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Conserved domains on  [gi|1541669349|gb|RTO10992|]
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HAD-IB family hydrolase [Enterobacter bugandensis]

Protein Classification

HAD family hydrolase( domain architecture ID 11552400)

HAD (haloacid dehalogenase) family hydrolase similar to Pseudomonas aeruginosa histidinol-phosphatase that catalyzes the dephosphorylation of histidinol-phosphate to histidinol, the direct precursor of histidine; the HAD (haloacid dehalogenase) family includes phosphoesterases, ATPases, phosphonatases, dehalogenases, and sugar phosphomutases acting on a remarkably diverse set of substrates

EC:  3.1.3.-
Gene Ontology:  GO:0046872|GO:0016791|GO:0016311
PubMed:  16889794|15337123
SCOP:  3001890

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
HAD_PGPPase cd02612
phosphatidylglycerol-phosphate phosphatase, similar to Escherichia coli K-12 ...
 16-208 8.39e-50

phosphatidylglycerol-phosphate phosphatase, similar to Escherichia coli K-12 phosphatidylglycerol-phosphate phosphatase C; This family includes Escherichia coli K-12 phosphatidylglycerol-phosphate phosphatase C, PgpC (previously named yfhB) which catalyzes the dephosphorylation of phosphatidylglycerol-phosphate (PGP) to phosphatidylglycerol (PG). This family belongs to the haloacid dehalogenase-like (HAD) hydrolases, a large superfamily of diverse enzymes that catalyze carbon or phosphoryl group transfer reactions on a range of substrates, using an active site aspartate in nucleophilic catalysis. Members of this superfamily include 2-L-haloalkanoic acid dehalogenase, azetidine hydrolase, phosphonoacetaldehyde hydrolase, phosphoserine phosphatase, phosphomannomutase, P-type ATPases and many others. HAD hydrolases are found in all three kingdoms of life, and most genomes are predicted to contain multiple HAD-like proteins. Members possess a highly conserved alpha/beta core domain, and many also possess a small cap domain, the fold and function of which is variable. HAD hydrolases are sometimes referred to as belonging to the DDDD superfamily of phosphohydrolases.


:

Pssm-ID: 319796 [Multi-domain]  Cd Length: 195  Bit Score: 160.93  E-value: 8.39e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541669349  16 LSVFDFDGTLTHHDSFIPFLRFAF--GKRYFAGRLVRMALPTLhcVRRKLTRDELKEVLIKtFLTGVDEHWLRQQAEAFC 93
Cdd:cd02612     1 LAFFDLDGTLIAGDSFFAFLRFKGiaERRAPLEELLLLRLMAL--YALGRLDGAGMEALLG-FATAGLAGELAALVEEFV 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541669349  94 EKYWNKLMRPEGVLAVAAEVNSGAEVTICSASPALVLQPWADRLGI-KLIGTQLEVKDGKLTGRITGNNCRCAQKVARLE 172
Cdd:cd02612    78 EEYILRVLYPEARELIAWHKAAGHDVVLISASPEELVAPIARKLGIdNVLGTQLETEDGRYTGRIIGPPCYGEGKVKRLR 157

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1541669349 173 KVYG--DLNDYHLRAWGDTRGDHELLAAAQDPHWRHFH 208
Cdd:cd02612   158 EWLAeeGIDLKDSYAYSDSINDLPMLEAVGHPVAVNPD 195
 
