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Conserved domains on  [gi|19075322|ref|NP_587822|]
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bifunctional CMP deaminase family methyltransferase/riboflavin-specific deaminase [Schizosaccharomyces pombe]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Riboflavin_deaminase-reductase cd01284
Riboflavin-specific deaminase. Riboflavin biosynthesis protein RibD ...
 262-380 1.95e-42

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: 144.68  E-value: 1.95e-42
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075322 262 MLKALNEAKKCE-PTDSAFCVGAVIVQ-NGKIVSTGYSReRPGNTHAEECAIEKFMLKNptdsLEGAIMYSTMEPCSKRL 339
Cdd:cd01284   1 MRRALELAEKGRgLTSPNPPVGCVIVDdDGEIVGEGYHR-KAGGPHAEVNALASAGEKL----ARGATLYVTLEPCSHHG 75

                        90       100       110       120
                ....*....|....*....|....*....|....*....|.
gi 19075322 340 sKKVSCTDLIVKQKFSTVVLGSLEPDIFVKCEGVDLLKKAG 380
Cdd:cd01284  76 -KTPPCVDAIIEAGIKRVVVGVRDPNPLVAGKGAERLRAAG 115
AdoMet_MTases super family cl17173
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 57-218 2.55e-10

S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; AdoMet-MTases are enzymes that use S-adenosyl-L-methionine (SAM or AdoMet) as a substrate for methyltransfer, creating the product S-adenosyl-L-homocysteine (AdoHcy). There are at least five structurally distinct families of AdoMet-MTases, class I being the largest and most diverse. Within this class enzymes can be classified by different substrate specificities (small molecules, lipids, nucleic acids, etc.) and different target atoms for methylation (nitrogen, oxygen, carbon, sulfur, etc.).


The actual alignment was detected with superfamily member pfam10294:

Pssm-ID: 473071  Cd Length: 172  Bit Score: 58.88  E-value: 2.55e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075322    57 LQSLHQSRGSTGSVLWKTSVKVVPWLLQQSWFM---NSLTPKtSILELGSGiSGLAGI----LLSPfvGNYVASDkqlyL 129
Cdd:pfam10294   7 LRIEEDTGNGIGGHVWDAAVVLSKYLEMKIFKElgaNNLSGL-NVLELGSG-TGLVGIavalLLPG--ASVTITD----L 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075322   130 KKIRENLDQN-----NASDVEVHELDWKSTPYPKDWTFDFLDYVLFFDCIYNPHLNAHLVSCLASLAERYPgmQCLFAQE 204
Cdd:pfam10294  79 EEALELLKKNielnaLSSKVVVKVLDWGENLPPDLFDGHPVDLILAADCVYNEDSFPLLEKTLKDLLGKES--VILVAYK 156

                         170
                  ....*....|....*
gi 19075322   205 LR-DQETlvDFLERV 218
Cdd:pfam10294 157 KRrEAEK--KFFKLL 169
 
Name Accession Description Interval E-value
Riboflavin_deaminase-reductase cd01284
Riboflavin-specific deaminase. Riboflavin biosynthesis protein RibD ...
 262-380 1.95e-42

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: 144.68  E-value: 1.95e-42
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075322 262 MLKALNEAKKCE-PTDSAFCVGAVIVQ-NGKIVSTGYSReRPGNTHAEECAIEKFMLKNptdsLEGAIMYSTMEPCSKRL 339
Cdd:cd01284   1 MRRALELAEKGRgLTSPNPPVGCVIVDdDGEIVGEGYHR-KAGGPHAEVNALASAGEKL----ARGATLYVTLEPCSHHG 75

                        90       100       110       120
                ....*....|....*....|....*....|....*....|.
gi 19075322 340 sKKVSCTDLIVKQKFSTVVLGSLEPDIFVKCEGVDLLKKAG 380
Cdd:cd01284  76 -KTPPCVDAIIEAGIKRVVVGVRDPNPLVAGKGAERLRAAG 115
Inv-AAD pfam18785
Invertebrate-AID/APOBEC-deaminase; A classical AID/APOBEC-like deaminases found in ...
 282-397 9.62e-30

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: 111.51  E-value: 9.62e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075322   282 GAVIV--QNGKIVSTGYSRERPGNTHAEECAIEKF-------------MLKNPTdslegaIMYSTMEPCSKRLSKKVSCT 346
Cdd:pfam18785   1 GAVLVdaDTNEILSTGYTLELPGNTHAEQCCFIKLaekhgvpeerlgeVLPPNT------VLYTTMEPCSKRLSGNLPCV 74

