMVGTRTALLDNPALTVRNWYGHNPVRIVMDRNHSLPQTSHLSDNSVSTLVFT 240
Cdd:COG0117 162 N--GESQWITGEEARADVHRLRARSDAILVGIGTVLADDPSLTVRLPGGENPPRRVVVDDLLLRPPPALLLVANDAALII 239
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1745509151 241 EHPRSGKENLEYITLNYQTDILPQILSALYQRNLQSLMVEGGRILLESFIRSGIWDEVIIEKSDKLL 307
Cdd:COG0117 240 VTVTADAAAALAALAAEAGVVLLLVGGLLLLALLLLLLLLLLLLLLLLLLLGGGGGLAAAALLAALL 306
|
|
| eubact_ribD |
TIGR00326 |
riboflavin biosynthesis protein RibD; This model describes the ribD protein as found in ... |
1-314 |
3.13e-96 |
|
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: 289.04 E-value: 3.13e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1745509151 1 MRRCIQLAKNGLCNVSPNPMVGAVIVCEGQIIGEGYHIRCGEAHAEVNAIRSVKDPslLKHSTIYVSLEPCSHHGKTPPC 80
Cdd:TIGR00326 1 MNRALDLAKKGQGTTHPNPLVGCVIVKNGEIVGEGAHQKAGEPHAEVHALRQAGEN--AKGATAYVTLEPCSHQGRTPPC 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1745509151 81 ADLIIEKQIPRIVIGCQDPFSKVAGKGIQKLRDAGCEVIVGVLEPECRELIRKFITFHTLHRPYIVLKWAESADGFIDLE 160
Cdd:TIGR00326 79 AEAIIEAGIKKVVVSMQDPNPLVAGRGAERLKQAGIEVTFGILKEEAERLNKGFLKRMRTGLPYVQLKLAASLDGKIATA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1745509151 161 RTEGQpvILSTPLTSMLVHKKRAESDAIMVGTRTALLDNPALTVRnWYG--HNPVRIVMDRNHSLPQTSHLSDNSVSTLV 238
Cdd:TIGR00326 159 SGESK--WITSEAARTDAQQLRAQSDAILVGGGTVKADNPALTAR-LDEatEQPLRVVLDTQLRIPEFAKLIPQIAPTWI 235
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1745509151 239 FTEH--PRSGKENLEYITLNYQTDILPQILSALYQRNLQSLMVEGGRILLESFIRSGIWDEVIIEKSDKLLySGVKAP 314
Cdd:TIGR00326 236 FTTArdKKKRLEAFEVNIFPLEKVTIREVMTQLGKRGINSVLVEGGPNLLGSFLDEGLVDELIIYIAPKLL-GGTHAP 312
|
|
| ribD |
PRK10786 |
bifunctional diaminohydroxyphosphoribosylaminopyrimidine deaminase/5-amino-6- ... |
1-307 |
7.60e-66 |
|
bifunctional diaminohydroxyphosphoribosylaminopyrimidine deaminase/5-amino-6-(5-phosphoribosylamino)uracil reductase RibD;
Pssm-ID: 182729 [Multi-domain] Cd Length: 367 Bit Score: 211.93 E-value: 7.60e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1745509151 1 MRRCIQLAKNGLCNVSPNPMVGAVIVCEGQIIGEGYHIRCGEAHAEVNAIRSVKDPSllKHSTIYVSLEPCSHHGKTPPC 80
Cdd:PRK10786 7 MARALKLAQRGRFTTHPNPNVGCVIVKDGEIVGEGYHQRAGEPHAEVHALRMAGEKA--KGATAYVTLEPCSHHGRTPPC 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1745509151 81 ADLIIEKQIPRIVIGCQDPFSKVAGKGIQKLRDAGCEVIVGVLEPECRELIRKFITFHTLHRPYIVLKWAESADGFIDLE 160
Cdd:PRK10786 85 CDALIAAGVARVVAAMQDPNPQVAGRGLYRLQQAGIDVSHGLMMSEAEALNKGFLKRMRTGFPYIQLKLGASLDGRTAMA 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1745509151 161 RTEGQPVilSTPLTSMLVHKKRAESDAIMVGTRTALLDNPALTVRnW----------YGH----NPVRIVMDR-NHSLPQ 225
Cdd:PRK10786 165 SGESQWI--TSPQARRDVQRLRAQSHAILTSSATVLADDPALTVR-WseldaqtqalYPQenlrQPVRIVIDSqNRVTPE 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1745509151 226 TSHLSDNSVSTLVFT-EHPRSGKENLEYITL---NYQTDiLPQILSALYQRNLQSLMVEGGRILLESFIRSGIWDEVIIE 301
Cdd:PRK10786 242 HRIVQQPGETWLARTqEDSREWPETVRTLLLpehNGHLD-LVVLMMQLGKQQINSIWVEAGPTLAGALLQAGLVDELIVY 320
|
....*.
