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Conserved domains on  [gi|494884502|ref|WP_007610550|]
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MULTISPECIES: Cof-type HAD-IIB family hydrolase [Bacillus]

Protein Classification

Cof-type HAD-IIB family hydrolase( domain architecture ID 11576297)

Cof-type HAD-IIB family hydrolase, part of the HAD (haloacid dehalogenase) family that includes phosphoesterases, ATPases, phosphonatases, dehalogenases, and sugar phosphomutases acting on a remarkably diverse set of substrates

CATH:  3.30.1240.10
EC:  3.-.-.-
Gene Ontology:  GO:0016787
PubMed:  16889794|15337123|33940035|37786806
SCOP:  3001890

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
HAD_Pase cd07516
phosphatase, similar to Escherichia coli Cof and Thermotoga maritima TM0651; belongs to the ...
 7-265 3.59e-87

phosphatase, similar to Escherichia coli Cof and Thermotoga maritima TM0651; belongs to the haloacid dehalogenase-like superfamily; Escherichia coli Cof is involved in the hydrolysis of HMP-PP (4-amino-2-methyl-5-hydroxymethylpyrimidine pyrophosphate, an intermediate in thiamin biosynthesis), Cof also has phosphatase activity against the coenzymes pyridoxal phosphate (PLP) and FMN. Thermotoga maritima TM0651 acts as a phosphatase with a phosphorylated carbohydrate molecule as a possible substrate. Escherichia coli YbhA is also a member of this family and catalyzes the dephosphorylation of PLP, YbhA can also hydrolyze erythrose-4-phosphate and fructose-1,6-bis-phosphate. Members of this family belong 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: 319818 [Multi-domain]  Cd Length: 253  Bit Score: 259.83  E-value: 3.59e-87
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494884502   7 LIALDLDGTLLKDDKTISPETARTIQTLKEAGHHVCISTGRPFRSSSMYYDELGLTTPIVNFNGAFVHHPKDESWgrYHT 86
Cdd:cd07516    1 LIALDLDGTLLNSDKEISPRTKEAIKKAKEKGIKVVIATGRPLRGAQPYLEELGLDSPLITFNGALVYDPTGKEI--LER 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494884502  87 SLSVDVVRQLAELTETYQI-HNVLAE--IIDDVYFHYHDEHLIEAFHMNTanvtfgDLRETVQEDVTSVLIHAKEEDVAD 163
Cdd:cd07516   79 LISKEDVKELEEFLRKLGIgINIYTNddWADTIYEENEDDEIIKPAEILD------DLLLPPDEDITKILFVGEDEELDE 152

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494884502 164 IRAHLsdVHAEVIDHRRWAAPWHVIEIIKHGMNKAVGLKKISDYYQVPRERIIAFGDEDNDLEMLRFAGCGVAMGNGTDE 243
Cdd:cd07516  153 LIAKL--PEEFFDDLSVVRSAPFYLEIMPKGVSKGNALKKLAEYLGISLEEVIAFGDNENDLSMLEYAGLGVAMGNAIDE 230

                        250       260
                 ....*....|....*....|..
gi 494884502 244 VKQAADRVTGSNEADGIAEFLK 265
Cdd:cd07516  231 VKEAADYVTLTNNEDGVAKAIE 252
 
Name Accession Description Interval E-value
HAD_Pase cd07516
phosphatase, similar to Escherichia coli Cof and Thermotoga maritima TM0651; belongs to the ...
 7-265 3.59e-87

phosphatase, similar to Escherichia coli Cof and Thermotoga maritima TM0651; belongs to the haloacid dehalogenase-like superfamily; Escherichia coli Cof is involved in the hydrolysis of HMP-PP (4-amino-2-methyl-5-hydroxymethylpyrimidine pyrophosphate, an intermediate in thiamin biosynthesis), Cof also has phosphatase activity against the coenzymes pyridoxal phosphate (PLP) and FMN. Thermotoga maritima TM0651 acts as a phosphatase with a phosphorylated carbohydrate molecule as a possible substrate. Escherichia coli YbhA is also a member of this family and catalyzes the dephosphorylation of PLP, YbhA can also hydrolyze erythrose-4-phosphate and fructose-1,6-bis-phosphate. Members of this family belong 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: 319818 [Multi-domain]  Cd Length: 253  Bit Score: 259.83  E-value: 3.59e-87
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494884502   7 LIALDLDGTLLKDDKTISPETARTIQTLKEAGHHVCISTGRPFRSSSMYYDELGLTTPIVNFNGAFVHHPKDESWgrYHT 86
Cdd:cd07516    1 LIALDLDGTLLNSDKEISPRTKEAIKKAKEKGIKVVIATGRPLRGAQPYLEELGLDSPLITFNGALVYDPTGKEI--LER 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494884502  87 SLSVDVVRQLAELTETYQI-HNVLAE--IIDDVYFHYHDEHLIEAFHMNTanvtfgDLRETVQEDVTSVLIHAKEEDVAD 163
Cdd:cd07516   79 LISKEDVKELEEFLRKLGIgINIYTNddWADTIYEENEDDEIIKPAEILD------DLLLPPDEDITKILFVGEDEELDE 152

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494884502 164 IRAHLsdVHAEVIDHRRWAAPWHVIEIIKHGMNKAVGLKKISDYYQVPRERIIAFGDEDNDLEMLRFAGCGVAMGNGTDE 243
Cdd:cd07516  153 LIAKL--PEEFFDDLSVVRSAPFYLEIMPKGVSKGNALKKLAEYLGISLEEVIAFGDNENDLSMLEYAGLGVAMGNAIDE 230

                        250       260
                 ....*....|....*....|..
gi 494884502 244 VKQAADRVTGSNEADGIAEFLK 265
Cdd:cd07516  231 VKEAADYVTLTNNEDGVAKAIE 252
Hydrolase_3 pfam08282
haloacid dehalogenase-like hydrolase; This family contains haloacid dehalogenase-like ...
 8-264 1.78e-78

haloacid dehalogenase-like hydrolase; This family contains haloacid dehalogenase-like hydrolase enzymes.


Pssm-ID: 429897 [Multi-domain]  Cd Length: 255  Bit Score: 237.91  E-value: 1.78e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494884502    8 IALDLDGTLLKDDKTISPETARTIQTLKEAGHHVCISTGRPFRSSSMYYDELGLTTPIVNFNGAFVHHPKDESwgRYHTS 87
Cdd:pfam08282   1 IASDLDGTLLNSDKKISEKTKEAIKKLKEKGIKFVIATGRPYRAILPVIKELGLDDPVICYNGALIYDENGKI--LYSNP 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494884502   88 LSVDVVRQLAELTETYQIHnVLAEIIDDVYFHYHDEH---LIEAFHMNTANVTFGDLRETVQEDVTSVLIHAKEEDVADI 164
Cdd:pfam08282  79 ISKEAVKEIIEYLKENNLE-ILLYTDDGVYILNDNELekiLKELNYTKSFVPEIDDFELLEDEDINKILILLDEEDLDEL 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494884502  165 RAHLSdvHAEVIDHRRWAAPWHVIEIIKHGMNKAVGLKKISDYYQVPRERIIAFGDEDNDLEMLRFAGCGVAMGNGTDEV 244
Cdd:pfam08282 158 EKELK--ELFGSLITITSSGPGYLEIMPKGVSKGTALKALAKHLNISLEEVIAFGDGENDIEMLEAAGLGVAMGNASPEV 235

                         250       260
                  ....*....|....*....|
gi 494884502  245 KQAADRVTGSNEADGIAEFL 264
Cdd:pfam08282 236 KAAADYVTDSNNEDGVAKAL 255
Cof COG0561
Hydroxymethylpyrimidine pyrophosphatase and other HAD family phosphatases [Coenzyme transport ...
 4-267 2.75e-69

Hydroxymethylpyrimidine pyrophosphatase and other HAD family phosphatases [Coenzyme transport and metabolism, General function prediction only];


Pssm-ID: 440327 [Multi-domain]  Cd Length: 192  Bit Score: 212.30  E-value: 2.75e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494884502   4 KPYLIALDLDGTLLKDDKTISPETARTIQTLKEAGHHVCISTGRPFRSSSMYYDELGLTTPIVNFNGAFVHHPKDESwgR 83
Cdd:COG0561    1 MIKLIALDLDGTLLNDDGEISPRTKEALRRLREKGIKVVIATGRPLRSALPLLEELGLDDPLITSNGALIYDPDGEV--L 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494884502  84 YHTSLSVDVVRQLAELTETYQIHnvlaeiiddvyfhyhdehlieafhmntanvtfgdlretvqedvtsvlihakeedvad 163
Cdd:COG0561   79 YERPLDPEDVREILELLREHGLH--------------------------------------------------------- 101

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494884502 164 irahlsdVHAEVIDHRRWaapwhvIEIIKHGMNKAVGLKKISDYYQVPRERIIAFGDEDNDLEMLRFAGCGVAMGNGTDE 243
Cdd:COG0561  102 -------LQVVVRSGPGF------LEILPKGVSKGSALKKLAERLGIPPEEVIAFGDSGNDLEMLEAAGLGVAMGNAPPE 168

                        250       260
                 ....*....|....*....|....
gi 494884502 244 VKQAADRVTGSNEADGIAEFLKSY 267
Cdd:COG0561  169 VKAAADYVTGSNDEDGVAEALEKL 192
Cof-subfamily TIGR00099
Cof subfamily of IIB subfamily of haloacid dehalogenase superfamily; This subfamily of ...
 7-264 8.62e-67