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 19075322   347 DLIVKQK--FSTVVLGSLEPDIFVKC-EGVDLLKKAGIVVIEKLTFQDDCLREA 397
Cdd:pfam18785  75 ERILRLKgaIKTVYVGVKEPEKFVGEnTGRKRLEDAGIEVVHVEGLEDEILEVA 128
RibD1 COG0117
Riboflavin biosynthesis protein RibD, pyrimidine deaminase domain [Coenzyme transport and ...
 259-385 5.80e-28

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: 112.07  E-value: 5.80e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075322 259 EEYMLKALNEAKKCEPTDSA-FCVGAVIVQNGKIVSTGYSReRPGNTHAEECAIEKFmlknpTDSLEGAIMYSTMEPCSK 337
Cdd:COG0117   1 ERYMRRALELARRGLGTTSPnPLVGCVIVKDGRIVGEGYHQ-RAGGPHAEVNALAQA-----GEAARGATLYVTLEPCSH 74

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*...
gi 19075322 338 RlSKKVSCTDLIVKQKFSTVVLGSLEPDIFVKCEGVDLLKKAGIVVIE 385
Cdd:COG0117  75 H-GRTPPCADALIEAGIKRVVIAMLDPNPLVAGKGIARLRAAGIEVEV 121
eubact_ribD TIGR00326
riboflavin biosynthesis protein RibD; This model describes the ribD protein as found in ...
 262-383 1.38e-17

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: 83.34  E-value: 1.38e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075322   262 MLKALNEAKKCE-PTDSAFCVGAVIVQNGKIVSTGYSrERPGNTHAEECAiekfmLKNPTDSLEGAIMYSTMEPCSKRlS 340
Cdd:TIGR00326   1 MNRALDLAKKGQgTTHPNPLVGCVIVKNGEIVGEGAH-QKAGEPHAEVHA-----LRQAGENAKGATAYVTLEPCSHQ-G 73

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 19075322   341 KKVSCTDLIVKQKFSTVVLGSLEPDIFVKCEGVDLLKKAGIVV 383
Cdd:TIGR00326  74 RTPPCAEAIIEAGIKKVVVSMQDPNPLVAGRGAERLKQAGIEV 116
PLN02807 PLN02807
diaminohydroxyphosphoribosylaminopyrimidine deaminase
 281-383 1.08e-12

diaminohydroxyphosphoribosylaminopyrimidine deaminase


Pssm-ID: 215433 [Multi-domain]  Cd Length: 380  Bit Score: 69.03  E-value: 1.08e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075322  281 VGAVIVQNGKIVSTGYsRERPGNTHAEecaieKFMLKNPTDSLEGAIMYSTMEPCSkRLSKKVSCTDLIVKQKFSTVVLG 360
Cdd:PLN02807  56 VGCVIVKDGRIVGEGF-HPKAGQPHAE-----VFALRDAGDLAENATAYVSLEPCN-HYGRTPPCTEALIKAKVKRVVVG 128

                         90       100
                 ....*....|....*....|...
gi 19075322  361 SLEPDIFVKCEGVDLLKKAGIVV 383
Cdd:PLN02807 129 MVDPNPIVASKGIERLRDAGIEV 151
Methyltransf_16 pfam10294
Lysine methyltransferase; Methyltrans_16 is a lysine methyltransferase. characterized members ...
 57-218 2.55e-10

Lysine methyltransferase; Methyltrans_16 is a lysine methyltransferase. characterized members of this family are protein methyltransferases targetting Lys residues in specific proteins, including calmodulin, VCP, Kin17 and Hsp70 proteins.