gi 1745509151 302 KSDKLL 307
Cdd:PRK10786 321 IAPKLL 326
|
|
| PLN02807 |
PLN02807 |
diaminohydroxyphosphoribosylaminopyrimidine deaminase |
1-299 |
4.88e-65 |
|
diaminohydroxyphosphoribosylaminopyrimidine deaminase
Pssm-ID: 215433 [Multi-domain] Cd Length: 380 Bit Score: 210.01 E-value: 4.88e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1745509151 1 MRRCIQLAKNGLCNVSPNPMVGAVIVCEGQIIGEGYHIRCGEAHAEVNAIRSVKDpsLLKHSTIYVSLEPCSHHGKTPPC 80
Cdd:PLN02807 36 MRRCVELARKAIGCTSPNPMVGCVIVKDGRIVGEGFHPKAGQPHAEVFALRDAGD--LAENATAYVSLEPCNHYGRTPPC 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1745509151 81 ADLIIEKQIPRIVIGCQDPFSKVAGKGIQKLRDAGCEVIVGVLEPECRELIRKFITFHTLHRPYIVLKWAESADGFIDLE 160
Cdd:PLN02807 114 TEALIKAKVKRVVVGMVDPNPIVASKGIERLRDAGIEVTVGVEEELCRKLNEAFIHRMLTGKPFVTLRYSMSMNGCLLNQ 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1745509151 161 RTEGQPVilSTPLTSMLVHkkraESDAIMVgTRTALLDNPALTVRNWYGHNPVRIVMDRNHSLP-QTSHLSDNSVS-TLV 238
Cdd:PLN02807 194 IGEGADD--AGGYYSQLLQ----EYDAVIL-SSALADADPLPLSQEAGAKQPLRIIIARSESSPlQIPSLREESAAkVLV 266
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1745509151 239 FT-----EHPRSGKENLEYITLNyQTDiLPQILSALYQRNLQSLMVE--GGRILLESFIRSGIWDEVI 299
Cdd:PLN02807 267 LAdkessAEPVLRRKGVEVVVLN-QIN-LDSILDLCYQRGLCSVLLDlrGNVGGLESLLKDALEDKLL 332
|
|
| RibD |
COG1985 |
Pyrimidine reductase, riboflavin biosynthesis [Coenzyme transport and metabolism]; Pyrimidine ... |
141-307 |
5.71e-55 |
|
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: 178.82 E-value: 5.71e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1745509151 141 HRPYIVLKWAESADGFIDLERteGQPVILSTPLTSMLVHKKRAESDAIMVGTRTALLDNPALTVRNW-YGHNPVRIVMDR 219
Cdd:COG1985 2 GRPYVTLKLAMSLDGKIATAD--GESKWITGEAARRDVHRLRARADAILVGAGTVLADDPSLTVRLPgLGRQPLRVVVDS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1745509151 220 NHSLPQTSHLSDNSVSTLVFTEH-------PRSGKENLEYITLNYQTDI-LPQILSALYQRNLQSLMVEGGRILLESFIR 291
Cdd:COG1985 80 SLRLPPDARLFDDAAPTLVLTTEaadaerrAALEAAGAEVIVLPGDGRVdLAALLAALAERGIRSVLVEGGPTLAGSFLA 159
|
170
....*....|....*.
