|
Name |
Accession |
Description |
Interval |
E-value |
| RibD1 |
COG0117 |
Riboflavin biosynthesis protein RibD, pyrimidine deaminase domain [Coenzyme transport and ... |
5-310 |
2.32e-138 |
|
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: 395.97 E-value: 2.32e-138
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038578244 5 KYMKLAIKLAQKGAGYVNPNPMVGAVIVKDNHIIGQGYHEFFGGPHAERNALKNCRESPVGATLYVTLEPCCHFGKTPPC 84
Cdd:COG0117 2 RYMRRALELARRGLGTTSPNPLVGCVIVKDGRIVGEGYHQRAGGPHAEVNALAQAGEAARGATLYVTLEPCSHHGRTPPC 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038578244 85 IDAIIDSGITRVVIGSLDCNPIVSGKGVKILEENNLQVTVGILENECLNLIKSFRKYITQHVPYVFMKYAMSMDGKIATK 164
Cdd:COG0117 82 ADALIEAGIKRVVIAMLDPNPLVAGKGIARLRAAGIEVEVGVLEEEARALNRGFLKRMRTGRPFVTLKLAMSLDGKIATA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038578244 165 TNQSKWITEEEARKHVHQLRHYVSAIMVGVNTVIQDDPLLTCRLEEGKNPIRIICDTHLRTPLTSKIVKTANDIKTYIAT 244
Cdd:COG0117 162 NGESQWITGEEARADVHRLRARSDAILVGIGTVLADDPSLTVRLPGGENPPRRVVVDDLLLRPPPALLLVANDAALIIVT 241
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2038578244 245 SSEDKNKMKLYQNHGCEILSIKKKGN---HIDLSSLMQHLGNMQIDSLVLEGGSLMNWSALEQQIVDEL 310
Cdd:COG0117 242 VTADAAAALAALAAEAGVVLLLVGGLlllALLLLLLLLLLLLLLLLLLLGGGGGLAAAALLAALLLDLL 310
|
|
| eubact_ribD |
TIGR00326 |
riboflavin biosynthesis protein RibD; This model describes the ribD protein as found in ... |
7-354 |
3.52e-115 |
|
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: 338.34 E-value: 3.52e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038578244 7 MKLAIKLAQKGAGYVNPNPMVGAVIVKDNHIIGQGYHEFFGGPHAERNALKNCRESPVGATLYVTLEPCCHFGKTPPCID 86
Cdd:TIGR00326 1 MNRALDLAKKGQGTTHPNPLVGCVIVKNGEIVGEGAHQKAGEPHAEVHALRQAGENAKGATAYVTLEPCSHQGRTPPCAE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038578244 87 AIIDSGITRVVIGSLDCNPIVSGKGVKILEENNLQVTVGILENECLNLIKSFRKYITQHVPYVFMKYAMSMDGKIATKTN 166
Cdd:TIGR00326 81 AIIEAGIKKVVVSMQDPNPLVAGRGAERLKQAGIEVTFGILKEEAERLNKGFLKRMRTGLPYVQLKLAASLDGKIATASG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038578244 167 QSKWITEEEARKHVHQLRHYVSAIMVGVNTVIQDDPLLTCRLEEGKN-PIRIICDTHLRTPLTSKIVKTANdiKTYIATS 245
Cdd:TIGR00326 161 ESKWITSEAARTDAQQLRAQSDAILVGGGTVKADNPALTARLDEATEqPLRVVLDTQLRIPEFAKLIPQIA--PTWIFTT 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038578244 246 SEDKNKmklyQNHGCEILSIKKKgnHIDLSSLMQHLGNMQIDSLVLEGGSLMNWSALEQQIVDELKIYIAPKIFGGS-AK 324
Cdd:TIGR00326 239 ARDKKK----RLEAFEVNIFPLE--KVTIREVMTQLGKRGINSVLVEGGPNLLGSFLDEGLVDELIIYIAPKLLGGThAP 312
|
330 340 350
....*....|....*....|....*....|
gi 2038578244 325 FPVGGEGISLPNDAIRLKPYAFSQIGNDYL 354
Cdd:TIGR00326 313 GLCSEPGFQKMADALNFKFLEINQIGPDIL 342
|
|
| ribD |
PRK10786 |
bifunctional diaminohydroxyphosphoribosylaminopyrimidine deaminase/5-amino-6- ... |
1-352 |
4.79e-88 |
|