Name Accession Description Interval E-value
HAD_PGPPase cd02612
phosphatidylglycerol-phosphate phosphatase, similar to Escherichia coli K-12 ...
 16-208 8.39e-50

phosphatidylglycerol-phosphate phosphatase, similar to Escherichia coli K-12 phosphatidylglycerol-phosphate phosphatase C; This family includes Escherichia coli K-12 phosphatidylglycerol-phosphate phosphatase C, PgpC (previously named yfhB) which catalyzes the dephosphorylation of phosphatidylglycerol-phosphate (PGP) to phosphatidylglycerol (PG). This family belongs to the haloacid dehalogenase-like (HAD) hydrolases, a large superfamily of diverse enzymes that catalyze carbon or phosphoryl group transfer reactions on a range of substrates, using an active site aspartate in nucleophilic catalysis. Members of this superfamily include 2-L-haloalkanoic acid dehalogenase, azetidine hydrolase, phosphonoacetaldehyde hydrolase, phosphoserine phosphatase, phosphomannomutase, P-type ATPases and many others. HAD hydrolases are found in all three kingdoms of life, and most genomes are predicted to contain multiple HAD-like proteins. Members possess a highly conserved alpha/beta core domain, and many also possess a small cap domain, the fold and function of which is variable. HAD hydrolases are sometimes referred to as belonging to the DDDD superfamily of phosphohydrolases.


Pssm-ID: 319796 [Multi-domain]  Cd Length: 195  Bit Score: 160.93  E-value: 8.39e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541669349  16 LSVFDFDGTLTHHDSFIPFLRFAF--GKRYFAGRLVRMALPTLhcVRRKLTRDELKEVLIKtFLTGVDEHWLRQQAEAFC 93
Cdd:cd02612     1 LAFFDLDGTLIAGDSFFAFLRFKGiaERRAPLEELLLLRLMAL--YALGRLDGAGMEALLG-FATAGLAGELAALVEEFV 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541669349  94 EKYWNKLMRPEGVLAVAAEVNSGAEVTICSASPALVLQPWADRLGI-KLIGTQLEVKDGKLTGRITGNNCRCAQKVARLE 172
Cdd:cd02612    78 EEYILRVLYPEARELIAWHKAAGHDVVLISASPEELVAPIARKLGIdNVLGTQLETEDGRYTGRIIGPPCYGEGKVKRLR 157

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1541669349 173 KVYG--DLNDYHLRAWGDTRGDHELLAAAQDPHWRHFH 208
Cdd:cd02612   158 EWLAeeGIDLKDSYAYSDSINDLPMLEAVGHPVAVNPD 195
HAD-SF-IB-hyp1 TIGR01490
HAD-superfamily subfamily IB hydrolase, TIGR01490; This hypothetical equivalog is a member of ...
 16-207 5.78e-33

HAD-superfamily subfamily IB hydrolase, TIGR01490; This hypothetical equivalog is a member of the IB subfamily (TIGR01488) of the haloacid dehalogenase (HAD) superfamily of aspartate-nucleophile hydrolases. The sequences modelled here are all bacterial. The IB subfamily includes the enzyme phosphoserine phosphatase (TIGR00338). Due to this relationship, several of these sequences have been annotated as "phosphoserine phosphatase related proteins," or "Phosphoserine phosphatase-family enzymes." There is presently no evidence that any of the enzymes in this model possess PSPase activity. OMNI|NTL01ML1250 is annotated as a "possible transferase," however this is due to the C-terminal domain found on this sequence which is homologous to a group of glycerol-phosphate acyltransferases (between trusted and noise to TIGR00530). A subset of these sequences including OMNI|CC1962, the Caulobacter crescentus CicA protein cluster together and may represent a separate equivalog. [Unknown function, Enzymes of unknown specificity]


Pssm-ID: 273654 [Multi-domain]  Cd Length: 202  Bit Score: 117.83  E-value: 5.78e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541669349  16 LSVFDFDGTLTHHDSFIPFLRFAFGKRYFAGRL-VRMALPTLHCVRRKLTRDELKEvliKTFLTGVDEHWLRQQAEAFCE 94
Cdd:TIGR01490   1 LAFFDFDGTLTAKDTLFIFLKFLASKNILFEELrLPKVLARFEFFLNRGLDYMAYY---RAFALDALAGLLEEDVRAIVE 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541669349  95 KYWN----KLMRPEGVLAVAAEVNSGAEVTICSASPALVLQPWADRLGIK-LIGTQL-EVKDGKLTGRITGNNCRCAQKV 168
Cdd:TIGR01490  78 EFVNqkieSILYPEARDLIRWHKAEGHTIVLVSASLTILVKPLARILGIDnAIGTRLeESEDGIYTGNIDGNNCKGEGKV 157