gi 1745509151 292 SGIWDEVIIEKSDKLL 307
Cdd:COG1985 160 AGLVDELILYIAPKLL 175
|
|
| Riboflavin_deaminase-reductase |
cd01284 |
Riboflavin-specific deaminase. Riboflavin biosynthesis protein RibD ... |
1-115 |
2.68e-53 |
|
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: 170.88 E-value: 2.68e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1745509151 1 MRRCIQLAKNGLCNVSPNPMVGAVIVC-EGQIIGEGYHIRCGEAHAEVNAIRSVKDpSLLKHSTIYVSLEPCSHHGKTPP 79
Cdd:cd01284 1 MRRALELAEKGRGLTSPNPPVGCVIVDdDGEIVGEGYHRKAGGPHAEVNALASAGE-KLARGATLYVTLEPCSHHGKTPP 79
|
90 100 110
....*....|....*....|....*....|....*.
gi 1745509151 80 CADLIIEKQIPRIVIGCQDPFSKVAGKGIQKLRDAG 115
Cdd:cd01284 80 CVDAIIEAGIKRVVVGVRDPNPLVAGKGAERLRAAG 115
|
|
| ribD_Cterm |
TIGR00227 |
riboflavin-specific deaminase C-terminal domain; Eubacterial riboflavin-specific deaminases ... |
142-314 |
1.33e-31 |
|
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: 118.26 E-value: 1.33e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1745509151 142 RPYIVLKWAESADGFIDLERTEGQPVilSTPLTSMLVHKKRAESDAIMVGTRTALLDNPALTVRnW----YGHNPVRIVM 217
Cdd:TIGR00227 2 RPYVILKYAMSLDGKIATASGESSWI--TSEEARRDVHQLRAQSDAILVGSGTVLADDPRLTVR-WveldELRNPVRVVL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1745509151 218 DRNHSLPQTSHLSDNSVSTLVFTEHP--RSGKENL-----EYITLNYQTDILPQILSALYQRNLQSLMVEGGRILLESFI 290
Cdd:TIGR00227 79 DSRLRVPPTARLLNDDAPTWVATSEPadEEKVKELedfgvEVLVLETKRVDLKKLMEILYEEGIRSVMVEGGGTLNGSLL 158
|
170 180
....*....|....*....|....
gi 1745509151 291 RSGIWDEVIIEKSDKLLySGVKAP 314
Cdd:TIGR00227 159 KEGLVDELIVYIAPKLL-GGRDAP 181
|
|
| RibD_C |
pfam01872 |
RibD C-terminal domain; The function of this domain is not known, but it is thought to be ... |
143-300 |
3.66e-31 |
|
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: 116.33 E-value: 3.66e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1745509151 143 PYIVLKWAESADGFIDLERTEGQPviLSTPLTSMLVHKKRAESDAIMVGTRTALLDNPALTVRNW----YGHNPVRIVMD 218
Cdd:pfam01872 1 PYVILKFAISLDGKIAAAGGSSQW--ITGEEARADVHQLRAEADAILVGRGTVRADNPSLTVRWVkgraAERQPPRVVVD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1745509151 219 RNHSLPQTSHLSDNSVSTLVFTEHPRSGKENLEYITLNYQtdiLPQILSALYQRNLQSLMVEGGRILLESFIRSGIWDEV 298
Cdd:pfam01872 79 STLRVPLDARVLNDDAPTLVATTEPADKEKVEKLKVLRVD---LKELLRELKERGIRSLLVEGGATLAGSLLRAGLVDEL 155
|
..