Pssm-ID: 313513  Cd Length: 172  Bit Score: 58.88  E-value: 2.55e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075322    57 LQSLHQSRGSTGSVLWKTSVKVVPWLLQQSWFM---NSLTPKtSILELGSGiSGLAGI----LLSPfvGNYVASDkqlyL 129
Cdd:pfam10294   7 LRIEEDTGNGIGGHVWDAAVVLSKYLEMKIFKElgaNNLSGL-NVLELGSG-TGLVGIavalLLPG--ASVTITD----L 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075322   130 KKIRENLDQN-----NASDVEVHELDWKSTPYPKDWTFDFLDYVLFFDCIYNPHLNAHLVSCLASLAERYPgmQCLFAQE 204
Cdd:pfam10294  79 EEALELLKKNielnaLSSKVVVKVLDWGENLPPDLFDGHPVDLILAADCVYNEDSFPLLEKTLKDLLGKES--VILVAYK 156

                         170
                  ....*....|....*
gi 19075322   205 LR-DQETlvDFLERV 218
Cdd:pfam10294 157 KRrEAEK--KFFKLL 169
SmtA COG0500
SAM-dependent methyltransferase [Secondary metabolites biosynthesis, transport and catabolism, ...
 80-213 1.59e-05

SAM-dependent methyltransferase [Secondary metabolites biosynthesis, transport and catabolism, General function prediction only];


Pssm-ID: 440266 [Multi-domain]  Cd Length: 199  Bit Score: 45.29  E-value: 1.59e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075322  80 PWLLQQSWFMNSLTPKTSILELGSGISGLAGILLSPFVGNYVASD-KQLYLKKIRENLDQNNASDVEVHELDWKSTPYPK 158
Cdd:COG0500  12 PGLAALLALLERLPKGGRVLDLGCGTGRNLLALAARFGGRVIGIDlSPEAIALARARAAKAGLGNVEFLVADLAELDPLP 91

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 19075322 159 DWTFDFldyVLFFDCIY--NPHLNAHLVSCLASLAEryPG----MQCLFAQELRDQETLVD 213
Cdd:COG0500  92 AESFDL---VVAFGVLHhlPPEEREALLRELARALK--PGgvllLSASDAAAALSLARLLL 147
 
Name Accession Description Interval E-value
Riboflavin_deaminase-reductase cd01284
Riboflavin-specific deaminase. Riboflavin biosynthesis protein RibD ...
 262-380 1.95e-42

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: 144.68  E-value: 1.95e-42
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075322 262 MLKALNEAKKCE-PTDSAFCVGAVIVQ-NGKIVSTGYSReRPGNTHAEECAIEKFMLKNptdsLEGAIMYSTMEPCSKRL 339
Cdd:cd01284   1 MRRALELAEKGRgLTSPNPPVGCVIVDdDGEIVGEGYHR-KAGGPHAEVNALASAGEKL----ARGATLYVTLEPCSHHG 75

                        90       100       110       120
                ....*....|....*....|....*....|....*....|.
gi 19075322 340 sKKVSCTDLIVKQKFSTVVLGSLEPDIFVKCEGVDLLKKAG 380
Cdd:cd01284  76 -KTPPCVDAIIEAGIKRVVVGVRDPNPLVAGKGAERLRAAG 115
Inv-AAD pfam18785
Invertebrate-AID/APOBEC-deaminase; A classical AID/APOBEC-like deaminases found in ...
 282-397 9.62e-30

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: 111.51  E-value: 9.62e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075322   282 GAVIV--QNGKIVSTGYSRERPGNTHAEECAIEKF-------------MLKNPTdslegaIMYSTMEPCSKRLSKKVSCT 346
Cdd:pfam18785   1 GAVLVdaDTNEILSTGYTLELPGNTHAEQCCFIKLaekhgvpeerlgeVLPPNT------VLYTTMEPCSKRLSGNLPCV 74

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 19075322   347 DLIVKQK--FSTVVLGSLEPDIFVKC-EGVDLLKKAGIVVIEKLTFQDDCLREA 397
Cdd:pfam18785  75 ERILRLKgaIKTVYVGVKEPEKFVGEnTGRKRLEDAGIEVVHVEGLEDEILEVA 128
RibD1 COG0117
Riboflavin biosynthesis protein RibD, pyrimidine deaminase domain [Coenzyme transport and ...
 259-385 5.80e-28

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: 112.07  E-value: 5.80e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075322 259 EEYMLKALNEAKKCEPTDSA-FCVGAVIVQNGKIVSTGYSReRPGNTHAEECAIEKFmlknpTDSLEGAIMYSTMEPCSK 337
Cdd:COG0117   1 ERYMRRALELARRGLGTTSPnPLVGCVIVKDGRIVGEGYHQ-RAGGPHAEVNALAQA-----GEAARGATLYVTLEPCSH 74