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1541669349 169 ARLEKVYG----DLNDYHlrAWGDTRGDHELLAAAQDPHWRHF 207
Cdd:TIGR01490 158 HALAELLAeeqiDLKDSY--AYGDSISDLPLLSLVGHPYVVNP 198
SerB COG0560
Phosphoserine phosphatase [Amino acid transport and metabolism]; Phosphoserine phosphatase is ...
 18-203 3.90e-26

Phosphoserine phosphatase [Amino acid transport and metabolism]; Phosphoserine phosphatase is part of the Pathway/BioSystem: Serine biosynthesis


Pssm-ID: 440326 [Multi-domain]  Cd Length: 221  Bit Score: 100.68  E-value: 3.90e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541669349  18 VFDFDGTLTHHDSFIPFLRFAFGKRYFAGRLV--RMALPTLHCVRRKLTRDELKEVLIKTfLTGVDEHWLRQQAEAFCEK 95
Cdd:COG0560     7 VFDLDGTLIAGESIDELARFLGRRGLVDRREVleEVAAITERAMAGELDFEESLRFRVAL-LAGLPEEELEELAERLFEE 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541669349  96 YwnKLMRPEGVLAVAAEVNSGAEVTICSASPALVLQPWADRLGIK-LIGTQLEVKDGKLTGRITGNNCRCAQKVARLEKv 174
Cdd:COG0560    86 V--PRLYPGARELIAEHRAAGHKVAIVSGGFTFFVEPIAERLGIDhVIANELEVEDGRLTGEVVGPIVDGEGKAEALRE- 162

                         170       180       190
                  ....*....|....*....|....*....|..
gi 1541669349 175 YGDLNDYHLR---AWGDTRGDHELLAAAQDPH 203
Cdd:COG0560   163 LAAELGIDLEqsyAYGDSANDLPMLEAAGLPV 194
HAD pfam12710
haloacid dehalogenase-like hydrolase;
18-196 1.60e-23

haloacid dehalogenase-like hydrolase;


Pssm-ID: 432733 [Multi-domain]  Cd Length: 188  Bit Score: 92.98  E-value: 1.60e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541669349  18 VFDFDGTLTHHDSFIPFLRFAFGKRYF-AGRLVRMALPTLHCVRRKLTRDELKEVLIKTFLTGVDEHWLRQQAEAFCEKY 96
Cdd:pfam12710   2 LFDLDGTLLDGDSLFLLIRALLRRGGPdLWRALLVLLLLALLRLLGRLSRAGARELLRALLAGLPEEDAAELERFVAEVA 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541669349  97 WNKlMRPEGVLAVAAEVNSGAEVTICSASPALVLQPWADRLGIK-LIGTQLEVKDGKLTGR--ITGNNCRCAQKVARLEK 173
Cdd:pfam12710  82 LPR-LHPGALELLAAHRAAGDRVVVVTGGLRPLVEPVLAELGFDeVLATELEVDDGRFTGElrLIGPPCAGEGKVRRLRA 160

                         170       180
                  ....*....|....*....|....*..
gi 1541669349 174 VYG----DLNDYHLRAWGDTRGDHELL 196
Cdd:pfam12710 161 WLAarglGLDLADSVAYGDSPSDLPML 187
 