gi 1745509151 299 II 300
Cdd:pfam01872 156 RL 157
|
|
| PRK05625 |
PRK05625 |
5-amino-6-(5-phosphoribosylamino)uracil reductase; Validated |
142-300 |
5.87e-28 |
|
5-amino-6-(5-phosphoribosylamino)uracil reductase; Validated
Pssm-ID: 180169 Cd Length: 217 Bit Score: 108.41 E-value: 5.87e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1745509151 142 RPYIVLKWAESADGFIDLERTEGQpviLSTPLTSMLVHKKRAESDAIMVGTRTALLDNPALTVRNWY---GHNPVRIVMD 218
Cdd:PRK05625 2 RPYVIVNAAMSADGKLATKTRYSR---ISGPEDFDRVHELRAEVDAVMVGIGTVLADDPSLTVHRYAagkPENPIRVVVD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1745509151 219 RNHSLPQTSHLSDNSVSTLVFTEH--PRSGKENLE------YITLNYQTDiLPQILSALYQRNLQSLMVEGGRILLESFI 290
Cdd:PRK05625 79 SSARTPPDARILDGPAKTIVAVSEaaPSEKVEELEkkgaevIVAGGERVD-LPDLLEDLYERGIKRLMVEGGGTLIWSMF 157
|
170
....*....|
gi 1745509151 291 RSGIWDEVII 300
Cdd:PRK05625 158 KEGLVDEVRV 167
|
|
| TadA |
COG0590 |
tRNA(Arg) A34 adenosine deaminase TadA [Translation, ribosomal structure and biogenesis]; tRNA ... |
1-135 |
8.93e-28 |
|
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: 105.59 E-value: 8.93e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1745509151 1 MRRCIQLAKNGLCN--VspnPmVGAVIVCEGQIIGEGYHIRCGE----AHAEVNAIR----SVKDPSlLKHSTIYVSLEP 70
Cdd:COG0590 8 MRRALELARKAVAEgeV---P-VGAVLVKDGEIIARGHNRVETLndptAHAEILAIRaaarKLGNWR-LSGCTLYVTLEP 82
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1745509151 71 CshhgktPPCADLIIEKQIPRIVIGCQDPFSKVAGKGIQKLRDA----GCEVIVGVLEPECRELIRKFI 135
Cdd:COG0590 83 C------PMCAGAIVWARIGRVVYGASDPKAGAAGSIYDLLADPrlnhRVEVVGGVLAEECAALLRDFF 145
|
|
| rib_reduct_arch |
TIGR01508 |
2,5-diamino-6-hydroxy-4-(5-phosphoribosylamino)pyrimidine 1'-reductase, archaeal; This model ... |
143-333 |
2.07e-27 |
|
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: 106.81 E-value: 2.07e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1745509151 143 PYIVLKWAESADGFIDLERTEgqpVILSTPLTSMLVHKKRAESDAIMVGTRTALLDNPALTVRnwYG---HNPVRIVMDR 219
Cdd:TIGR01508 1 PYVIVNVAMSLDGKLATINRD---SRISCEEDLIRVHEIRAEVDAIMVGIGTVLADDPRLTVK--KIksdRNPVRVVVDS 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1745509151 220 NHSLPQTSHLSDNSVSTLVFT------EHPRS-GKENLEYITLNYQTDILPQILSALYQRNLQSLMVEGGRILLESFIRS 292
Cdd:TIGR01508 76 KLRVPLNARILNKDAKTIIATsedepeEKVEElEDKGVEVVKFGEGRVDLKKLLDILYDKGVRRLMVEGGGTLIWSLFKE 155
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1745509151 293 GIWDEVIIEKSDKlLYSGVKAPEISDKISYSEEkhFCTTFR 333
Cdd:TIGR01508 156 NLVDEISVYIAPK-IFGGRDAPTYVDGEGFKTE--DCPKLE 193
|
|
| dCMP_cyt_deam_1 |
pfam00383 |
Cytidine and deoxycytidylate deaminase zinc-binding region; |
1-95 |
1.52e-18 |
|
Cytidine and deoxycytidylate deaminase zinc-binding region;
Pssm-ID: 395307 [Multi-domain] Cd Length: 100 Bit Score: 79.65 E-value: 1.52e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1745509151 1 MRRCIQLAKNGLCnvSPNPMVGAVIVCE-GQIIGEGYHIR-CG---EAHAEVNAIR---SVKDPSLLKHSTIYVSLEPCS 72
Cdd:pfam00383 6 MRLALKAAKRAYP--YSNFPVGAVIVKKdGEIIATGYNGEnAGydpTIHAERNAIRqagKRGEGVRLEGATLYVTLEPCG 83
|
90 100
....*....|....*....|...