bifunctional diaminohydroxyphosphoribosylaminopyrimidine deaminase/5-amino-6-(5-phosphoribosylamino)uracil reductase RibD;
Pssm-ID: 182729 [Multi-domain] Cd Length: 367 Bit Score: 269.71 E-value: 4.79e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038578244 1 MSDSKYMKLAIKLAQKGAGYVNPNPMVGAVIVKDNHIIGQGYHEFFGGPHAERNALKNCRESPVGATLYVTLEPCCHFGK 80
Cdd:PRK10786 1 MQDEFYMARALKLAQRGRFTTHPNPNVGCVIVKDGEIVGEGYHQRAGEPHAEVHALRMAGEKAKGATAYVTLEPCSHHGR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038578244 81 TPPCIDAIIDSGITRVVIGSLDCNPIVSGKGVKILEENNLQVTVGILENECLNLIKSFRKYITQHVPYVFMKYAMSMDGK 160
Cdd:PRK10786 81 TPPCCDALIAAGVARVVAAMQDPNPQVAGRGLYRLQQAGIDVSHGLMMSEAEALNKGFLKRMRTGFPYIQLKLGASLDGR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038578244 161 IATKTNQSKWITEEEARKHVHQLRHYVSAIMVGVNTVIQDDPLLTCRLEE-------------GKNPIRIICDTHLRTPL 227
Cdd:PRK10786 161 TAMASGESQWITSPQARRDVQRLRAQSHAILTSSATVLADDPALTVRWSEldaqtqalypqenLRQPVRIVIDSQNRVTP 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038578244 228 TSKIVKTANDikTYIATSSEDKNKMKlyqnHGCEILSIKKKGNHIDLSSLMQHLGNMQIDSLVLEGGSLMNWSALEQQIV 307
Cdd:PRK10786 241 EHRIVQQPGE--TWLARTQEDSREWP----ETVRTLLLPEHNGHLDLVVLMMQLGKQQINSIWVEAGPTLAGALLQAGLV 314
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 2038578244 308 DELKIYIAPKIFGGSAKFPVGGEGISLPNDAIRLKPYAFSQIGND 352
Cdd:PRK10786 315 DELIVYIAPKLLGSDARGLCTLPGLEKLADAPQFKFSEIRHVGPD 359
|
|
| RibD_C |
pfam01872 |
RibD C-terminal domain; The function of this domain is not known, but it is thought to be ... |
147-355 |
2.51e-58 |
|
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: 187.59 E-value: 2.51e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038578244 147 PYVFMKYAMSMDGKIATKTNQSKWITEEEARKHVHQLRHYVSAIMVGVNTVIQDDPLLTCRLEEG----KNPIRIICDTH 222
Cdd:pfam01872 1 PYVILKFAISLDGKIAAAGGSSQWITGEEARADVHQLRAEADAILVGRGTVRADNPSLTVRWVKGraaeRQPPRVVVDST 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038578244 223 LRTPLTSKIVKTanDIKTYIATSSEDKNKMKlyqnhgceilsIKKKGNHIDLSSLMQHLGNMQIDSLVLEGGSLMNWSAL 302
Cdd:pfam01872 81 LRVPLDARVLND--DAPTLVATTEPADKEKV-----------EKLKVLRVDLKELLRELKERGIRSLLVEGGATLAGSLL 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2038578244 303 EQQIVDELKIYIAPKIFGGSAKFPVGGEGIslpnDAIRLKPYAFSQIGNDYLI 355
Cdd:pfam01872 148 RAGLVDELRLYIAPKLLGGGGRTLFGGEGF----LALKLKLVSSEAIGNGVVL 196
|
|
| Riboflavin_deaminase-reductase |
cd01284 |
Riboflavin-specific deaminase. Riboflavin biosynthesis protein RibD ... |
7-118 |
1.06e-57 |
|
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: 183.20 E-value: 1.06e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038578244 7 MKLAIKLAQKGAGYVNPNPMVGAVIVKDNH-IIGQGYHEFFGGPHAERNALKNCRE-SPVGATLYVTLEPCCHFGKTPPC 84
Cdd:cd01284 1 MRRALELAEKGRGLTSPNPPVGCVIVDDDGeIVGEGYHRKAGGPHAEVNALASAGEkLARGATLYVTLEPCSHHGKTPPC 80
|
90 100 110
....*....|....*....|....*....|....