Cof subfamily of IIB subfamily of haloacid dehalogenase superfamily; This subfamily of sequences falls within the Class-IIB subfamily (TIGR01484) of the Haloacid Dehalogenase superfamily of aspartate-nucleophile hydrolases. The use of the name "Cof" as an identifier here is arbitrary and refers to the E. coli Cof protein. This subfamily is notable for the large number of recent paralogs in many species. Listeria, for instance, has 12, Clostridium, Lactococcus and Streptococcus pneumoniae have 8 each, Enterococcus and Salmonella have 7 each, and Bacillus subtilus, Mycoplasma, Staphylococcus and E. coli have 6 each. This high degree of gene duplication is limited to the gamma proteobacteria and low-GC gram positive lineages. The profusion of genes in this subfamily is not coupled with a high degree of divergence, so it is impossible to determine an accurate phylogeny at the equivalog level. Considering the relationship of this subfamily to the other known members of the HAD-IIB subfamily (TIGR01484), sucrose and trehalose phosphatases and phosphomannomutase, it seems a reasonable hypothesis that these enzymes act on phosphorylated sugars. Possibly the diversification of genes in this subfamily represents the diverse sugars and polysaccharides that various bacteria find in their biological niches. The members of this subfamily are restricted almost exclusively to bacteria (one sequences from S. pombe scores above trusted, while another is between trusted and noise). It is notable that no archaea are found in this group, the closest relations to the archaea found here being two Deinococcus sequences. [Unknown function, Enzymes of unknown specificity]


Pssm-ID: 272905 [Multi-domain]  Cd Length: 256  Bit Score: 207.89  E-value: 8.62e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494884502    7 LIALDLDGTLLKDDKTISPETARTIQTLKEAGHHVCISTGRPFRSSSMYYDELGLTTPIVNFNGAFVHHPKDESwgRYHT 86
Cdd:TIGR00099   1 LIFIDLDGTLLNDDHTISPSTKEALAKLREKGIKVVLATGRPYKEVKNILKELGLDTPFITANGAAVIDDQGEI--LYKK 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494884502   87 SLSVDVVRQLAELTETYQIHNVLAEIiDDVYFHYHDEHLIEAF--HMNTANVTFGDLRETVQEDVTSVLIHAKEEDVADI 164
Cdd:TIGR00099  79 PLDLDLVEEILNFLKKHGLDVILYGD-DSIYASKNDPEYFTIFkkFLGEPKLEVVDIQYLPDDILKILLLFLDPEDLDLL 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494884502  165 RAHLSdvHAEVIDHRRWAAP-WHVIEIIKHGMNKAVGLKKISDYYQVPRERIIAFGDEDNDLEMLRFAGCGVAMGNGTDE 243
Cdd:TIGR00099 158 IEALN--KLELEENVSVVSSgPYSIEITAKGVSKGSALQSLAEALGISLEDVIAFGDGMNDIEMLEAAGYGVAMGNADEE 235

                         250       260
                  ....*....|....*....|.
gi 494884502  244 VKQAADRVTGSNEADGIAEFL 264
Cdd:TIGR00099 236 LKALADYVTDSNNEDGVALAL 256
PRK10530 PRK10530
pyridoxal phosphate (PLP) phosphatase; Provisional
 7-267 3.80e-38

pyridoxal phosphate (PLP) phosphatase; Provisional


Pssm-ID: 182523 [Multi-domain]  Cd Length: 272  Bit Score: 134.77  E-value: 3.80e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494884502   7 LIALDLDGTLLKDDKTISPETARTIQTLKEAGHHVCISTGR------PFrsssmyYDELGLTTPIVNFNGAFVHHpkdes 80
Cdd:PRK10530   5 VIALDLDGTLLTPKKTILPESLEALARAREAGYKVIIVTGRhhvaihPF------YQALALDTPAICCNGTYLYD----- 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494884502  81 wgrYHTS-------LSVDVVRQLAELTETYQIHNVLaeIIDD--VYFHYHD---------EHLIEAFHMNTANVTfgDLR 142
Cdd:PRK10530  74 ---YQAKkvleadpLPVQQALQVIEMLDEHQIHGLM--YVDDamLYEHPTGhvirtlnwaQTLPPEQRPTFTQVD--SLA 146

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494884502 143 ETVQeDVTSVLIHA-KEEDVADIRAHLSDVHAEVIDHRRWAapWH-VIEIIKHGMNKAVGLKKISDYYQVPRERIIAFGD 220
Cdd:PRK10530 147 QAAR-QVNAIWKFAlTHEDLPQLQHFAKHVEHELGLECEWS--WHdQVDIARKGNSKGKRLTQWVEAQGWSMKNVVAFGD 223

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*..
gi 494884502 221 EDNDLEMLRFAGCGVAMGNGTDEVKQAADRVTGSNEADGIAEFLKSY 267
Cdd:PRK10530 224 NFNDISMLEAAGLGVAMGNADDAVKARADLVIGDNTTPSIAEFIYSH 270
 
Name Accession Description Interval E-value
HAD_Pase cd07516
phosphatase, similar to Escherichia coli Cof and Thermotoga maritima TM0651; belongs to the ...
 7-265 3.59e-87

phosphatase, similar to Escherichia coli Cof and Thermotoga maritima TM0651; belongs to the haloacid dehalogenase-like superfamily; Escherichia coli Cof is involved in the hydrolysis of HMP-PP (4-amino-2-methyl-5-hydroxymethylpyrimidine pyrophosphate, an intermediate in thiamin biosynthesis), Cof also has phosphatase activity against the coenzymes pyridoxal phosphate (PLP) and FMN. Thermotoga maritima TM0651 acts as a phosphatase with a phosphorylated carbohydrate molecule as a possible substrate. Escherichia coli YbhA is also a member of this family and catalyzes the dephosphorylation of PLP, YbhA can also hydrolyze erythrose-4-phosphate and fructose-1,6-bis-phosphate. Members of this family belong 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: 319818 [Multi-domain]  Cd Length: 253  Bit Score: 259.83  E-value: 3.59e-87
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494884502   7 LIALDLDGTLLKDDKTISPETARTIQTLKEAGHHVCISTGRPFRSSSMYYDELGLTTPIVNFNGAFVHHPKDESWgrYHT 86
Cdd:cd07516    1 LIALDLDGTLLNSDKEISPRTKEAIKKAKEKGIKVVIATGRPLRGAQPYLEELGLDSPLITFNGALVYDPTGKEI--LER 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494884502  87 SLSVDVVRQLAELTETYQI-HNVLAE--IIDDVYFHYHDEHLIEAFHMNTanvtfgDLRETVQEDVTSVLIHAKEEDVAD 163
Cdd:cd07516   79 LISKEDVKELEEFLRKLGIgINIYTNddWADTIYEENEDDEIIKPAEILD------DLLLPPDEDITKILFVGEDEELDE 152

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494884502 164 IRAHLsdVHAEVIDHRRWAAPWHVIEIIKHGMNKAVGLKKISDYYQVPRERIIAFGDEDNDLEMLRFAGCGVAMGNGTDE 243
Cdd:cd07516  153 LIAKL--PEEFFDDLSVVRSAPFYLEIMPKGVSKGNALKKLAEYLGISLEEVIAFGDNENDLSMLEYAGLGVAMGNAIDE 230

                        250       260
                 ....*....|....*....|..
gi 494884502 244 VKQAADRVTGSNEADGIAEFLK 265
Cdd:cd07516  231 VKEAADYVTLTNNEDGVAKAIE 252
Hydrolase_3 pfam08282
haloacid dehalogenase-like hydrolase; This family contains haloacid dehalogenase-like ...
 8-264 1.78e-78

haloacid dehalogenase-like hydrolase; This family contains haloacid dehalogenase-like hydrolase enzymes.


Pssm-ID: 429897 [Multi-domain]  Cd Length: 255  Bit Score: 237.91  E-value: 1.78e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494884502    8 IALDLDGTLLKDDKTISPETARTIQTLKEAGHHVCISTGRPFRSSSMYYDELGLTTPIVNFNGAFVHHPKDESwgRYHTS 87
Cdd:pfam08282   1 IASDLDGTLLNSDKKISEKTKEAIKKLKEKGIKFVIATGRPYRAILPVIKELGLDDPVICYNGALIYDENGKI--LYSNP 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494884502   88 LSVDVVRQLAELTETYQIHnVLAEIIDDVYFHYHDEH---LIEAFHMNTANVTFGDLRETVQEDVTSVLIHAKEEDVADI 164
Cdd:pfam08282  79 ISKEAVKEIIEYLKENNLE-ILLYTDDGVYILNDNELekiLKELNYTKSFVPEIDDFELLEDEDINKILILLDEEDLDEL 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494884502  165 RAHLSdvHAEVIDHRRWAAPWHVIEIIKHGMNKAVGLKKISDYYQVPRERIIAFGDEDNDLEMLRFAGCGVAMGNGTDEV 244
Cdd:pfam08282 158 EKELK--ELFGSLITITSSGPGYLEIMPKGVSKGTALKALAKHLNISLEEVIAFGDGENDIEMLEAAGLGVAMGNASPEV 235

                         250       260
                  ....*....|....*....|
gi 494884502  245 KQAADRVTGSNEADGIAEFL 264
Cdd:pfam08282 236 KAAADYVTDSNNEDGVAKAL 255
Cof COG0561
Hydroxymethylpyrimidine pyrophosphatase and other HAD family phosphatases [Coenzyme transport ...
 4-267 2.75e-69