Name Accession Description Interval E-value
HAD_PGPPase cd02612
phosphatidylglycerol-phosphate phosphatase, similar to Escherichia coli K-12 ...
 16-208 8.39e-50

phosphatidylglycerol-phosphate phosphatase, similar to Escherichia coli K-12 phosphatidylglycerol-phosphate phosphatase C; This family includes Escherichia coli K-12 phosphatidylglycerol-phosphate phosphatase C, PgpC (previously named yfhB) which catalyzes the dephosphorylation of phosphatidylglycerol-phosphate (PGP) to phosphatidylglycerol (PG). This family belongs to the haloacid dehalogenase-like (HAD) hydrolases, a large superfamily of diverse enzymes that catalyze carbon or phosphoryl group transfer reactions on a range of substrates, using an active site aspartate in nucleophilic catalysis. Members of this superfamily include 2-L-haloalkanoic acid dehalogenase, azetidine hydrolase, phosphonoacetaldehyde hydrolase, phosphoserine phosphatase, phosphomannomutase, P-type ATPases and many others. HAD hydrolases are found in all three kingdoms of life, and most genomes are predicted to contain multiple HAD-like proteins. Members possess a highly conserved alpha/beta core domain, and many also possess a small cap domain, the fold and function of which is variable. HAD hydrolases are sometimes referred to as belonging to the DDDD superfamily of phosphohydrolases.


Pssm-ID: 319796 [Multi-domain]  Cd Length: 195  Bit Score: 160.93  E-value: 8.39e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541669349  16 LSVFDFDGTLTHHDSFIPFLRFAF--GKRYFAGRLVRMALPTLhcVRRKLTRDELKEVLIKtFLTGVDEHWLRQQAEAFC 93
Cdd:cd02612     1 LAFFDLDGTLIAGDSFFAFLRFKGiaERRAPLEELLLLRLMAL--YALGRLDGAGMEALLG-FATAGLAGELAALVEEFV 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541669349  94 EKYWNKLMRPEGVLAVAAEVNSGAEVTICSASPALVLQPWADRLGI-KLIGTQLEVKDGKLTGRITGNNCRCAQKVARLE 172
Cdd:cd02612    78 EEYILRVLYPEARELIAWHKAAGHDVVLISASPEELVAPIARKLGIdNVLGTQLETEDGRYTGRIIGPPCYGEGKVKRLR 157

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1541669349 173 KVYG--DLNDYHLRAWGDTRGDHELLAAAQDPHWRHFH 208
Cdd:cd02612   158 EWLAeeGIDLKDSYAYSDSINDLPMLEAVGHPVAVNPD 195
HAD-SF-IB-hyp1 TIGR01490
HAD-superfamily subfamily IB hydrolase, TIGR01490; This hypothetical equivalog is a member of ...
 16-207 5.78e-33

HAD-superfamily subfamily IB hydrolase, TIGR01490; This hypothetical equivalog is a member of the IB subfamily (TIGR01488) of the haloacid dehalogenase (HAD) superfamily of aspartate-nucleophile hydrolases. The sequences modelled here are all bacterial. The IB subfamily includes the enzyme phosphoserine phosphatase (TIGR00338). Due to this relationship, several of these sequences have been annotated as "phosphoserine phosphatase related proteins," or "Phosphoserine phosphatase-family enzymes." There is presently no evidence that any of the enzymes in this model possess PSPase activity. OMNI|NTL01ML1250 is annotated as a "possible transferase," however this is due to the C-terminal domain found on this sequence which is homologous to a group of glycerol-phosphate acyltransferases (between trusted and noise to TIGR00530). A subset of these sequences including OMNI|CC1962, the Caulobacter crescentus CicA protein cluster together and may represent a separate equivalog. [Unknown function, Enzymes of unknown specificity]