gi 1745509151 73 HhgktppCADLIIEKQIPRIVIG 95
Cdd:pfam00383 84 M------CAQAIIESGIKRVVFG 100
|
|
| nucleoside_deaminase |
cd01285 |
Nucleoside deaminases include adenosine, guanine and cytosine deaminases. These enzymes are Zn ... |
1-100 |
7.37e-16 |
|
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: 72.26 E-value: 7.37e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1745509151 1 MRRCIQLAKNGLCNvSPNPmVGAVIVC-EGQIIGEGYHIRCGE----AHAEVNAIRSVKD---PSLLKHSTIYVSLEPCs 72
Cdd:cd01285 1 MRLAIELARKALAE-GEVP-FGAVIVDdDGKVIARGHNRVEQDgdptAHAEIVAIRNAARrlgSYLLSGCTLYTTLEPC- 77
|
90 100
....*....|....*....|....*...
gi 1745509151 73 hhgktPPCADLIIEKQIPRIVIGCQDPF 100
Cdd:cd01285 78 -----PMCAGALLWARIKRVVYGASDPK 100
|
|
| PRK10860 |
PRK10860 |
tRNA-specific adenosine deaminase; Provisional |
1-134 |
8.39e-15 |
|
tRNA-specific adenosine deaminase; Provisional
Pssm-ID: 182786 [Multi-domain] Cd Length: 172 Bit Score: 71.38 E-value: 8.39e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1745509151 1 MRRCIQLAKNGlcNVSPNPMVGAVIVCEGQIIGEGYHIRCGE----AHAEVNAIRS----VKDPSLLKhSTIYVSLEPCS 72
Cdd:PRK10860 17 MRHALTLAKRA--WDEREVPVGAVLVHNNRVIGEGWNRPIGRhdptAHAEIMALRQgglvLQNYRLLD-ATLYVTLEPCV 93
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1745509151 73 HhgktppCADLIIEKQIPRIVIGCQDPFSKVAGKGIQKLRDAG----CEVIVGVLEPECRELIRKF 134
Cdd:PRK10860 94 M------CAGAMVHSRIGRLVFGARDAKTGAAGSLMDVLHHPGmnhrVEITEGVLADECAALLSDF 153
|
|
| MafB19-deam |
pfam14437 |
MafB19-like deaminase; A member of the nucleic acid/nucleotide deaminase superfamily ... |
21-136 |
3.00e-14 |
|
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: 69.09 E-value: 3.00e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1745509151 21 VGAVIVCEGQIIGEGYHIRCGE----AHAEVNAI-RSVKD--PSLLKHSTIYVSLEPCshhgktPPCADLIIEKQIPRIV 93
Cdd:pfam14437 25 IGAVIVKDGKVIARGYNRKELNadttAHAEILAIqQAAKKlgSWRLDDATLYVTLEPC------PMCAGAIVQAGLKSLV 98
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 1745509151 94 IGCQDPFSKVAGKGIQKLRDAGCEVIVGVLEPECRELIRKFIT 136
Cdd:pfam14437 99 YGAGNPKGGAVGSVLNKLVIVLWNHRVELVEEDCSEILKGFFK 141
|
|
| PRK14719 |
PRK14719 |
bifunctional RNAse/5-amino-6-(5-phosphoribosylamino)uracil reductase; Provisional |
178-318 |
6.26e-12 |
|
bifunctional RNAse/5-amino-6-(5-phosphoribosylamino)uracil reductase; Provisional