Hydroxymethylpyrimidine pyrophosphatase and other HAD family phosphatases [Coenzyme transport and metabolism, General function prediction only];


Pssm-ID: 440327 [Multi-domain]  Cd Length: 192  Bit Score: 212.30  E-value: 2.75e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494884502   4 KPYLIALDLDGTLLKDDKTISPETARTIQTLKEAGHHVCISTGRPFRSSSMYYDELGLTTPIVNFNGAFVHHPKDESwgR 83
Cdd:COG0561    1 MIKLIALDLDGTLLNDDGEISPRTKEALRRLREKGIKVVIATGRPLRSALPLLEELGLDDPLITSNGALIYDPDGEV--L 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494884502  84 YHTSLSVDVVRQLAELTETYQIHnvlaeiiddvyfhyhdehlieafhmntanvtfgdlretvqedvtsvlihakeedvad 163
Cdd:COG0561   79 YERPLDPEDVREILELLREHGLH--------------------------------------------------------- 101

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494884502 164 irahlsdVHAEVIDHRRWaapwhvIEIIKHGMNKAVGLKKISDYYQVPRERIIAFGDEDNDLEMLRFAGCGVAMGNGTDE 243
Cdd:COG0561  102 -------LQVVVRSGPGF------LEILPKGVSKGSALKKLAERLGIPPEEVIAFGDSGNDLEMLEAAGLGVAMGNAPPE 168

                        250       260
                 ....*....|....*....|....
gi 494884502 244 VKQAADRVTGSNEADGIAEFLKSY 267
Cdd:COG0561  169 VKAAADYVTGSNDEDGVAEALEKL 192
Cof-subfamily TIGR00099
Cof subfamily of IIB subfamily of haloacid dehalogenase superfamily; This subfamily of ...
 7-264 8.62e-67

Cof subfamily of IIB subfamily of haloacid dehalogenase superfamily; This subfamily of sequences falls within the Class-IIB subfamily (TIGR01484) of the Haloacid Dehalogenase superfamily of aspartate-nucleophile hydrolases. The use of the name "Cof" as an identifier here is arbitrary and refers to the E. coli Cof protein. This subfamily is notable for the large number of recent paralogs in many species. Listeria, for instance, has 12, Clostridium, Lactococcus and Streptococcus pneumoniae have 8 each, Enterococcus and Salmonella have 7 each, and Bacillus subtilus, Mycoplasma, Staphylococcus and E. coli have 6 each. This high degree of gene duplication is limited to the gamma proteobacteria and low-GC gram positive lineages. The profusion of genes in this subfamily is not coupled with a high degree of divergence, so it is impossible to determine an accurate phylogeny at the equivalog level. Considering the relationship of this subfamily to the other known members of the HAD-IIB subfamily (TIGR01484), sucrose and trehalose phosphatases and phosphomannomutase, it seems a reasonable hypothesis that these enzymes act on phosphorylated sugars. Possibly the diversification of genes in this subfamily represents the diverse sugars and polysaccharides that various bacteria find in their biological niches. The members of this subfamily are restricted almost exclusively to bacteria (one sequences from S. pombe scores above trusted, while another is between trusted and noise). It is notable that no archaea are found in this group, the closest relations to the archaea found here being two Deinococcus sequences. [Unknown function, Enzymes of unknown specificity]


Pssm-ID: 272905 [Multi-domain]  Cd Length: 256  Bit Score: 207.89  E-value: 8.62e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494884502    7 LIALDLDGTLLKDDKTISPETARTIQTLKEAGHHVCISTGRPFRSSSMYYDELGLTTPIVNFNGAFVHHPKDESwgRYHT 86
Cdd:TIGR00099   1 LIFIDLDGTLLNDDHTISPSTKEALAKLREKGIKVVLATGRPYKEVKNILKELGLDTPFITANGAAVIDDQGEI--LYKK 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494884502   87 SLSVDVVRQLAELTETYQIHNVLAEIiDDVYFHYHDEHLIEAF--HMNTANVTFGDLRETVQEDVTSVLIHAKEEDVADI 164
Cdd:TIGR00099  79 PLDLDLVEEILNFLKKHGLDVILYGD-DSIYASKNDPEYFTIFkkFLGEPKLEVVDIQYLPDDILKILLLFLDPEDLDLL 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494884502  165 RAHLSdvHAEVIDHRRWAAP-WHVIEIIKHGMNKAVGLKKISDYYQVPRERIIAFGDEDNDLEMLRFAGCGVAMGNGTDE 243
Cdd:TIGR00099 158 IEALN--KLELEENVSVVSSgPYSIEITAKGVSKGSALQSLAEALGISLEDVIAFGDGMNDIEMLEAAGYGVAMGNADEE 235

                         250       260
                  ....*....|....*....|.
gi 494884502  244 VKQAADRVTGSNEADGIAEFL 264
Cdd:TIGR00099 236 LKALADYVTDSNNEDGVALAL 256
PRK10530 PRK10530
pyridoxal phosphate (PLP) phosphatase; Provisional
 7-267 3.80e-38

pyridoxal phosphate (PLP) phosphatase; Provisional


Pssm-ID: 182523 [Multi-domain]  Cd Length: 272  Bit Score: 134.77  E-value: 3.80e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494884502   7 LIALDLDGTLLKDDKTISPETARTIQTLKEAGHHVCISTGR------PFrsssmyYDELGLTTPIVNFNGAFVHHpkdes 80
Cdd:PRK10530   5 VIALDLDGTLLTPKKTILPESLEALARAREAGYKVIIVTGRhhvaihPF------YQALALDTPAICCNGTYLYD----- 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494884502  81 wgrYHTS-------LSVDVVRQLAELTETYQIHNVLaeIIDD--VYFHYHD---------EHLIEAFHMNTANVTfgDLR 142
Cdd:PRK10530  74 ---YQAKkvleadpLPVQQALQVIEMLDEHQIHGLM--YVDDamLYEHPTGhvirtlnwaQTLPPEQRPTFTQVD--SLA 146

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494884502 143 ETVQeDVTSVLIHA-KEEDVADIRAHLSDVHAEVIDHRRWAapWH-VIEIIKHGMNKAVGLKKISDYYQVPRERIIAFGD 220
Cdd:PRK10530 147 QAAR-QVNAIWKFAlTHEDLPQLQHFAKHVEHELGLECEWS--WHdQVDIARKGNSKGKRLTQWVEAQGWSMKNVVAFGD 223

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*..
gi 494884502 221 EDNDLEMLRFAGCGVAMGNGTDEVKQAADRVTGSNEADGIAEFLKSY 267
Cdd:PRK10530 224 NFNDISMLEAAGLGVAMGNADDAVKARADLVIGDNTTPSIAEFIYSH 270
HAD_HPP cd07517
phosphatase, similar to Bacteroides thetaiotaomicron VPI-5482 BT4131 hexose phosphate ...
 10-265 6.24e-37

phosphatase, similar to Bacteroides thetaiotaomicron VPI-5482 BT4131 hexose phosphate phosphatase; belongs to the haloacid dehalogenase-like superfamily; Bacteroides thetaiotaomicron VPI-5482 BT4131 is a phosphatase with preference for hexose phosphates. In addition this family includes uncharacterized Bacillus subtilis YkrA, a putative phosphatase and uncharacterized Streptococcus pyogenes MGAS10394 a putative bifunctional phosphatase/peptidyl-prolyl cis-trans isomerase. Members of this family belong 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: 319819 [Multi-domain]  Cd Length: 213  Bit Score: 130.04  E-value: 6.24e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494884502  10 LDLDGTLLKDDKTISPETARTIQTLKEAGHHVCISTGRPFRSSSMYYDELGLTTpIVNFNGAFVHHPKDESwgrYHTSLS 89
Cdd:cd07517    5 FDIDGTLLDEDTTIPESTKEAIAALKEKGILVVIATGRAPFEIQPIVKALGIDS-YVSYNGQYVFFEGEVI---YKNPLP 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494884502  90 VDVVRQLAEltetyqihnvlaeiiddvyfhYHDEHLIEaFHMNTANVTFGDLREtvqedvtsvlihakEEDVADIRAHLS 169
Cdd:cd07517   81 QELVERLTE---------------------FAKEQGHP-VSFYGQLLLFEDEEE--------------EQKYEELRPELR 124

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494884502 170 DVHaevidhrrwaapWH--VIEIIKHGMNKAVGLKKISDYYQVPRERIIAFGDEDNDLEMLRFAGCGVAMGNGTDEVKQA 247
Cdd:cd07517  125 FVR------------WHplSTDVIPKGGSKAKGIQKVIEHLGIKKEETMAFGDGLNDIEMLEAVGIGIAMGNAHEELKEI 192

                        250
                 ....*....|....*...
gi 494884502 248 ADRVTGSNEADGIAEFLK 265
Cdd:cd07517  193 ADYVTKDVDEDGILKALK 210
PRK10513 PRK10513
sugar phosphate phosphatase; Provisional
 7-261 9.92e-37

sugar phosphate phosphatase; Provisional


Pssm-ID: 182509 [Multi-domain]  Cd Length: 270  Bit Score: 130.97  E-value: 9.92e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494884502   7 LIALDLDGTLLKDDKTISPETARTIQTLKEAGHHVCISTGRPFRSSSMYYDELGLTTP----IVNfNGAFVHHPKDESwG 82
Cdd:PRK10513   5 LIAIDMDGTLLLPDHTISPAVKQAIAAARAKGVNVVLTTGRPYAGVHRYLKELHMEQPgdycITN-NGALVQKAADGE-T 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494884502  83 RYHTSLSVDVVRQLAELTETYQIHnvlaeiiddvyFHYHD-EHL------IEAFHMNTANVTFGDLRETVQEDVTSVLIH 155
Cdd:PRK10513  83 VAQTALSYDDYLYLEKLSREVGVH-----------FHALDrNTLytanrdISYYTVHESFLTGIPLVFREVEKMDPNLQF 151