gi 2038578244 85 IDAIIDSGITRVVIGSLDCNPIVSGKGVKILEEN 118
Cdd:cd01284 81 VDAIIEAGIKRVVVGVRDPNPLVAGKGAERLRAA 114
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| RibD1 |
COG0117 |
Riboflavin biosynthesis protein RibD, pyrimidine deaminase domain [Coenzyme transport and ... |
5-310 |
2.32e-138 |
|
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: 395.97 E-value: 2.32e-138
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038578244 5 KYMKLAIKLAQKGAGYVNPNPMVGAVIVKDNHIIGQGYHEFFGGPHAERNALKNCRESPVGATLYVTLEPCCHFGKTPPC 84
Cdd:COG0117 2 RYMRRALELARRGLGTTSPNPLVGCVIVKDGRIVGEGYHQRAGGPHAEVNALAQAGEAARGATLYVTLEPCSHHGRTPPC 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038578244 85 IDAIIDSGITRVVIGSLDCNPIVSGKGVKILEENNLQVTVGILENECLNLIKSFRKYITQHVPYVFMKYAMSMDGKIATK 164
Cdd:COG0117 82 ADALIEAGIKRVVIAMLDPNPLVAGKGIARLRAAGIEVEVGVLEEEARALNRGFLKRMRTGRPFVTLKLAMSLDGKIATA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038578244 165 TNQSKWITEEEARKHVHQLRHYVSAIMVGVNTVIQDDPLLTCRLEEGKNPIRIICDTHLRTPLTSKIVKTANDIKTYIAT 244
Cdd:COG0117 162 NGESQWITGEEARADVHRLRARSDAILVGIGTVLADDPSLTVRLPGGENPPRRVVVDDLLLRPPPALLLVANDAALIIVT 241
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2038578244 245 SSEDKNKMKLYQNHGCEILSIKKKGN---HIDLSSLMQHLGNMQIDSLVLEGGSLMNWSALEQQIVDEL 310
Cdd:COG0117 242 VTADAAAALAALAAEAGVVLLLVGGLlllALLLLLLLLLLLLLLLLLLLGGGGGLAAAALLAALLLDLL 310
|
|
| eubact_ribD |
TIGR00326 |
riboflavin biosynthesis protein RibD; This model describes the ribD protein as found in ... |
7-354 |
3.52e-115 |
|
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: 338.34 E-value: 3.52e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038578244 7 MKLAIKLAQKGAGYVNPNPMVGAVIVKDNHIIGQGYHEFFGGPHAERNALKNCRESPVGATLYVTLEPCCHFGKTPPCID 86
Cdd:TIGR00326 1 MNRALDLAKKGQGTTHPNPLVGCVIVKNGEIVGEGAHQKAGEPHAEVHALRQAGENAKGATAYVTLEPCSHQGRTPPCAE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038578244 87 AIIDSGITRVVIGSLDCNPIVSGKGVKILEENNLQVTVGILENECLNLIKSFRKYITQHVPYVFMKYAMSMDGKIATKTN 166
Cdd:TIGR00326 81 AIIEAGIKKVVVSMQDPNPLVAGRGAERLKQAGIEVTFGILKEEAERLNKGFLKRMRTGLPYVQLKLAASLDGKIATASG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038578244 167 QSKWITEEEARKHVHQLRHYVSAIMVGVNTVIQDDPLLTCRLEEGKN-PIRIICDTHLRTPLTSKIVKTANdiKTYIATS 245
Cdd:TIGR00326 161 ESKWITSEAARTDAQQLRAQSDAILVGGGTVKADNPALTARLDEATEqPLRVVLDTQLRIPEFAKLIPQIA--PTWIFTT 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038578244 246 SEDKNKmklyQNHGCEILSIKKKgnHIDLSSLMQHLGNMQIDSLVLEGGSLMNWSALEQQIVDELKIYIAPKIFGGS-AK 324
Cdd:TIGR00326 239 ARDKKK----RLEAFEVNIFPLE--KVTIREVMTQLGKRGINSVLVEGGPNLLGSFLDEGLVDELIIYIAPKLLGGThAP 312
|
330 340 350
....*....|....*....|....*....|
gi 2038578244 325 FPVGGEGISLPNDAIRLKPYAFSQIGNDYL 354
Cdd:TIGR00326 313 GLCSEPGFQKMADALNFKFLEINQIGPDIL 342
|
|
| ribD |
PRK10786 |
bifunctional diaminohydroxyphosphoribosylaminopyrimidine deaminase/5-amino-6- ... |
1-352 |
4.79e-88 |
|
bifunctional diaminohydroxyphosphoribosylaminopyrimidine deaminase/5-amino-6-(5-phosphoribosylamino)uracil reductase RibD;
Pssm-ID: 182729 [Multi-domain] Cd Length: 367 Bit Score: 269.71 E-value: 4.79e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038578244 1 MSDSKYMKLAIKLAQKGAGYVNPNPMVGAVIVKDNHIIGQGYHEFFGGPHAERNALKNCRESPVGATLYVTLEPCCHFGK 80