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*...
gi 19075322 338 RlSKKVSCTDLIVKQKFSTVVLGSLEPDIFVKCEGVDLLKKAGIVVIE 385
Cdd:COG0117  75 H-GRTPPCADALIEAGIKRVVIAMLDPNPLVAGKGIARLRAAGIEVEV 121
dCMP_cyt_deam_1 pfam00383
Cytidine and deoxycytidylate deaminase zinc-binding region;
257-360 1.36e-27

Cytidine and deoxycytidylate deaminase zinc-binding region;


Pssm-ID: 395307 [Multi-domain]  Cd Length: 100  Bit Score: 105.08  E-value: 1.36e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075322   257 NHEEYMLKALNEAKKCEPtDSAFCVGAVIV-QNGKIVSTGYSRERPGNT---HAEECAIEKFMLKNPTDSLEGAIMYSTM 332
Cdd:pfam00383   1 WDEYFMRLALKAAKRAYP-YSNFPVGAVIVkKDGEIIATGYNGENAGYDptiHAERNAIRQAGKRGEGVRLEGATLYVTL 79

                          90       100
                  ....*....|....*....|....*...
gi 19075322   333 EPCSkrlskkvSCTDLIVKQKFSTVVLG 360
Cdd:pfam00383  80 EPCG-------MCAQAIIESGIKRVVFG 100
eubact_ribD TIGR00326
riboflavin biosynthesis protein RibD; This model describes the ribD protein as found in ...
 262-383 1.38e-17

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: 83.34  E-value: 1.38e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075322   262 MLKALNEAKKCE-PTDSAFCVGAVIVQNGKIVSTGYSrERPGNTHAEECAiekfmLKNPTDSLEGAIMYSTMEPCSKRlS 340
Cdd:TIGR00326   1 MNRALDLAKKGQgTTHPNPLVGCVIVKNGEIVGEGAH-QKAGEPHAEVHA-----LRQAGENAKGATAYVTLEPCSHQ-G 73

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 19075322   341 KKVSCTDLIVKQKFSTVVLGSLEPDIFVKCEGVDLLKKAGIVV 383
Cdd:TIGR00326  74 RTPPCAEAIIEAGIKKVVVSMQDPNPLVAGRGAERLKQAGIEV 116
TadA COG0590
tRNA(Arg) A34 adenosine deaminase TadA [Translation, ribosomal structure and biogenesis]; tRNA ...
 257-335 5.50e-14

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: 68.99  E-value: 5.50e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075322 257 NHEEYMLKALNEAKKCE-----PtdsafcVGAVIVQNGKIVSTGYSRERPGN---THAEECAIEKF--MLKNPtdSLEGA 326
Cdd:COG0590   3 DDEEFMRRALELARKAVaegevP------VGAVLVKDGEIIARGHNRVETLNdptAHAEILAIRAAarKLGNW--RLSGC 74


                ....*....
gi 19075322 327 IMYSTMEPC 335
Cdd:COG0590  75 TLYVTLEPC 83
PLN02807 PLN02807
diaminohydroxyphosphoribosylaminopyrimidine deaminase
 281-383 1.08e-12

diaminohydroxyphosphoribosylaminopyrimidine deaminase


Pssm-ID: 215433 [Multi-domain]  Cd Length: 380  Bit Score: 69.03  E-value: 1.08e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075322  281 VGAVIVQNGKIVSTGYsRERPGNTHAEecaieKFMLKNPTDSLEGAIMYSTMEPCSkRLSKKVSCTDLIVKQKFSTVVLG 360
Cdd:PLN02807  56 VGCVIVKDGRIVGEGF-HPKAGQPHAE-----VFALRDAGDLAENATAYVSLEPCN-HYGRTPPCTEALIKAKVKRVVVG 128

                         90       100
                 ....*....|....*....|...
gi 19075322  361 SLEPDIFVKCEGVDLLKKAGIVV 383
Cdd:PLN02807 129 MVDPNPIVASKGIERLRDAGIEV 151
ComEB COG2131
Deoxycytidylate deaminase [Nucleotide transport and metabolism];
253-392 6.46e-12

Deoxycytidylate deaminase [Nucleotide transport and metabolism];