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494884502 156 AK-----EEDVADirAHLSDVHAEVidHRRWA----APWHvIEIIKHGMNKAVGLKKISDYYQVPRERIIAFGDEDNDLE 226
Cdd:PRK10513 152 PKvmmidEPEILD--AAIARIPAEV--KERYTvlksAPYF-LEILDKRVNKGTGVKSLAEHLGIKPEEVMAIGDQENDIA 226

                        250       260       270
                 ....*....|....*....|....*....|....*
gi 494884502 227 MLRFAGCGVAMGNGTDEVKQAADRVTGSNEADGIA 261
Cdd:PRK10513 227 MIEYAGVGVAMGNAIPSVKEVAQFVTKSNLEDGVA 261
HAD_YbiV-Like cd07518
Escherichia coli YbiV sugar phosphatase/phosphotransferase and related proteins; belongs to ...
 7-265 2.87e-27

Escherichia coli YbiV sugar phosphatase/phosphotransferase and related proteins; belongs to the haloacid dehalogenase-like superfamily; Escherichia coli YbiV can act as both a sugar phosphatase and as a phosphotransferase. Members of this family belong 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: 319820 [Multi-domain]  Cd Length: 184  Bit Score: 103.82  E-value: 2.87e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494884502   7 LIALDLDGTLLKDDKT-ISPETARTIQTLKEAGHHVCISTGRPFrsssmyydelglttpivnfngafvhhpkdeswgryh 85
Cdd:cd07518    2 LIATDMDGTFLNDDKTyDHERFFAILDQLLKKGIKFVVASGRQY------------------------------------ 45

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494884502  86 tslsvdvvrqlaeltetYQIHNVLAEIIDDVYFHYHdehlieafhmNTANVtfgdlretvqedVTSVLIHAKEEDVADIR 165
Cdd:cd07518   46 -----------------YQLISFFPEIKDEMSFVAE----------NGAVV------------YFKFTLNVPDEAAPDII 86

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494884502 166 AHLSDVHAEviDHRRWAAPWHVIEIIKHGMNKAVGLKKISDYYQVPRERIIAFGDEDNDLEMLRFAGCGVAMGNGTDEVK 245
Cdd:cd07518   87 DELNQKFGG--ILRAVTSGFGSIDIIPPGVNKATGLKQLLKHWGISPDEVMAFGDGGNDIEMLKYAGYSYAMENAPEEVK 164

                        250       260
                 ....*....|....*....|
gi 494884502 246 QAADRVTGSNEADGIAEFLK 265
Cdd:cd07518  165 AAAKYVAPSNNENGVLQVIE 184
PRK01158 PRK01158
phosphoglycolate phosphatase; Provisional
 3-265 2.69e-23

phosphoglycolate phosphatase; Provisional


Pssm-ID: 234910 [Multi-domain]  Cd Length: 230  Bit Score: 94.65  E-value: 2.69e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494884502   3 TKPYLIALDLDGTLLKDDKTISPETARTIQTLKEAGHHVCISTGR--PF-RSSSMYydeLGLTTPIVNFNGAFVHHPKDE 79
Cdd:PRK01158   1 MKIKAIAIDIDGTITDKDRRLSLKAVEAIRKAEKLGIPVILATGNvlCFaRAAAKL---IGTSGPVIAENGGVISVGFDG 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494884502  80 SwGRYHTSLSvDVVRQLAELTETYQIHNVLAEIIDDVYfhyhdehlieafhmntaNVTFGDLRETVQ-EDVTSVLihakE 158
Cdd:PRK01158  78 K-RIFLGDIE-ECEKAYSELKKRFPEASTSLTKLDPDY-----------------RKTEVALRRTVPvEEVRELL----E 134

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494884502 159 EDVADIrahlsdvhaEVIDhRRWAapWHvieIIKHGMNKAVGLKKISDYYQVPRERIIAFGDEDNDLEMLRFAGCGVAMG 238
Cdd:PRK01158 135 ELGLDL---------EIVD-SGFA--IH---IKSPGVNKGTGLKKLAELMGIDPEEVAAIGDSENDLEMFEVAGFGVAVA 199

                        250       260
                 ....*....|....*....|....*..
gi 494884502 239 NGTDEVKQAADRVTGSNEADGIAEFLK 265
Cdd:PRK01158 200 NADEELKEAADYVTEKSYGEGVAEAIE 226
HAD-SF-IIB TIGR01484
HAD-superfamily hydrolase, subfamily IIB; This subfamily falls within the Haloacid ...
 7-237 3.98e-20

HAD-superfamily hydrolase, subfamily IIB; This subfamily falls within the Haloacid Dehalogenase (HAD) superfamily of aspartate-nucleophile hydrolases. The Class II subfamilies are characterized by a domain that is located between the second and third conserved catalytic motifs of the superfamily domain. The IIB subfamily is distinguished from the IIA subfamily (TIGR01460) by homology and the predicted secondary structure of this domain by PSI-PRED. The IIB subfamily's Class II domain has the following predicted structure: Helix-Sheet-Sheet-(Helix or Sheet)-Helix-Sheet-(variable)-Helix-Sheet-Sheet. The IIB subfamily consists of Trehalose-6-phosphatase (TIGR00685), plant and cyanobacterial Sucrose-phosphatase and a closely related group of bacterial and archaeal sequences, eukaryotic phosphomannomutase (pfam03332), a large subfamily ("Cof-like hydrolases", TIGR00099) containing many closely related bacterial sequences, a hypothetical equivalog containing the E. coli YedP protein, as well as two small clusters containing OMNI|TC0379 and OMNI|SA2196 whose relationship to the other groups is unclear. [Unknown function, Enzymes of unknown specificity]


Pssm-ID: 273651 [Multi-domain]  Cd Length: 207  Bit Score: 85.51  E-value: 3.98e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494884502    7 LIALDLDGTLLK-DDKTISPETARTIQTLKEAGHHVCISTGRPFRSSSMYYDELGLTTPIVNFNGAFVHHPKDESWGRYh 85
Cdd:TIGR01484   1 LLFFDLDGTLLDpNAHELSPETIEALERLREAGVKVVIVTGRSLAEIKELLKQLNLPLPLIAENGALIFYPGEILYIEP- 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494884502   86 tslsvdvvRQLAELTETYQIHNVLAEIiddvyfHYHDEHLIEAFH--MNTAnVTFGDLRETVQEDVTSVLIHAKEedVAD 163
Cdd:TIGR01484  80 --------SDVFEEILGIKFEEIGAEL------KSLSEHYVGTFIedKAIA-VAIHYVGAELGQELDSKMRERLE--KIG 142

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 494884502  164 IRAHLSDVHAEVIdhrrwaapwHVIEIIKHGMNKAVGLKKISDYYQVPRERIIAFGDEDNDLEMLRFAGCGVAM 237
Cdd:TIGR01484 143 RNDLELEAIYSGK---------TDLEVLPAGVNKGSALQALLQELNGKKDEILAFGDSGNDEEMFEVAGLAVAV 207
HAD_Pase cd07514
phosphatase, similar to Thermoplasma acidophilum TA0175 phosphoglycolate phosphatase (PCPase), ...
 194-268 1.98e-18

phosphatase, similar to Thermoplasma acidophilum TA0175 phosphoglycolate phosphatase (PCPase), and Pyrococcus horikoshii PH1421, a magnesium-dependent phosphatase; belongs to the haloacid dehalogenase-like superfamily; Thermoplasma acidophilum TA0175 phosphoglycolate phosphatase (PGPase) catalyzes the magnesium-dependent dephosphorylation of phosphoglycolate. This family also includes Pyrococcus horikoshii OT3 PH1421, a magnesium-dependent phosphatase. 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: 319816 [Multi-domain]  Cd Length: 139  Bit Score: 79.17  E-value: 1.98e-18
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 494884502 194 GMNKAVGLKKISDYYQVPRERIIAFGDEDNDLEMLRFAGCGVAMGNGTDEVKQAADRVTGSNEADGIAEFLKSYF 268
Cdd:cd07514   65 GVDKGTGLEKLAERLGIDPEEVLAIGDSENDIEMFKVAGFKVAVANADEELKEAADYVTDASYGDGVLEAIDKLL 139
Pglycolate_arch TIGR01487
phosphoglycolate phosphatase, TA0175-type; This group of Archaeal sequences, now known to be ...
 5-264 9.98e-17

phosphoglycolate phosphatase, TA0175-type; This group of Archaeal sequences, now known to be phosphoglycolate phosphatases, is most closely related to the sucrose-phosphate phosphatases from plants and cyanobacteria (TIGR01485). Together, these two models comprise a subfamily model (TIGR01482). TIGR01482, in turn, is a member of the IIB subfamily (TIGR01484) of the Haloacid Dehalogenase (HAD) superfamily of aspartate-nucleophile hydrolases.