Cdd:PRK10786 1 MQDEFYMARALKLAQRGRFTTHPNPNVGCVIVKDGEIVGEGYHQRAGEPHAEVHALRMAGEKAKGATAYVTLEPCSHHGR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038578244 81 TPPCIDAIIDSGITRVVIGSLDCNPIVSGKGVKILEENNLQVTVGILENECLNLIKSFRKYITQHVPYVFMKYAMSMDGK 160
Cdd:PRK10786 81 TPPCCDALIAAGVARVVAAMQDPNPQVAGRGLYRLQQAGIDVSHGLMMSEAEALNKGFLKRMRTGFPYIQLKLGASLDGR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038578244 161 IATKTNQSKWITEEEARKHVHQLRHYVSAIMVGVNTVIQDDPLLTCRLEE-------------GKNPIRIICDTHLRTPL 227
Cdd:PRK10786 161 TAMASGESQWITSPQARRDVQRLRAQSHAILTSSATVLADDPALTVRWSEldaqtqalypqenLRQPVRIVIDSQNRVTP 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038578244 228 TSKIVKTANDikTYIATSSEDKNKMKlyqnHGCEILSIKKKGNHIDLSSLMQHLGNMQIDSLVLEGGSLMNWSALEQQIV 307
Cdd:PRK10786 241 EHRIVQQPGE--TWLARTQEDSREWP----ETVRTLLLPEHNGHLDLVVLMMQLGKQQINSIWVEAGPTLAGALLQAGLV 314
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 2038578244 308 DELKIYIAPKIFGGSAKFPVGGEGISLPNDAIRLKPYAFSQIGND 352
Cdd:PRK10786 315 DELIVYIAPKLLGSDARGLCTLPGLEKLADAPQFKFSEIRHVGPD 359
|
|
| RibD |
COG1985 |
Pyrimidine reductase, riboflavin biosynthesis [Coenzyme transport and metabolism]; Pyrimidine ... |
147-356 |
7.48e-85 |
|
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: 256.24 E-value: 7.48e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038578244 147 PYVFMKYAMSMDGKIATKTNQSKWITEEEARKHVHQLRHYVSAIMVGVNTVIQDDPLLTCRLE-EGKNPIRIICDTHLRT 225
Cdd:COG1985 4 PYVTLKLAMSLDGKIATADGESKWITGEAARRDVHRLRARADAILVGAGTVLADDPSLTVRLPgLGRQPLRVVVDSSLRL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038578244 226 PLTSKIVKTAndIKTYIATSSE-DKNKMKLYQNHGCEILSIKKKGnHIDLSSLMQHLGNMQIDSLVLEGGSLMNWSALEQ 304
Cdd:COG1985 84 PPDARLFDDA--APTLVLTTEAaDAERRAALEAAGAEVIVLPGDG-RVDLAALLAALAERGIRSVLVEGGPTLAGSFLAA 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2038578244 305 QIVDELKIYIAPKIFGGSAKFPVGGEGISLPNDAIRLKPYAFSQIGNDYLIE 356
Cdd:COG1985 161 GLVDELILYIAPKLLGGDGPTLVGGPGLETLADAPRLRLVSVRRLGDDLLLR 212
|
|
| ribD_Cterm |
TIGR00227 |
riboflavin-specific deaminase C-terminal domain; Eubacterial riboflavin-specific deaminases ... |
146-356 |
1.40e-71 |
|
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: 222.26 E-value: 1.40e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038578244 146 VPYVFMKYAMSMDGKIATKTNQSKWITEEEARKHVHQLRHYVSAIMVGVNTVIQDDPLLTCR---LEEGKNPIRIICDTH 222
Cdd:TIGR00227 2 RPYVILKYAMSLDGKIATASGESSWITSEEARRDVHQLRAQSDAILVGSGTVLADDPRLTVRwveLDELRNPVRVVLDSR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038578244 223 LRTPLTSKIVKTanDIKTYIATSSE-DKNKMKLYQNHGCEILSIKKKgnHIDLSSLMQHLGNMQIDSLVLEGGSLMNWSA 301
Cdd:TIGR00227 82 LRVPPTARLLND--DAPTWVATSEPaDEEKVKELEDFGVEVLVLETK--RVDLKKLMEILYEEGIRSVMVEGGGTLNGSL 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2038578244 302 LEQQIVDELKIYIAPKIFGG-SAKFPVGGEGISLPNDAIRLKPYAFSQIGNDYLIE 356
Cdd:TIGR00227 158 LKEGLVDELIVYIAPKLLGGrDAPTLVDGEGFQKMADAPNLELKEIYQIGEDIVLT 213
|
|
| PLN02807 |
PLN02807 |
diaminohydroxyphosphoribosylaminopyrimidine deaminase |
3-356 |
3.23e-61 |
|
diaminohydroxyphosphoribosylaminopyrimidine deaminase