Pssm-ID: 273654 [Multi-domain]  Cd Length: 202  Bit Score: 117.83  E-value: 5.78e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541669349  16 LSVFDFDGTLTHHDSFIPFLRFAFGKRYFAGRL-VRMALPTLHCVRRKLTRDELKEvliKTFLTGVDEHWLRQQAEAFCE 94
Cdd:TIGR01490   1 LAFFDFDGTLTAKDTLFIFLKFLASKNILFEELrLPKVLARFEFFLNRGLDYMAYY---RAFALDALAGLLEEDVRAIVE 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541669349  95 KYWN----KLMRPEGVLAVAAEVNSGAEVTICSASPALVLQPWADRLGIK-LIGTQL-EVKDGKLTGRITGNNCRCAQKV 168
Cdd:TIGR01490  78 EFVNqkieSILYPEARDLIRWHKAEGHTIVLVSASLTILVKPLARILGIDnAIGTRLeESEDGIYTGNIDGNNCKGEGKV 157

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1541669349 169 ARLEKVYG----DLNDYHlrAWGDTRGDHELLAAAQDPHWRHF 207
Cdd:TIGR01490 158 HALAELLAeeqiDLKDSY--AYGDSISDLPLLSLVGHPYVVNP 198
SerB COG0560
Phosphoserine phosphatase [Amino acid transport and metabolism]; Phosphoserine phosphatase is ...
 18-203 3.90e-26

Phosphoserine phosphatase [Amino acid transport and metabolism]; Phosphoserine phosphatase is part of the Pathway/BioSystem: Serine biosynthesis


Pssm-ID: 440326 [Multi-domain]  Cd Length: 221  Bit Score: 100.68  E-value: 3.90e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541669349  18 VFDFDGTLTHHDSFIPFLRFAFGKRYFAGRLV--RMALPTLHCVRRKLTRDELKEVLIKTfLTGVDEHWLRQQAEAFCEK 95
Cdd:COG0560     7 VFDLDGTLIAGESIDELARFLGRRGLVDRREVleEVAAITERAMAGELDFEESLRFRVAL-LAGLPEEELEELAERLFEE 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541669349  96 YwnKLMRPEGVLAVAAEVNSGAEVTICSASPALVLQPWADRLGIK-LIGTQLEVKDGKLTGRITGNNCRCAQKVARLEKv 174
Cdd:COG0560    86 V--PRLYPGARELIAEHRAAGHKVAIVSGGFTFFVEPIAERLGIDhVIANELEVEDGRLTGEVVGPIVDGEGKAEALRE- 162

                         170       180       190
                  ....*....|....*....|....*....|..
gi 1541669349 175 YGDLNDYHLR---AWGDTRGDHELLAAAQDPH 203
Cdd:COG0560   163 LAAELGIDLEqsyAYGDSANDLPMLEAAGLPV 194
HAD pfam12710
haloacid dehalogenase-like hydrolase;
18-196 1.60e-23

haloacid dehalogenase-like hydrolase;


Pssm-ID: 432733 [Multi-domain]  Cd Length: 188  Bit Score: 92.98  E-value: 1.60e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541669349  18 VFDFDGTLTHHDSFIPFLRFAFGKRYF-AGRLVRMALPTLHCVRRKLTRDELKEVLIKTFLTGVDEHWLRQQAEAFCEKY 96
Cdd:pfam12710   2 LFDLDGTLLDGDSLFLLIRALLRRGGPdLWRALLVLLLLALLRLLGRLSRAGARELLRALLAGLPEEDAAELERFVAEVA 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541669349  97 WNKlMRPEGVLAVAAEVNSGAEVTICSASPALVLQPWADRLGIK-LIGTQLEVKDGKLTGR--ITGNNCRCAQKVARLEK 173
Cdd:pfam12710  82 LPR-LHPGALELLAAHRAAGDRVVVVTGGLRPLVEPVLAELGFDeVLATELEVDDGRFTGElrLIGPPCAGEGKVRRLRA 160

                         170       180
                  ....*....|....*....|....*..
gi 1541669349 174 VYG----DLNDYHLRAWGDTRGDHELL 196
Cdd:pfam12710 161 WLAarglGLDLADSVAYGDSPSDLPML 187
HAD-SF-IB TIGR01488
Haloacid Dehalogenase superfamily, subfamily IB, phosphoserine phosphatase-like; This model ...
 16-199 1.13e-22