Pssm-ID: 273652 [Multi-domain]  Cd Length: 215  Bit Score: 76.70  E-value: 9.98e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494884502    5 PYLIALDLDGTLLKDDKTISPETARTIQTLKEAGHHVCISTGRPFRSSSMYYDELGLTTPIVNFNGAFV-HHPKDESWGR 83
Cdd:TIGR01487   1 IKLVAIDIDGTLTDPNRMISERAIEAIRKAEKKGIPVSLVTGNTVPFARALAVLIGTSGPVVAENGGVIfYNKEDIFLAN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494884502   84 YHTSLSVDVVRQLAELTETYQihNVLAEIIDdvyfhyhdehlieafhmntanvtFGDlRETVQEDVTSVLIHAKEEDVAD 163
Cdd:TIGR01487  81 MEEEWFLDEEKKKRFPRDRLS--NEYPRASL-----------------------VIM-REGKDVDEVREIIKERGLNLVA 134

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494884502  164 IRahlSDVHaevidhrrwaapwhvieIIKHGMNKAVGLKKISDYYQVPRERIIAFGDEDNDLEMLRFAGCGVAMGNGTDE 243
Cdd:TIGR01487 135 SG---FAIH-----------------IMKKGVDKGVGVEKLKELLGIKPEEVAAIGDSENDIDLFRVVGFKVAVANADDQ 194

                         250       260
                  ....*....|....*....|.
gi 494884502  244 VKQAADRVTGSNEADGIAEFL 264
Cdd:TIGR01487 195 LKEIADYVTSNPYGEGVVEVL 215
PRK15126 PRK15126
HMP-PP phosphatase;
7-264 2.94e-16

HMP-PP phosphatase;


Pssm-ID: 185080 [Multi-domain]  Cd Length: 272  Bit Score: 76.27  E-value: 2.94e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494884502   7 LIALDLDGTLLKDDKTISPETARTIQTLKEAGHHVCISTGRPFRSSSMYYDELGLTTPIVNFNGAFVHHPKDESWgrYHT 86
Cdd:PRK15126   4 LAAFDMDGTLLMPDHHLGEKTLSTLARLRERDITLTFATGRHVLEMQHILGALSLDAYLITGNGTRVHSLEGELL--HRQ 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494884502  87 SLSVDVVRQLaeLTETYQIHNVLAEIIDDVYF-HYHDEHLIEAFHMNTANVTFGDLRETVQEDVTSVLIHAKEEDVADIR 165
Cdd:PRK15126  82 DLPADVAELV--LHQQWDTRASMHVFNDDGWFtGKEIPALLQAHVYSGFRYQLIDLKRLPAHGVTKICFCGDHDDLTRLQ 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494884502 166 AHLSDVHAEVIDHRRWAApwHVIEIIKHGMNKAVGLKKISDYYQVPRERIIAFGDEDNDLEMLRFAGCGVAMGNGTDEVK 245
Cdd:PRK15126 160 IQLNEALGERAHLCFSAT--DCLEVLPVGCNKGAALAVLSQHLGLSLADCMAFGDAMNDREMLGSVGRGFIMGNAMPQLR 237

                        250       260
                 ....*....|....*....|.
gi 494884502 246 QAAD--RVTGSNEADGIAEFL 264
Cdd:PRK15126 238 AELPhlPVIGHCRNQAVSHYL 258
PRK00192 PRK00192
mannosyl-3-phosphoglycerate phosphatase; Reviewed
 4-239 8.93e-16

mannosyl-3-phosphoglycerate phosphatase; Reviewed


Pssm-ID: 234684 [Multi-domain]  Cd Length: 273  Bit Score: 74.98  E-value: 8.93e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494884502   4 KPYLIALDLDGTLLkDDKTISPETAR-TIQTLKEAGHHVCISTG------RPFRsssmyyDELGLTTP-IVNfNGAFVHH 75
Cdd:PRK00192   3 MKLLVFTDLDGTLL-DHHTYSYEPAKpALKALKEKGIPVIPCTSktaaevEVLR------KELGLEDPfIVE-NGAAIYI 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494884502  76 PKDESWGRYHTSLSVDVVRQLaELTETYQ-IHNVLAEIIDDVyfhyhDEHLIeafhmntanvTFGDLR-ETVQE------ 147
Cdd:PRK00192  75 PKNYFPFQPDGERLKGDYWVI-ELGPPYEeLREILDEISDEL-----GYPLK----------GFGDLSaEEVAEltglsg 138

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494884502 148 -----------DVTsVLIHAKEEDVADIRAHLSDVHAEVIDHRRWaapWHVIeiikHGMNKAVGLKKISDYYQVPRER-I 215
Cdd:PRK00192 139 esarlakdrefSEP-FLWNGSEAAKERFEEALKRLGLKVTRGGRF---LHLL----GGGDKGKAVRWLKELYRRQDGVeT 210

                        250       260
                 ....*....|....*....|....
gi 494884502 216 IAFGDEDNDLEMLRFAGCGVAMGN 239
Cdd:PRK00192 211 IALGDSPNDLPMLEAADIAVVVPG 234
PRK10976 PRK10976
putative hydrolase; Provisional
 6-268 5.39e-15

putative hydrolase; Provisional


Pssm-ID: 182878 [Multi-domain]  Cd Length: 266  Bit Score: 72.77  E-value: 5.39e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494884502   6 YLIALDLDGTLLKDDKTISPETARTIQTLKEAGHHVCISTGRPFRSSSMYYDELGLTTPIVNFNGAFVHHPKDESWGRYh 85
Cdd:PRK10976   3 QVVASDLDGTLLSPDHTLSPYAKETLKLLTARGIHFVFATGRHHVDVGQIRDNLEIKSYMITSNGARVHDTDGNLIFSH- 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494884502  86 tSLSVDVVRQLaeltetYQIHNVLAEIIDDVYfhYHDEHLIeafhmntaNVTFGDLRETVQEDVTSVLIHAKEEDVADIR 165
Cdd:PRK10976  82 -NLDRDIASDL------FGVVHDNPDIITNVY--RDDEWFM--------NRHRPEEMRFFKEAVFKYQLYEPGLLEPDGV 144

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494884502 166 AHL---SDVHAEVID-----HRRWAAPWHV-------IEIIKHGMNKAVGLKKISDYYQVPRERIIAFGDEDNDLEMLRF 230
Cdd:PRK10976 145 SKVfftCDSHEKLLPleqaiNARWGDRVNVsfstltcLEVMAGGVSKGHALEAVAKKLGYSLKDCIAFGDGMNDAEMLSM 224

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|
gi 494884502 231 AGCGVAMGNGTDEVKQAAD--RVTGSNEADGIAEFLKSYF 268
Cdd:PRK10976 225 AGKGCIMGNAHQRLKDLLPelEVIGSNADDAVPHYLRKLY 264
HAD_SPP cd02605
sucrose-phosphatase, similar to Synechocystis sp PCC 6803 SPP; Sucrose-phosphatase (SPP; EC 3. ...
 7-267 1.50e-14

sucrose-phosphatase, similar to Synechocystis sp PCC 6803 SPP; Sucrose-phosphatase (SPP; EC 3.1.3.24) catalyzes the dephosphorylation of sucrose-6(F)-phosphate (Suc6P)-the final step in the pathway of sucrose biosynthesis in plants and cyanobacteria. 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: 319792 [Multi-domain]  Cd Length: 245  Bit Score: 71.23  E-value: 1.50e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494884502   7 LIALDLDGTLLKDDktISPETARTIQTLKEA-----GHHVCISTGRPFRSSSMYYDELGLTTP--IVNFNGAFVHHPKDE 79
Cdd:cd02605    1 LLVSDLDETLVGHD--TNLQALERLQDLLEQltadnDVILVYATGRSPESVLELIKEVMLPKPdfIISDVGTEIYYGESG 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494884502  80 SWGR---YHTSLSVDVVRQLaeltetyqihnvLAEIIDDVyfhyHDEHLIEAFHMNTANVTFgDLRETVQEDVTSVLihA 156
Cdd:cd02605   79 YLEPdtyWNEVLSEGWERFL------------FEAIADLF----KQLKPQSELEQNPHKISF-YLDPQNDAAVIEQL--E 139

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494884502 157 KEEDVADIRAHLSDVHAEVIDhrrwaapwhvIEIIKHGMNKAVGLKKISDYYQVPRERIIAFGDEDNDLEMLRFAGCGVA 236
Cdd:cd02605  140 EMLLKAGLTVRIIYSSGLAYD----------LDILPLGAGKGEALRYLQEKWNFPPERTLVCGDSGNDIALLSTGTRGVI 209

                        250       260       270
                 ....*....|....*....|....*....|....*.
gi 494884502 237 MGNGTDEVKQAADRVTG-----SNEADGIAEFLKSY 267
Cdd:cd02605  210 VGNAQPELLKWADRVTRsrlakGPYAGGILEGLAHF 245
PLN02887 PLN02887
hydrolase family protein
 8-267 2.31e-14

hydrolase family protein


Pssm-ID: 215479 [Multi-domain]  Cd Length: 580  Bit Score: 72.60  E-value: 2.31e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494884502   8 IALDLDGTLLKDDKTISPETARTIQTLKEAGHHVCISTG--RPFRSSSMYYDELGLTTPIVNFNGAFVHHPKDESWGR-- 83
Cdd:PLN02887 311 IFCDMDGTLLNSKSQISETNAKALKEALSRGVKVVIATGkaRPAVIDILKMVDLAGKDGIISESSPGVFLQGLLVYGRqg 390