Pssm-ID: 441734 [Multi-domain]  Cd Length: 154  Bit Score: 62.94  E-value: 6.46e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075322 253 MKPYNHEEYMLKALNEAKKCepTDSAFCVGAVIVQNGKIVSTGYSRERPGNTHAEE--CAIEKFMLKNPTD--------- 321
Cdd:COG2131   4 ERPSWDEYFMEIAKLVALRS--TCLRRQVGAVIVKDKRILATGYNGAPSGLPHCDEvgCLREKLGIPSGERgeccrtvha 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075322 322 -------------SLEGAIMYSTMEPCskrlskkVSCTDLIVKQKFSTVVLGSLEPDIfvkcEGVDLLKKAGIVViEKLT 388
Cdd:COG2131  82 eqnailqaarhgvSTEGATLYVTHFPC-------LECAKMIIQAGIKRVVYLEDYPDE----LAKELLKEAGVEV-RQLE 149


                ....
gi 19075322 389 FQDD 392
Cdd:COG2131 150 LEEE 153
MafB19-deam pfam14437
MafB19-like deaminase; A member of the nucleic acid/nucleotide deaminase superfamily ...
 257-390 2.02e-11

MafB19-like deaminase; A member of the nucleic acid/nucleotide deaminase superfamily prototyped by Neisseria MafB19. Members of this family are present in a wide phyletic range of bacteria and are predicted to function as toxins in bacterial polymorphic toxin systems.


Pssm-ID: 433953 [Multi-domain]  Cd Length: 144  Bit Score: 61.38  E-value: 2.02e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075322   257 NHEEYMLKALNEAKKCEPTDSAfCVGAVIVQNGKIVSTGYSReRPGN----THAEECAIEKFMLKNPTDSLEGAIMYSTM 332
Cdd:pfam14437   2 NHEKWFRKALGLAEKAYDAGEV-PIGAVIVKDGKVIARGYNR-KELNadttAHAEILAIQQAAKKLGSWRLDDATLYVTL 79

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075322   333 EPCSkrlskkvSCTDLIVKQKFSTVVLGSLEPdifvkcegvdllkKAGIV--VIEKLTFQ 390
Cdd:pfam14437  80 EPCP-------MCAGAIVQAGLKSLVYGAGNP-------------KGGAVgsVLNKLVIV 119
Methyltransf_16 pfam10294
Lysine methyltransferase; Methyltrans_16 is a lysine methyltransferase. characterized members ...
 57-218 2.55e-10

Lysine methyltransferase; Methyltrans_16 is a lysine methyltransferase. characterized members of this family are protein methyltransferases targetting Lys residues in specific proteins, including calmodulin, VCP, Kin17 and Hsp70 proteins.


Pssm-ID: 313513  Cd Length: 172  Bit Score: 58.88  E-value: 2.55e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075322    57 LQSLHQSRGSTGSVLWKTSVKVVPWLLQQSWFM---NSLTPKtSILELGSGiSGLAGI----LLSPfvGNYVASDkqlyL 129
Cdd:pfam10294   7 LRIEEDTGNGIGGHVWDAAVVLSKYLEMKIFKElgaNNLSGL-NVLELGSG-TGLVGIavalLLPG--ASVTITD----L 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075322   130 KKIRENLDQN-----NASDVEVHELDWKSTPYPKDWTFDFLDYVLFFDCIYNPHLNAHLVSCLASLAERYPgmQCLFAQE 204
Cdd:pfam10294  79 EEALELLKKNielnaLSSKVVVKVLDWGENLPPDLFDGHPVDLILAADCVYNEDSFPLLEKTLKDLLGKES--VILVAYK 156

                         170
                  ....*....|....*
gi 19075322   205 LR-DQETlvDFLERV 218
Cdd:pfam10294 157 KRrEAEK--KFFKLL 169
ribD PRK10786
bifunctional diaminohydroxyphosphoribosylaminopyrimidine deaminase/5-amino-6- ...
 257-383 4.70e-10

bifunctional diaminohydroxyphosphoribosylaminopyrimidine deaminase/5-amino-6-(5-phosphoribosylamino)uracil reductase RibD;


Pssm-ID: 182729 [Multi-domain]  Cd Length: 367  Bit Score: 60.55  E-value: 4.70e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075322  257 NHEEYMLKALNEAKKCEPTDSAF-CVGAVIVQNGKIVSTGYsRERPGNTHAEECAiekfmLKNPTDSLEGAIMYSTMEPC 335
Cdd:PRK10786   2 QDEFYMARALKLAQRGRFTTHPNpNVGCVIVKDGEIVGEGY-HQRAGEPHAEVHA-----LRMAGEKAKGATAYVTLEPC 75