Pssm-ID: 237801 [Multi-domain] Cd Length: 360 Bit Score: 65.73 E-value: 6.26e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1745509151 178 VHKKRAESDAIMVGTRTALLDNPALTVRNWYG---HNPVRIVMDRNHSLPQTSHLSDNSVSTLVFTEHPRSGKENLEYIT 254
Cdd:PRK14719 172 VHEIRKDVDAIMVGIGTVLKDDPRLTVHKINAspkDNPLRIVVDSNLKIPLNARVLNKDAKTVIATTTPISDEKEEKIRK 251
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1745509151 255 LN------YQTDI----LPQILSALYQRNLQSLMVEGGRILLESFIRSGIWDEVIIEKSDKlLYSGVKAPEISD 318
Cdd:PRK14719 252 LKemgitvLQAGVqkvdLRKIMNEIYKMGINKILLEGGGTLNWGMFKENLINEVRVYIAPK-VFGGANSPTYVD 324
|
|
| cytidine_deaminase-like |
cd00786 |
Cytidine and deoxycytidylate deaminase zinc-binding region. The family contains cytidine ... |
17-95 |
4.08e-11 |
|
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: 58.72 E-value: 4.08e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1745509151 17 PNPMVGAVIV--CEGQIIGEGYHIR----CGEAHAEVNAIRSVKDPSLLKHSTIYVSLEPCSHhgktppCADLIIE--KQ 88
Cdd:cd00786 16 SNFQVGACLVnkKDGGKVGRGCNIEnaaySMCNHAERTALFNAGSEGDTKGQMLYVALSPCGA------CAQLIIElgIK 89
|
....*..
gi 1745509151 89 IPRIVIG 95
Cdd:cd00786 90 DVIVVLT 96
|
|
| ComEB |
COG2131 |
Deoxycytidylate deaminase [Nucleotide transport and metabolism]; |
1-119 |
3.80e-10 |
|
Deoxycytidylate deaminase [Nucleotide transport and metabolism];
Pssm-ID: 441734 [Multi-domain] Cd Length: 154 Bit Score: 57.54 E-value: 3.80e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1745509151 1 MRRCIQLAKNGLCnvsPNPMVGAVIVCEGQIIGEGY--------------HIR-------------CGEAHAEVNAI-RS 52
Cdd:COG2131 13 MEIAKLVALRSTC---LRRQVGAVIVKDKRILATGYngapsglphcdevgCLReklgipsgergecCRTVHAEQNAIlQA 89
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1745509151 53 VKDPSLLKHSTIYVSLEPCSHhgktppCADLIIEKQIPRIVigCQDPFSKVAGKGIqkLRDAGCEVI 119
Cdd:COG2131 90 ARHGVSTEGATLYVTHFPCLE------CAKMIIQAGIKRVV--YLEDYPDELAKEL--LKEAGVEVR 146
|
|
| deoxycytidylate_deaminase |
cd01286 |
Deoxycytidylate deaminase domain. Deoxycytidylate deaminase catalyzes the deamination of dCMP ... |
21-93 |
1.33e-09 |
|
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: 55.74 E-value: 1.33e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1745509151 21 VGAVIVCEGQIIGEGY--------------HIRCGE-----------AHAEVNAI-RSVKDPSLLKHSTIYVSLEPCSHh 74
Cdd:cd01286 22 VGAVIVKDKRIISTGYngspsglphcaevgCERDDLpsgedqkccrtVHAEQNAIlQAARHGVSLEGATLYVTLFPCIE- 100
|
90
....*....|....*....