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494884502  84 ---YHTSLSVDVVRQLAELTETYQIHNVLAE-----------IIDDVYFHYHD---------EHLIEAfhMNTANVTFGD 140
Cdd:PLN02887 391 reiYRSNLDQEVCREACLYSLEHKIPLIAFSqdrcltlfdhpLVDSLHTIYHEpkaeimssvDQLLAA--ADIQKVIFLD 468

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494884502 141 lretVQEDVTSVLIHAKEEDVADiRAHLSDvhaevidhrrwAAPwHVIEIIKHGMNKAVGLKKISDYYQVPRERIIAFGD 220
Cdd:PLN02887 469 ----TAEGVSSVLRPYWSEATGD-RANVVQ-----------AQP-DMLEIVPPGTSKGNGVKMLLNHLGVSPDEIMAIGD 531

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*..
gi 494884502 221 EDNDLEMLRFAGCGVAMGNGTDEVKQAADRVTGSNEADGIAEFLKSY 267
Cdd:PLN02887 532 GENDIEMLQLASLGVALSNGAEKTKAVADVIGVSNDEDGVADAIYRY 578
HAD-SF-IIB-MPGP TIGR01486
mannosyl-3-phosphoglycerate phosphatase family; This small group of proteins is a member of ...
 7-243 5.49e-11

mannosyl-3-phosphoglycerate phosphatase family; This small group of proteins is a member of the IIB subfamily (TIGR01484) of the Haloacid Dehalogenase (HAD) superfamily of aspartate-nucleophile hydrolases. Several members of this family from thermophiles (and from Dehalococcoides ethenogenes) are now known to act as mannosyl-3-phosphoglycerate (MPG) phosphatase. In these cases, the enzyme acts after MPG synthase to make the compatible solute mannosylglycerate. We propose that other mesophilic members of this family do not act as mannosyl-3-phosphoglycerate phosphatase. A member of this family is found in Escherichia coli, which appears to lack MPG synthase. Mannosylglycerate is imported in E. coli by phosphoenolpyruvate-dependent transporter (), but it appears the phosphorylation is not on the glycerate moiety, that the phosphorylated import is degraded by an alpha-mannosidase from an adjacent gene, and that E. coli would have no pathway to obtain MPG.


Pssm-ID: 130550 [Multi-domain]  Cd Length: 256  Bit Score: 61.26  E-value: 5.49e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494884502    7 LIALDLDGTLLkDDKTISPETAR-TIQTLKEAGHHVCISTGRPFRSSSMYYDELGLTTPIVNFNGAFVHHPKDeswgryh 85
Cdd:TIGR01486   1 WIFTDLDGTLL-DPHGYDWGPAKeVLERLQELGIPVIPCTSKTAAEVEYLRKELGLEDPFIVENGGAIYGPRG------- 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494884502   86 tSLSVDVVRQLaELTETYQI----HNVLAEIIDDVYFHYHDEHLIEAfhmntANVTfGDLRETV---QEDVTSVLIHAKE 158
Cdd:TIGR01486  73 -WRPEPEYPVI-ALGIPYEKirarLRELSEELGFKFRGLGDLTDEEI-----AELT-GLSRELArlaQRREYSETILWSE 144

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494884502  159 EDVADIRAHLSDVHAEVIDHRRWaapWHVIEIikhGMNKAVGLKKISDYYQVPRERI--IAFGDEDNDLEMLRFAGCGVA 236
Cdd:TIGR01486 145 ERRERFTEALVAVGLEVTHGGRF---YHVLGA---GSDKGKAVNALKAFYNQPGGAIkvVGLGDSPNDLPLLEVVDLAVV 218


                  ....*..
gi 494884502  237 MGNGTDE 243
Cdd:TIGR01486 219 VPGPNGP 225
YedP COG3769
Mannosyl-3-phosphoglycerate phosphatase YedP/MpgP, HAD superfamily [Carbohydrate transport and ...
 3-228 4.89e-09

Mannosyl-3-phosphoglycerate phosphatase YedP/MpgP, HAD superfamily [Carbohydrate transport and metabolism];


Pssm-ID: 442983 [Multi-domain]  Cd Length: 268  Bit Score: 55.60  E-value: 4.89e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494884502   3 TKPYLIALDLDGTLLkDDKTISPETAR-TIQTLKEAGHHVCIST------GRPFRsssmyyDELGLTTP-IVNfNGAFVH 74
Cdd:COG3769    1 MPPLLVFTDLDGTLL-DHDTYSWAAALpALARLKARGIPVILNTsktaaeVEPLR------QELGLSDPfIVE-NGAAIF 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494884502  75 HPKDESWGRYHTSLSVDVVRQlaELTETYQ-IHNVLAEIIDDVYFHYhdehlieafhmntanVTFGDLreTVQE--DVT- 150
Cdd:COG3769   73 IPKGYFAFPSGTADIDGYWVI--ELGKPYAeIRAVLEQLREELGFKF---------------TGFGDM--SAEEvaELTg 133

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494884502 151 ----------------SVLIHAKEEDVADIRAHLSDVHAEVIDHRRWaapWHVIeiikHGMNKAVGLKKISDYYQVPRE- 213
Cdd:COG3769  134 lsleqaalakqrefsePLLWLGSDEALERFIAALAALGLTVLRGGRF---LHLM----GGADKGKAVRWLVEQYRQRFGk 206

                        250
                 ....*....|....*..
gi 494884502 214 --RIIAFGDEDNDLEML 228
Cdd:COG3769  207 nvVTIALGDSPNDIPML 223
SerB COG0560
Phosphoserine phosphatase [Amino acid transport and metabolism]; Phosphoserine phosphatase is ...
 187-253 2.82e-08

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: 52.92  E-value: 2.82e-08
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 494884502 187 VIEIIKHGMNKAVGLKKISDYYQVPRERIIAFGDEDNDLEMLRFAGCGVAMgNGTDEVKQAADRVTG 253
Cdd:COG0560  146 VVGPIVDGEGKAEALRELAAELGIDLEQSYAYGDSANDLPMLEAAGLPVAV-NPDPALREAADRERG 211
S6PP pfam05116
Sucrose-6F-phosphate phosphohydrolase; This family consists of Sucrose-6F-phosphate ...
 4-267 1.40e-07

Sucrose-6F-phosphate phosphohydrolase; This family consists of Sucrose-6F-phosphate phosphohydrolase proteins found in plants and cyanobacteria. Sucrose-6(F)-phosphate phosphohydrolase catalyzes the final step in the pathway of sucrose biosynthesis.


Pssm-ID: 428314 [Multi-domain]  Cd Length: 246  Bit Score: 51.11  E-value: 1.40e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494884502    4 KPYLIALDLDGTLLK-DDKTIspetARTIQTLKEAGHHV--CISTGRPFRSSSMYYDELGLTTP--IVNFNGAFVHHPK- 77
Cdd:pfam05116   1 PPLLLVSDLDNTLVDgDNEAL----ARLNQLLEAYRPDVglVFATGRSLDSAKELLKEKPLPTPdyLITSVGTEIYYGPs 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494884502   78 ---DESWGRY-----HTSLSVDVVRQLAELT---ETYQ-IHNVlaeiiddvYFHYHDEHLieafhmntanvtfgdlretv 145
Cdd:pfam05116  77 lvpDQSWQEHldyhwDRQAVVEALAKFPGLTlqpEEEQrPHKV--------SYFLDPEAA-------------------- 128

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494884502  146 qedvtsvlihakEEDVADIRAHL--SDVHAEVIDHRRWAapwhvIEIIKHGMNKAVGLKKISDYYQVPRERIIAFGDEDN 223
Cdd:pfam05116 129 ------------AAVLAELEQLLrkRGLDVKVIYSSGRD-----LDILPLRASKGEALRYLALKLGLPLENTLVCGDSGN 191

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|...
gi 494884502  224 DLEMLRFAGCGVAMGNGTDEVKQAADRVTGSNE---------ADGIAEFLKSY 267
Cdd:pfam05116 192 DEELFIGGTRGVVVGNAQPELLQWYLENARDNPriyfasgrcAGGILEGIRHF 244
HAD_Pase cd07507
haloacid dehalogenase-like superfamily phosphatase similar to Pyrococcus horikoshii ...
 7-229 1.59e-05

haloacid dehalogenase-like superfamily phosphatase similar to Pyrococcus horikoshii mannosyl-3-phosphoglycerate phosphatase and Persephonella marina glucosyl-3-phosphoglycerate phosphatase; This family includes Pyrococcus horikoshii and Thermus thermophilus HB27 mannosyl-3-phosphoglycerate phosphatases (MpgPs) which catalyze the dephosphorylation of alpha-mannosyl-3-phosphoglycerate (MPG) to produce alpha-mannosylglycerate (MG), and Persephonella marina glucosyl-3-phosphoglycerate phosphatase (GpgP) which catalyzes the dephosphorylation of glucosyl-3-phosphoglycerate (GPG) to produce glucosylglycerate (GG). It also includes Methanococcoides burtonii MpgP protein which is able to dephosphorylate GPG to GG, and MPG to MG. Similar flexibilities in substrate specificity have been confirmed in vitro for the MpgPs from Thermus thermophiles and Pyrococcus horikoshii. Screens with natural substrates have not yet detected activity for another member Escherichia Coli YedP. Members of this family belong 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: 319810 [Multi-domain]  Cd Length: 255  Bit Score: 45.05  E-value: 1.59e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494884502   7 LIALDLDGTLLkDDKTISPETAR-TIQTLKEAGHHVCISTGRPFRSSSMYYDELGLTTPIVNFNGAFVHHPKD--ESWGR 83
Cdd:cd07507    1 VIFTDLDGTLL-DHHTYSFDPARpALERLKERGIPVVPCTSKTRAEVEYLRKELGIEDPFIVENGGAIFIPRGyfKFPGR 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494884502  84 YHTSLSVDVVRQLAELTETYQIHNVLAEIIDDVYFHYHD--EHLIEAF-HMNTANVTFGDLRETvqeDVTsVLIHAKEED 160
Cdd:cd07507   80 CKSEGGYEVIELGKPYREIRAALEKIREETGFKITGFGDltEEEIAELtGLPRERAALAKEREY---SET-IILRSDEEE 155