Pssm-ID: 215433 [Multi-domain] Cd Length: 380 Bit Score: 201.15 E-value: 3.23e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038578244 3 DSKYMKLAIKLAQKGAGYVNPNPMVGAVIVKDNHIIGQGYHEFFGGPHAERNALKNCRESPVGATLYVTLEPCCHFGKTP 82
Cdd:PLN02807 32 DSFYMRRCVELARKAIGCTSPNPMVGCVIVKDGRIVGEGFHPKAGQPHAEVFALRDAGDLAENATAYVSLEPCNHYGRTP 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038578244 83 PCIDAIIDSGITRVVIGSLDCNPIVSGKGVKILEENNLQVTVGILENECLNLIKSFRKYITQHVPYVFMKYAMSMDGKIa 162
Cdd:PLN02807 112 PCTEALIKAKVKRVVVGMVDPNPIVASKGIERLRDAGIEVTVGVEEELCRKLNEAFIHRMLTGKPFVTLRYSMSMNGCL- 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038578244 163 tkTNQSKWITEEEARKHVHQLRHYVSAIMvgVNTVIQDDPLLTCRLEEGKNPIRIICDTHLRTPLTSKIVKTANDIKTYI 242
Cdd:PLN02807 191 --LNQIGEGADDAGGYYSQLLQEYDAVIL--SSALADADPLPLSQEAGAKQPLRIIIARSESSPLQIPSLREESAAKVLV 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038578244 243 ATSSEDKNKMKLYQNhGCEILSIkkkgNHIDLSSLMQHLGNMQIDSLVLE-----GG--SLMNwSALEQQIVDELKIYIA 315
Cdd:PLN02807 267 LADKESSAEPVLRRK-GVEVVVL----NQINLDSILDLCYQRGLCSVLLDlrgnvGGleSLLK-DALEDKLLQKVVVEVL 340
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 2038578244 316 PkIFGGSAKFPVGGEGISlpnDAIRLKPYAFSQIGNDYLIE 356
Cdd:PLN02807 341 P-FWSGSQGQSIASFGGS---QSFKLKRLTSREVGGSVVLE 377
|
|
| PRK05625 |
PRK05625 |
5-amino-6-(5-phosphoribosylamino)uracil reductase; Validated |
147-361 |
1.33e-60 |
|
5-amino-6-(5-phosphoribosylamino)uracil reductase; Validated
Pssm-ID: 180169 Cd Length: 217 Bit Score: 194.31 E-value: 1.33e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038578244 147 PYVFMKYAMSMDGKIATKTNQSKwITEEEARKHVHQLRHYVSAIMVGVNTVIQDDPLLT-CRLEEGK--NPIRIICDTHL 223
Cdd:PRK05625 3 PYVIVNAAMSADGKLATKTRYSR-ISGPEDFDRVHELRAEVDAVMVGIGTVLADDPSLTvHRYAAGKpeNPIRVVVDSSA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038578244 224 RTPLTSKIVKTanDIKTYIATS-SEDKNKMKLYQNHGCEIlsIKKKGNHIDLSSLMQHLGNMQIDSLVLEGGSLMNWSAL 302
Cdd:PRK05625 82 RTPPDARILDG--PAKTIVAVSeAAPSEKVEELEKKGAEV--IVAGGERVDLPDLLEDLYERGIKRLMVEGGGTLIWSMF 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038578244 303 EQQIVDELKIYIAPKIFGG-SAKFPVGGEGISLPNDAIRLKPYAFSQIGNDYLIESEVIY 361
Cdd:PRK05625 158 KEGLVDEVRVTVGPKIIGGkDAPTLADGEGFIEEEDPLKLELAKVCRCDEGVVLTYKVKK 217
|
|
| RibD_C |
pfam01872 |
RibD C-terminal domain; The function of this domain is not known, but it is thought to be ... |
147-355 |
2.51e-58 |
|
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: 187.59 E-value: 2.51e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038578244 147 PYVFMKYAMSMDGKIATKTNQSKWITEEEARKHVHQLRHYVSAIMVGVNTVIQDDPLLTCRLEEG----KNPIRIICDTH 222
Cdd:pfam01872 1 PYVILKFAISLDGKIAAAGGSSQWITGEEARADVHQLRAEADAILVGRGTVRADNPSLTVRWVKGraaeRQPPRVVVDST 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038578244 223 LRTPLTSKIVKTanDIKTYIATSSEDKNKMKlyqnhgceilsIKKKGNHIDLSSLMQHLGNMQIDSLVLEGGSLMNWSAL 302
Cdd:pfam01872 81 LRVPLDARVLND--DAPTLVATTEPADKEKV-----------EKLKVLRVDLKELLRELKERGIRSLLVEGGATLAGSLL 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2038578244 303 EQQIVDELKIYIAPKIFGGSAKFPVGGEGIslpnDAIRLKPYAFSQIGNDYLI 355
Cdd:pfam01872 148 RAGLVDELRLYIAPKLLGGGGRTLFGGEGF----LALKLKLVSSEAIGNGVVL 196
|
|
| Riboflavin_deaminase-reductase |
cd01284 |