Haloacid Dehalogenase superfamily, subfamily IB, phosphoserine phosphatase-like; This model represents a subfamily of the Haloacid Dehalogenase superfamily of aspartate-nucleophile hydrolases. Subfamily IA, B, C and D are distinguished from the rest of the superfamily by the presence of a variable domain between the first and second conserved catalytic motifs. In subfamilies IA and IB, this domain consists of an alpha-helical bundle. It was necessary to model these two subfamilies separately, breaking them at a an apparent phylogenetic bifurcation, so that the resulting model(s) are not so broadly defined that members of subfamily III (which lack the variable domain) are included. Subfamily IA includes the enzyme phosphoserine phosphatase (TIGR00338) as well as three hypothetical equivalogs. Many members of these hypothetical equivalogs have been annotated as PSPase-like or PSPase-family proteins. In particular, the hypothetical equivalog which appears to be most closely related to PSPase contains only Archaea (while TIGR00338 contains only eukaryotes and bacteria) of which some are annotated as PSPases. Although this is a reasonable conjecture, none of these sequences has sufficient evidence for this assignment. If such should be found, this model should be retired while the PSPase model should be broadened to include these sequences. [Unknown function, Enzymes of unknown specificity]


Pssm-ID: 273653 [Multi-domain]  Cd Length: 177  Bit Score: 90.49  E-value: 1.13e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541669349  16 LSVFDFDGTLTHHDSFIPFLRFAFGKRYFAGRLVRMALPtlhcvRRKLTRDELKEVLIKtfltgvdEHWLRQQAEAfCEK 95
Cdd:TIGR01488   1 LAIFDFDGTLTRQDSLIDLLAKLLGTNDEVIELTRLAPS-----GRISFEDALGRRLAL-------LHRSRSEEVA-KEF 67

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541669349  96 YWNKLMRPEGVLA-VAAEVNSGAEVTICSASPALVLQPWADRLGI-KLIGTQLEVKD-GKLTGRITGN-NCRCAQKVARL 171
Cdd:TIGR01488  68 LARQVALRPGARElISWLKERGIDTVIVSGGFDFFVEPVAEKLGIdDVFANRLEFDDnGLLTGPIEGQvNPEGECKGKVL 147

                         170       180       190
                  ....*....|....*....|....*....|
gi 1541669349 172 EKVYGDLND--YHLRAWGDTRGDHELLAAA 199
Cdd:TIGR01488 148 KELLEESKItlKKIIAVGDSVNDLPMLKLA 177
YigB COG1011
FMN and 5-amino-6-(5-phospho-D-ribitylamino)uracil phosphatase YigB, HAD superfamily ...
 18-139 3.20e-03

FMN and 5-amino-6-(5-phospho-D-ribitylamino)uracil phosphatase YigB, HAD superfamily (riboflavin biosynthesis) [Coenzyme transport and metabolism];


Pssm-ID: 440635 [Multi-domain]  Cd Length: 220  Bit Score: 37.32  E-value: 3.20e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541669349  18 VFDFDGTLTHHDSFIPFLRFAFGKRYFAGRLVRMALPTLHCVRRKLTRD-ELKEVLIKTFLTGVDEHWLRQQAEAFCEKY 96
Cdd:COG1011     5 LFDLDGTLLDFDPVIAEALRALAERLGLLDEAEELAEAYRAIEYALWRRyERGEITFAELLRRLLEELGLDLAEELAEAF 84

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1541669349  97 ---WNKLMRP-EGVLAVAAEV-NSGAEVTICSASPALVLQPWADRLGI 139
Cdd:COG1011    85 laaLPELVEPyPDALELLEALkARGYRLALLTNGSAELQEAKLRRLGL 132
 
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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