gi 1745509151 75 gktppCADLIIEKQIPRIV 93
Cdd:cd01286 101 -----CAKLIIQAGIKKVV 114
|
|
| cd |
PHA02588 |
deoxycytidylate deaminase; Provisional |
1-119 |
1.09e-07 |
|
deoxycytidylate deaminase; Provisional
Pssm-ID: 222894 [Multi-domain] Cd Length: 168 Bit Score: 50.91 E-value: 1.09e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1745509151 1 MRRCIQLAKNGLCnVSPNpmVGAVIVCEGQIIGEGYH------IRC------------------------------GEAH 44
Cdd:PHA02588 7 LQIAYLVSQESKC-VSWK--VGAVIEKNGRIISTGYNgtpaggVNCcdhaneqgwlddegklkkehrpehsawsskNEIH 83
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1745509151 45 AEVNAIRSV-KDPSLLKHSTIYVSLEPCshhgktPPCADLIIEKQIPRIVIGcqDPFSKVAGKGIQKLRDAGCEVI 119
Cdd:PHA02588 84 AELNAILFAaRNGISIEGATMYVTASPC------PDCAKAIAQSGIKKLVYC--EKYDRNGPGWDDILRKSGIEVI 151
|
|
| APOBEC_N |
pfam08210 |
APOBEC-like N-terminal domain; A mechanism of generating protein diversity is mRNA editing. ... |
43-118 |
3.94e-03 |
|
APOBEC-like N-terminal domain; A mechanism of generating protein diversity is mRNA editing. Members of this family are C-to-U editing enzymes. The N-terminal domain of APOBEC-1 like proteins is the catalytic domain, while the C-terminal domain is a pseudocatalyitc domain. More specifically, the catalytic domain is a zinc dependent deaminases domain and is essential for cytidine deamination.APOBEC-3 like members contain two copies of this domain. RNA editing by APOBEC-1 requires homodimerization and this complex interacts with RNA binding proteins to from the editosome (and references therein). This family also includes the functionally homologous activation induced deaminase (AID), which is essential for the development of antibody diversity in B lymphocytes, and the sea lamprey PmCDA1 and PmCDA2, which are predicted to play an AID-like role in the adaptive immune response of jawless vertebrates. Divergent members of this family are present in various eukaryotes such as Nematostella, C. elegans, Micromonas and Emiliania, and prokaryotes such as Wolbachia and Pseudomonas brassicacearum.
Pssm-ID: 462396 [Multi-domain] Cd Length: 170 Bit Score: 37.73 E-value: 3.94e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1745509151 43 AHAE---VNAIRS-VKDPSLLKHSTIYVSLEPCSHhgktppCADLIIE--KQIP----RIVIG----CQDPFSKvAGKGI 108
Cdd:pfam08210 46 LHAEerfLRWIHDlALDPGSNYEVTWYVSWSPCNE------CASELAAflSKHPnvrlRIFVSrlyyWEEPDYW-NREGL 118
|
90
....*....|
gi 1745509151 109 QKLRDAGCEV 118
Cdd:pfam08210 119 RSLAQAGVQL 128
|
|
| Inv-AAD |
pfam18785 |
Invertebrate-AID/APOBEC-deaminase; A classical AID/APOBEC-like deaminases found in ... |
22-135 |
8.79e-03 |
|
Invertebrate-AID/APOBEC-deaminase; A classical AID/APOBEC-like deaminases found in lophotrochozoans, echinoderms and cnidarians.
Pssm-ID: 408556 [Multi-domain] Cd Length: 129 Bit Score: 36.01 E-value: 8.79e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1745509151 22 GAVIVCE--GQIIGEGYHIRC-GEAHAE------VNAIRSVKDPSL---LKHSTI-YVSLEPCSHH--GKTPpCADLIIe 86
Cdd:pfam18785 1 GAVLVDAdtNEILSTGYTLELpGNTHAEqccfikLAEKHGVPEERLgevLPPNTVlYTTMEPCSKRlsGNLP-CVERIL- 78
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 1745509151 87 kqiprivigcqdpfskvagkgiqKLRDAGCEVIVGVLEPEcrelirKFI 135
Cdd:pfam18785 79 -----------------------RLKGAIKTVYVGVKEPE------KFV 98
|
|
| |