Riboflavin-specific deaminase. Riboflavin biosynthesis protein RibD ... |
7-118 |
1.06e-57 |
|
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: 183.20 E-value: 1.06e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038578244 7 MKLAIKLAQKGAGYVNPNPMVGAVIVKDNH-IIGQGYHEFFGGPHAERNALKNCRE-SPVGATLYVTLEPCCHFGKTPPC 84
Cdd:cd01284 1 MRRALELAEKGRGLTSPNPPVGCVIVDDDGeIVGEGYHRKAGGPHAEVNALASAGEkLARGATLYVTLEPCSHHGKTPPC 80
|
90 100 110
....*....|....*....|....*....|....
gi 2038578244 85 IDAIIDSGITRVVIGSLDCNPIVSGKGVKILEEN 118
Cdd:cd01284 81 VDAIIEAGIKRVVVGVRDPNPLVAGKGAERLRAA 114
|
|
| rib_reduct_arch |
TIGR01508 |
2,5-diamino-6-hydroxy-4-(5-phosphoribosylamino)pyrimidine 1'-reductase, archaeal; This model ... |
147-359 |
2.55e-45 |
|
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: 154.58 E-value: 2.55e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038578244 147 PYVFMKYAMSMDGKIATKTNQSKwITEEEARKHVHQLRHYVSAIMVGVNTVIQDDPLLTCR-LEEGKNPIRIICDTHLRT 225
Cdd:TIGR01508 1 PYVIVNVAMSLDGKLATINRDSR-ISCEEDLIRVHEIRAEVDAIMVGIGTVLADDPRLTVKkIKSDRNPVRVVVDSKLRV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038578244 226 PLTSKIVKTanDIKTYIATSS-EDKNKMKLYQNHGCEIlsIKKKGNHIDLSSLMQHLGNMQIDSLVLEGGSLMNWSALEQ 304
Cdd:TIGR01508 80 PLNARILNK--DAKTIIATSEdEPEEKVEELEDKGVEV--VKFGEGRVDLKKLLDILYDKGVRRLMVEGGGTLIWSLFKE 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2038578244 305 QIVDELKIYIAPKIFGG-SAKFPVGGEGIsLPNDAIRLKPYAFSQIGNDYLIESEV 359
Cdd:TIGR01508 156 NLVDEISVYIAPKIFGGrDAPTYVDGEGF-KTEDCPKLELKNFYRLGEGIVLEFKV 210
|
|
| PRK14719 |
PRK14719 |
bifunctional RNAse/5-amino-6-(5-phosphoribosylamino)uracil reductase; Provisional |
135-360 |
4.26e-39 |
|
bifunctional RNAse/5-amino-6-(5-phosphoribosylamino)uracil reductase; Provisional
Pssm-ID: 237801 [Multi-domain] Cd Length: 360 Bit Score: 142.38 E-value: 4.26e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038578244 135 IKSFRKYITQHV-----------PYVFMKYAMSMDGKIATKTNQSKwITEEEARKHVHQLRHYVSAIMVGVNTVIQDDPL 203
Cdd:PRK14719 117 IESLYPYISRRIninsdlsdimlPYVISNVGMTLDGKLATIENDSR-ISGENDLKRVHEIRKDVDAIMVGIGTVLKDDPR 195
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038578244 204 LTCR---LEEGKNPIRIICDTHLRTPLTSKIVKTanDIKTYIAT----SSEDKNKMKLYQNHGceILSIKKKGNHIDLSS 276
Cdd:PRK14719 196 LTVHkinASPKDNPLRIVVDSNLKIPLNARVLNK--DAKTVIATttpiSDEKEEKIRKLKEMG--ITVLQAGVQKVDLRK 271
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038578244 277 LMQHLGNMQIDSLVLEGGSLMNWSALEQQIVDELKIYIAPKIFGGS-AKFPVGGEGISLPNDAIRLKPYAFSQIGNDYLI 355
Cdd:PRK14719 272 IMNEIYKMGINKILLEGGGTLNWGMFKENLINEVRVYIAPKVFGGAnSPTYVDGEGFKNVEECTKLELKNYYPLDDGIVL 351
|
....*
gi 2038578244 356 ESEVI 360
Cdd:PRK14719 352 EYRVI 356
|
|
| dCMP_cyt_deam_1 |
pfam00383 |
Cytidine and deoxycytidylate deaminase zinc-binding region; |
3-99 |
6.53e-25 |
|
Cytidine and deoxycytidylate deaminase zinc-binding region;
Pssm-ID: 395307 [Multi-domain] Cd Length: 100 Bit Score: 96.99 E-value: 6.53e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038578244 3 DSKYMKLAIKLAQKGAGYvnPNPMVGAVIVKDNH-IIGQGYHEFFGG----PHAERNALKNC-----RESPVGATLYVTL 72
Cdd:pfam00383 2 DEYFMRLALKAAKRAYPY--SNFPVGAVIVKKDGeIIATGYNGENAGydptIHAERNAIRQAgkrgeGVRLEGATLYVTL 79
|
90 100
....*....|....*....|....*..