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 494884502 161 VADIRAHLSDVHAEVIDHRRwaaPWHVieiikHGMN--KAVGLKKISDYYQVPRERI--IAFGDEDNDLEMLR 229
Cdd:cd07507  156 DEKVLEALEERGLKITKGGR---FYHV-----LGAGadKGKAVAILAALYRQLYEAIvtVGLGDSPNDLPMLE 220
OtsB COG1877
Trehalose-6-phosphate phosphatase [Carbohydrate transport and metabolism];
3-240 1.09e-04

Trehalose-6-phosphate phosphatase [Carbohydrate transport and metabolism];


Pssm-ID: 441481 [Multi-domain]  Cd Length: 242  Bit Score: 42.49  E-value: 1.09e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494884502   3 TKPYLIALDLDGTLLK-----DDKTISPETARTIQTLKEA-GHHVCISTGRPfrsssmyYDELGLTTPIVNFN-----GA 71
Cdd:COG1877    1 APRLLLFLDFDGTLAPivpdpDAARPPPELRELLRRLAARpGGAVAIVSGRD-------LADLDRLLGPLGLPlagshGA 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494884502  72 FVHHPkDESWGRyhTSLSVDVVRQLAELTEtyqihnVLAEIIDDvyfhyHDEHLIEafhmntanvtfgdlretvqEDVTS 151
Cdd:COG1877   74 ERRLP-GGEWEV--LPLAAEAPEWLDALRA------ALEALAAR-----TPGVLVE-------------------DKGAS 120

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494884502 152 VLIH---AKEEDVADIRAHLSDVHAevidhrRWAAPWH------VIEIIKHGMNKAVGLKKISDYYQVPReRIIAFGDED 222
Cdd:COG1877  121 LALHyrqAPPEEAEELRAALRELAA------RLGPGLEvlpgkkVVELRPAGVDKGRAVRALLAELPFGR-APVFIGDDV 193

                        250       260
                 ....*....|....*....|.
gi 494884502 223 NDLEMLRFA---GCGVAMGNG 240
Cdd:COG1877  194 TDEDAFAALpagGLGIKVGSG 214
HAD_TPP cd01627
trehalose-phosphate phosphatase similar to Escherichia coli trehalose-6-phosphate phosphatase ...
 7-240 1.35e-04

trehalose-phosphate phosphatase similar to Escherichia coli trehalose-6-phosphate phosphatase OtsB and Saccharomyces cerevisiae trehalose-phosphatase TPS2; Trehalose biosynthesis in bacteria is known through three pathways - OtsAB, TreYZ and TreS. The OtsAB pathway, also known as the trehalose 6-phosphate synthase (TSP)/ Trehalose-6-phosphate phosphatase (TPP) pathway, is the most common route known to be involved in the stress response of Escherichia coli. It involves converting glucose-6-phosphate and UDP-glucose to form trehalose-6-phosphate (T6P), catalyzed by TPS, the product of the otsA gene, this step is followed by the dephosphorylation of T6P to yield trehalose and inorganic phosphate, catalyzed by a specific TPP, the product of otsB gene. This OtsAB (or TSP/TPP) pathway, is also the most common route known to be involved in the stress response of yeast In Saccharomyces cerevisiae, the corresponding enzymes, TPS1p and TPS2p, form a multimeric synthase complex together with additional regulatory subunits encoded by Tsl1 and Tps3. Trehalose is a common disaccharide accumulated by organisms as a reservation of carbohydrate and in response to unfavorable growth conditions. 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: 319767 [Multi-domain]  Cd Length: 228  Bit Score: 42.28  E-value: 1.35e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494884502   7 LIALDLDGTLLK-----DDKTISPETARTIQTLKE-AGHHVCISTGRPFRSSSMYYDELGLttPIVNFNGAFVHHPKDES 80
Cdd:cd01627    1 LLFLDYDGTLAPivpdpDAAVPSPELLEALKKLAAdPKNAVAIVSGRDLDDLDKWLGLPGI--GLAGEHGAEIRLPGGGE 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494884502  81 WgryhtslsvdvvRQLAEltetyqihNVLAEIIDDVyfhyhdEHLIEAFHMNTAnvtfgdlRETVQEDVTSVLIH---AK 157
Cdd:cd01627   79 W------------VTLAP--------KADLEWKEEV------EAIFKYFTERTP-------GSLVEDKGASLAWHyrnAD 125

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494884502 158 EEDVADIRAHLSDVHAEVIDHRRWAAPWHVIEIIKHGMNKAVGLKKISDYYQVPRERIIAFGDEDNDLEMLRFA----GC 233
Cdd:cd01627  126 PEGARAALELALHLASDLLKALEVVPGKKVVEVRPVGVNKGEAVERILGELPFAGDFVLCAGDDVTDEDAFRALngegGF 205


                 ....*..
gi 494884502 234 GVAMGNG 240
Cdd:cd01627  206 SVKVGEG 212
HAD_PSP cd07500
phosphoserine phosphatase (PSP), similar to Methanococcus Jannaschii PSP and Saccharomyces ...
 196-236 5.55e-04

phosphoserine phosphatase (PSP), similar to Methanococcus Jannaschii PSP and Saccharomyces cerevisiae SER2p; This family includes Methanococcus jannaschii PSP, and Saccharomyces cerevisiae phosphoserine phosphatase SER2p, EC 3.1.3.3, which participates in a pathway whereby serine and glycine are synthesized from the glycolytic intermediate 3-phosphoglycerate; phosphoserine phosphatase catalyzes the hydrolysis of phospho-L-serine to L-serine and inorganic phosphate, the third reaction in this pathway. 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: 319803 [Multi-domain]  Cd Length: 180  Bit Score: 39.84  E-value: 5.55e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 494884502 196 NKAVGLKKISDYYQVPRERIIAFGDEDNDLEMLRFAGCGVA 236
Cdd:cd07500  137 RKAETLQELAARLGIPLEQTVAVGDGANDLPMLKAAGLGIA 177
PRK14502 PRK14502
bifunctional mannosyl-3-phosphoglycerate synthase/mannosyl-3 phosphoglycerate phosphatase; ...
 7-228 7.69e-04

bifunctional mannosyl-3-phosphoglycerate synthase/mannosyl-3 phosphoglycerate phosphatase; Provisional


Pssm-ID: 184713 [Multi-domain]  Cd Length: 694  Bit Score: 40.68  E-value: 7.69e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494884502   7 LIALDLDGTLLKDDKTISPETARTIQTLKEAGHHVCISTGRPFRSSSMYYDELGLTTPIVNFNGAFVHHPKDeswgRYHT 86
Cdd:PRK14502 418 IVYTDLDGTLLNPLTYSYSTALDALRLLKDKELPLVFCSAKTMGEQDLYRNELGIKDPFITENGGAIFIPKD----YFRL 493

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494884502  87 SLSVDVVRQ---LAELTETYQ-IHNVLAEIIDDVyfhyhDEHLIEAFHMNTANVT-FGDLreTVQEDVTSVLIHAKEEDV 161
Cdd:PRK14502 494 PFAYDRVAGnylVIELGMAYKdIRHILKKALAEA-----CTEIENSEKAGNIFITsFGDM--SVEDVSRLTDLNLKQAEL 566

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494884502 162 ADIRAHLSDVHaevIDHRRWAAPWHVIEIIKHGMNKAVG---------------LKKISDYYQVPRERIIAF--GDEDND 224
Cdd:PRK14502 567 AKQREYSETVH---IEGDKRSTNIVLNHIQQSGLEYSFGgrfyevtggndkgkaIKILNELFRLNFGNIHTFglGDSEND 643


                 ....
gi 494884502 225 LEML 228
Cdd:PRK14502 644 YSML 647
Hydrolase_6 pfam13344
Haloacid dehalogenase-like hydrolase; This family is part of the HAD superfamily.
 8-59 8.14e-04

Haloacid dehalogenase-like hydrolase; This family is part of the HAD superfamily.