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 19075322  336 SKRlSKKVSCTDLIVKQKFSTVVLGSLEPDIFVKCEGVDLLKKAGIVV 383
Cdd:PRK10786  76 SHH-GRTPPCCDALIAAGVARVVAAMQDPNPQVAGRGLYRLQQAGIDV 122
nucleoside_deaminase cd01285
Nucleoside deaminases include adenosine, guanine and cytosine deaminases. These enzymes are Zn ...
 262-365 1.09e-09

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: 55.32  E-value: 1.09e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075322 262 MLKALNEAKKCEPTDSaFCVGAVIVQN-GKIVSTGYSRERPGNT---HAEECAIEKFMLKNPTDSLEGAIMYSTMEPCsk 337
Cdd:cd01285   1 MRLAIELARKALAEGE-VPFGAVIVDDdGKVIARGHNRVEQDGDptaHAEIVAIRNAARRLGSYLLSGCTLYTTLEPC-- 77

                        90       100
                ....*....|....*....|....*...
gi 19075322 338 rlskkVSCTDLIVKQKFSTVVLGSLEPD 365
Cdd:cd01285  78 -----PMCAGALLWARIKRVVYGASDPK 100
deoxycytidylate_deaminase cd01286
Deoxycytidylate deaminase domain. Deoxycytidylate deaminase catalyzes the deamination of dCMP ...
 258-358 9.62e-08

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: 50.35  E-value: 9.62e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075322 258 HEEYMLKALNEAKKCepTDSAFCVGAVIVQNGKIVSTGYS----------------RERPGNT--------HAEECAIeK 313
Cdd:cd01286   1 DEYFMAIARLAALRS--TCPRRQVGAVIVKDKRIISTGYNgspsglphcaevgcerDDLPSGEdqkccrtvHAEQNAI-L 77

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*
gi 19075322 314 FMLKNPTdSLEGAIMYSTMEPCSKrlskkvsCTDLIVKQKFSTVV 358
Cdd:cd01286  78 QAARHGV-SLEGATLYVTLFPCIE-------CAKLIIQAGIKKVV 114
cd PHA02588
deoxycytidylate deaminase; Provisional
 261-385 3.75e-07

deoxycytidylate deaminase; Provisional


Pssm-ID: 222894 [Multi-domain]  Cd Length: 168  Bit Score: 49.76  E-value: 3.75e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075322  261 YMLKALNEAK--KCEPTDsafcVGAVIVQNGKIVSTGYS---------------------------RERPGNT------- 304
Cdd:PHA02588   6 YLQIAYLVSQesKCVSWK----VGAVIEKNGRIISTGYNgtpaggvnccdhaneqgwlddegklkkEHRPEHSawsskne 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075322  305 -HAEECAIeKFMLKNpTDSLEGAIMYSTMEPCSKrlskkvsCTDLIVKQKFSTVVLGSL---EPDifvkcEGVDLLKKAG 380
Cdd:PHA02588  82 iHAELNAI-LFAARN-GISIEGATMYVTASPCPD-------CAKAIAQSGIKKLVYCEKydrNGP-----GWDDILRKSG 147


                 ....*
gi 19075322  381 IVVIE 385
Cdd:PHA02588 148 IEVIQ 152
SmtA COG0500
SAM-dependent methyltransferase [Secondary metabolites biosynthesis, transport and catabolism, ...
 80-213 1.59e-05

SAM-dependent methyltransferase [Secondary metabolites biosynthesis, transport and catabolism, General function prediction only];


Pssm-ID: 440266 [Multi-domain]  Cd Length: 199  Bit Score: 45.29  E-value: 1.59e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075322  80 PWLLQQSWFMNSLTPKTSILELGSGISGLAGILLSPFVGNYVASD-KQLYLKKIRENLDQNNASDVEVHELDWKSTPYPK 158
Cdd:COG0500  12 PGLAALLALLERLPKGGRVLDLGCGTGRNLLALAARFGGRVIGIDlSPEAIALARARAAKAGLGNVEFLVADLAELDPLP 91

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 19075322 159 DWTFDFldyVLFFDCIY--NPHLNAHLVSCLASLAEryPG----MQCLFAQELRDQETLVD 213
Cdd:COG0500  92 AESFDL---VVAFGVLHhlPPEEREALLRELARALK--PGgvllLSASDAAAALSLARLLL 147
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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