gi 2038578244 73 EPCCHfgktppCIDAIIDSGITRVVIG 99
Cdd:pfam00383 80 EPCGM------CAQAIIESGIKRVVFG 100
|
|
| TadA |
COG0590 |
tRNA(Arg) A34 adenosine deaminase TadA [Translation, ribosomal structure and biogenesis]; tRNA ... |
1-138 |
1.11e-24 |
|
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: 97.88 E-value: 1.11e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038578244 1 MSDSKYMKLAIKLAQKG--AGYVnpnPmVGAVIVKDNHIIGQGY--HEFFGGP--HAERNALKN-CR----ESPVGATLY 69
Cdd:COG0590 2 EDDEEFMRRALELARKAvaEGEV---P-VGAVLVKDGEIIARGHnrVETLNDPtaHAEILAIRAaARklgnWRLSGCTLY 77
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2038578244 70 VTLEPCchfgktPPCIDAIIDSGITRVVIGSLDCNPIVSGKGVKILEENNL----QVTVGILENECLNLIKSF 138
Cdd:COG0590 78 VTLEPC------PMCAGAIVWARIGRVVYGASDPKAGAAGSIYDLLADPRLnhrvEVVGGVLAEECAALLRDF 144
|
|
| ComEB |
COG2131 |
Deoxycytidylate deaminase [Nucleotide transport and metabolism]; |
3-97 |
1.10e-16 |
|
Deoxycytidylate deaminase [Nucleotide transport and metabolism];
Pssm-ID: 441734 [Multi-domain] Cd Length: 154 Bit Score: 76.42 E-value: 1.10e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038578244 3 DSKYMKLAIKLAQKGAgyvNPNPMVGAVIVKDNHIIGQGY---------------------------HEFFGGPHAERNA 55
Cdd:COG2131 9 DEYFMEIAKLVALRST---CLRRQVGAVIVKDKRILATGYngapsglphcdevgclreklgipsgerGECCRTVHAEQNA 85
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 2038578244 56 LKNCR---ESPVGATLYVTLEPCchfgktPPCIDAIIDSGITRVV 97
Cdd:COG2131 86 ILQAArhgVSTEGATLYVTHFPC------LECAKMIIQAGIKRVV 124
|
|
| MafB19-deam |
pfam14437 |
MafB19-like deaminase; A member of the nucleic acid/nucleotide deaminase superfamily ... |
1-140 |
5.41e-16 |
|
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: 74.10 E-value: 5.41e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038578244 1 MSDSKYMKLAIKLAQKGAGyVNPNPmVGAVIVKDNHIIGQGYHEFFG----GPHAERNAL-----KNCRESPVGATLYVT 71
Cdd:pfam14437 1 ENHEKWFRKALGLAEKAYD-AGEVP-IGAVIVKDGKVIARGYNRKELnadtTAHAEILAIqqaakKLGSWRLDDATLYVT 78
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2038578244 72 LEPCchfgktPPCIDAIIDSGITRVVIGSLDCNPIVSGKGVKILEENNLQVTVGILENECLNLIKSFRK 140
Cdd:pfam14437 79 LEPC------PMCAGAIVQAGLKSLVYGAGNPKGGAVGSVLNKLVIVLWNHRVELVEEDCSEILKGFFK 141
|
|
| deoxycytidylate_deaminase |
cd01286 |
Deoxycytidylate deaminase domain. Deoxycytidylate deaminase catalyzes the deamination of dCMP ... |
3-97 |
4.24e-15 |
|
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: 71.15 E-value: 4.24e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038578244 3 DSKYMKLAIKLAQKGAgyvNPNPMVGAVIVKDNHIIGQGY--------HEFFGGP-----------------HAERNALK 57
Cdd:cd01286 1 DEYFMAIARLAALRST---CPRRQVGAVIVKDKRIISTGYngspsglpHCAEVGCerddlpsgedqkccrtvHAEQNAIL 77
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 2038578244 58 NCR---ESPVGATLYVTLEPCchfgktPPCIDAIIDSGITRVV 97
Cdd:cd01286 78 QAArhgVSLEGATLYVTLFPC------IECAKLIIQAGIKKVV 114
|
|
| PRK10860 |
PRK10860 |
tRNA-specific adenosine deaminase; Provisional |
2-138 |
1.91e-14 |
|
tRNA-specific adenosine deaminase; Provisional
Pssm-ID: 182786 [Multi-domain] Cd Length: 172 Bit Score: 70.61 E-value: 1.91e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038578244 2 SDSKYMKLAIKLAQKG--AGYVnpnPmVGAVIVKDNHIIGQGYHEFFG----GPHAERNALK-------NCREspVGATL 68
Cdd:PRK10860 12 SHEYWMRHALTLAKRAwdEREV---P-VGAVLVHNNRVIGEGWNRPIGrhdpTAHAEIMALRqgglvlqNYRL--LDATL 85
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2038578244 69 YVTLEPCCHfgktppCIDAIIDSGITRVVIGSLDCNPIVSGKGVKILEE----NNLQVTVGILENECLNLIKSF 138
Cdd:PRK10860 86 YVTLEPCVM------CAGAMVHSRIGRLVFGARDAKTGAAGSLMDVLHHpgmnHRVEITEGVLADECAALLSDF 153
|
|
| cytidine_deaminase-like |
cd00786 |
Cytidine and deoxycytidylate deaminase zinc-binding region. The family contains cytidine ... |
7-98 |
3.47e-13 |
|
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: 64.88 E-value: 3.47e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038578244 7 MKLAIKLAQKGAgYVNPNPMVGAVIV--KDNHIIGQGYH-EFFGGP---HAERNALKNC--RESPVGATLYVTLEPCCHf 78
Cdd:cd00786 1 MTEALKAADLGY-AKESNFQVGACLVnkKDGGKVGRGCNiENAAYSmcnHAERTALFNAgsEGDTKGQMLYVALSPCGA- 78
|
90 100
....*....|....*....|
gi 2038578244 79 gktppCIDAIIDSGITRVVI 98
Cdd:cd00786 79 -----CAQLIIELGIKDVIV 93
|
|
| nucleoside_deaminase |
cd01285 |
Nucleoside deaminases include adenosine, guanine and cytosine deaminases. These enzymes are Zn ... |
7-99 |
6.63e-12 |
|
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: 61.48 E-value: 6.63e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038578244 7 MKLAIKLAQKGAGYVNpNPmVGAVIVKDNH-IIGQGYHEF--FGGP--HAERNALKNC-----RESPVGATLYVTLEPCc 76
Cdd:cd01285 1 MRLAIELARKALAEGE-VP-FGAVIVDDDGkVIARGHNRVeqDGDPtaHAEIVAIRNAarrlgSYLLSGCTLYTTLEPC- 77
|
90 100
....*....|....*....|...
gi 2038578244 77 hfgktPPCIDAIIDSGITRVVIG 99
Cdd:cd01285 78 -----PMCAGALLWARIKRVVYG 95
|
|
| cd |
PHA02588 |
deoxycytidylate deaminase; Provisional |
1-101 |
1.49e-09 |
|
deoxycytidylate deaminase; Provisional
Pssm-ID: 222894 [Multi-domain] Cd Length: 168 Bit Score: 56.30 E-value: 1.49e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038578244 1 MSDSKYMKLAIKLAQKGAGYVNpnpMVGAVIVKDNHIIGQGY------------HEFFGGP------------------- 49
Cdd:PHA02588 1 MKDSTYLQIAYLVSQESKCVSW---KVGAVIEKNGRIISTGYngtpaggvnccdHANEQGWlddegklkkehrpehsaws 77
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038578244 50 -----HAERNAL---KNCRESPVGATLYVTLEPCchfgktPPCIDAIIDSGITRVVIGSL 101
Cdd:PHA02588 78 skneiHAELNAIlfaARNGISIEGATMYVTASPC------PDCAKAIAQSGIKKLVYCEK 131
|
|
| |