Pssm-ID: 433132  Cd Length: 101  Bit Score: 37.83  E-value: 8.14e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 494884502    8 IALDLDGTLLKDDKTIsPETARTIQTLKEAGHHVCISTGRPFRSSSMYYDEL 59
Cdd:pfam13344   1 FLFDIDGVLWRGGEPI-PGAAEALRALRAAGKPVVFVTNNSSRSREEYAEKL 51
HAD_KDO-like cd01630
haloacid dehalogenase-like (HAD) hydrolase, similar to Escherichia coli ...
 172-252 9.12e-04

haloacid dehalogenase-like (HAD) hydrolase, similar to Escherichia coli 3-deoxy-D-manno-octulosonate 8-phosphate (KDO 8-P) phosphatase KdsC, and rainbow trout N-acylneuraminate cytidylyltransferase; KDO 8-P phosphatase catalyzes the hydrolysis of KDO 8-P to KDO (3-deoxy-D-manno-octulosonate) and inorganic phosphate and is the last enzyme in the KDO biosynthetic pathway. KDO is an 8-carbon sugar that links the lipid A and polysaccharide moieties of the lipopolysaccharide region in Gram-negative bacteria. An interruption in KDO biosynthesis leads to the accumulation of lipid A precursors and subsequent arrest in cell growth. The KDO biosynthesis pathway involves five sequential enzymatic reactions. This family also includes rainbow trout CMP-sialic acid synthetase which effectively converts both deaminoneuraminic acid (KDN, 2-keto-3-deoxy-D-glycero-D-galacto-nononic acid) and N-acetylneuraminic acid (Neu5Ac) to CMP-KDN and CMP-Neu5Ac, respectively. 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: 319769 [Multi-domain]  Cd Length: 146  Bit Score: 38.66  E-value: 9.12e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494884502 172 HAEVIDHRrwAAPWHVIEIIKHGMNKAVGLKKISDYYQVPRERIIAFGDEDNDLEMLRFAGCGVAMGNGTDEVKQAADRV 251
Cdd:cd01630   54 QSEAVRRR--AKELGIEDLFQGVKDKLEALEELLEKLGLSDEEVAYMGDDLPDLPVMKRVGLSVAPADAHPEVREAADYV 131


                 .
gi 494884502 252 T 252
Cdd:cd01630  132 T 132
serB PRK11133
phosphoserine phosphatase; Provisional
 186-236 9.97e-04

phosphoserine phosphatase; Provisional


Pssm-ID: 182988 [Multi-domain]  Cd Length: 322  Bit Score: 39.93  E-value: 9.97e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 494884502 186 HVIEIIKHGMNKAVGLKKISDYYQVPRERIIAFGDEDNDLEMLRFAGCGVA 236
Cdd:PRK11133 238 NVLGDIVDAQYKADTLTRLAQEYEIPLAQTVAIGDGANDLPMIKAAGLGIA 288
Hydrolase pfam00702
haloacid dehalogenase-like hydrolase; This family is structurally different from the alpha ...
 7-232 1.18e-03

haloacid dehalogenase-like hydrolase; This family is structurally different from the alpha/beta hydrolase family (pfam00561). This family includes L-2-haloacid dehalogenase, epoxide hydrolases and phosphatases. The structure of the family consists of two domains. One is an inserted four helix bundle, which is the least well conserved region of the alignment, between residues 16 and 96 of Swiss:P24069. The rest of the fold is composed of the core alpha/beta domain. Those members with the characteriztic DxD triad at the N-terminus are probably phosphatidylglycerolphosphate (PGP) phosphatases involved in cardiolipin biosynthesis in the mitochondria.


Pssm-ID: 459910 [Multi-domain]  Cd Length: 191  Bit Score: 39.11  E-value: 1.18e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494884502    7 LIALDLDGTLLKddktISPETARTIqtlkeaghhvcistgrpfrsssmyyDELGLTTPIVNfngAFVHHPKDESWG--RY 84
Cdd:pfam00702   3 AVVFDLDGTLTD----GEPVVTEAI-------------------------AELASEHPLAK---AIVAAAEDLPIPveDF 50

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494884502   85 HTSLSVDVVRQLAELTETYQIHNVLAEIIDDVYFHYHDEhlieafhmntanVTFGDLRETVQEDVTSVLIHAKEEDV--- 161
Cdd:pfam00702  51 TARLLLGKRDWLEELDILRGLVETLEAEGLTVVLVELLG------------VIALADELKLYPGAAEALKALKERGIkva 118

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 494884502  162 ---ADIRAHLSDVhAEVIDHRRWAAPWHVIEIIKHGMNKAVGLKKISDYYQVPRERIIAFGDEDNDLEMLRFAG 232
Cdd:pfam00702 119 iltGDNPEAAEAL-LRLLGLDDYFDVVISGDDVGVGKPKPEIYLAALERLGVKPEEVLMVGDGVNDIPAAKAAG 191
P-type_ATPase cd02609
uncharacterized subfamily of P-type ATPase transporter, similar to uncharacterized ...
 219-251 2.72e-03

uncharacterized subfamily of P-type ATPase transporter, similar to uncharacterized Streptococcus pneumoniae exported protein 7, Exp7; This subfamily contains P-type ATPase transporters of unknown function, similar to Streptococcus pneumoniae Exp7. The P-type ATPases, are a large family of integral membrane transporters that are of critical importance in all kingdoms of life. They generate and maintain (electro-) chemical gradients across cellular membranes, by translocating cations, heavy metals and lipids. They are distinguished from other main classes of transport ATPases (F- , V- , and ABC- type) by the formation of a phosphorylated (P-) intermediate state in the catalytic cycle. A general characteristic of P-type ATPases is a bundle of transmembrane helices which make up the transport path, and three domains on the cytoplasmic side of the membrane. Members include pumps that transport various light metal ions, such as H(+), Na(+), K(+), Ca(2+), and Mg(2+), pumps that transport indispensable trace elements, such as Zn(2+) and Cu(2+), pumps that remove toxic heavy metal ions, such as Cd(2+), and pumps such as aminophospholipid translocases which transport phosphatidylserine and phosphatidylethanolamine.


Pssm-ID: 319795 [Multi-domain]  Cd Length: 661  Bit Score: 38.80  E-value: 2.72e-03
                         10        20        30
                 ....*....|....*....|....*....|...
gi 494884502 219 GDEDNDLEMLRFAGCGVAMGNGTDEVKQAADRV 251
Cdd:cd02609  527 GDGVNDVLALKEADCSIAMASGSDATRQVAQVV 559
HAD_like cd01427
Haloacid dehalogenase-like hydrolases; The haloacid dehalogenase-like (HAD) superfamily ...
 196-237 4.65e-03

Haloacid dehalogenase-like hydrolases; The haloacid dehalogenase-like (HAD) superfamily includes L-2-haloacid dehalogenase, epoxide hydrolase, phosphoserine phosphatase, phosphomannomutase, phosphoglycolate phosphatase, P-type ATPase, and many others. This superfamily includes a variety of enzymes that catalyze the cleavage of substrate C-Cl, P-C, and P-OP bonds via nucleophilic substitution pathways. All of which use a nucleophilic aspartate in their phosphoryl transfer reaction. They catalyze nucleophilic substitution reactions at phosphorus or carbon centers, using a conserved Asp carboxylate in covalent catalysis. All 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. Members of this superfamily are sometimes referred to as belonging to the DDDD superfamily of phosphohydrolases.


Pssm-ID: 319763 [Multi-domain]  Cd Length: 106  Bit Score: 35.83  E-value: 4.65e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 494884502 196 NKAVGLKKISDYYQVPRERIIAFGDEDNDLEMLRFAGC-GVAM 237
Cdd:cd01427   64 PKPKPLLLLLLKLGVDPEEVLFVGDSENDIEAARAAGGrTVAV 106
P-type_ATPase_SPCA cd02085
golgi-associated secretory pathway Ca(2+) transport ATPases, similar to human ATPase secretory ...
 139-251 4.77e-03

golgi-associated secretory pathway Ca(2+) transport ATPases, similar to human ATPase secretory pathway Ca(2+) transporting 1/hSPCA1 and Saccharomyces cerevisiae Ca(2+)/Mn(2+)-transporting P-type ATPase, Pmr1p; SPCAs are Ca(2+) pumps important for the golgi-associated secretion pathway, in addition some function as Mn(2+) pumps in Mn(2+) detoxification. Saccharomyces cerevisiae Pmr1p is a high affinity Ca(2+)/Mn(2+) ATPase which transports Ca(2+) and Mn(2+) from the cytoplasm into the Golgi. Pmr1p also contributes to Cd(2+) detoxification. This subfamily includes human SPCA1 and SPCA2, encoded by the ATP2C1 and ATP2C2 genes; autosomal dominant Hailey-Hailey disease is caused by mutations in the human ATP2C1 gene. It also includes Strongylocentrotus purpuratus testis secretory pathway calcium transporting ATPase SPCA which plays an important role in fertilization. This subfamily belongs to the P-type ATPases, a large family of integral membrane transporters that are of critical importance in all kingdoms of life. They generate and maintain (electro-) chemical gradients across cellular membranes, by translocating cations, heavy metals and lipids, and are distinguished from other main classes of transport ATPases (F- , V- , and ABC- type) by the formation of a phosphorylated (P-) intermediate state in the catalytic cycle.


Pssm-ID: 319779 [Multi-domain]  Cd Length: 804  Bit Score: 38.15  E-value: 4.77e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494884502 139 GDLRETVQEDVTSVLIHAKE------EDVADIRAH-LSDVHAEVIDHRRwAAPWHVIEIIKhgmnkavGLKKISDyyqvp 211
Cdd:cd02085  479 GDAQETAIAIGSSLGLYSPSlqalsgEEVDQMSDSqLASVVRKVTVFYR-ASPRHKLKIVK-------ALQKSGA----- 545

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 494884502 212 rerIIAF-GDEDNDLEMLRFAGCGVAMG-NGTDEVKQAADRV 251
Cdd:cd02085  546 ---VVAMtGDGVNDAVALKSADIGIAMGrTGTDVCKEAADMI 584
P-type_ATPase_SERCA cd02083
sarco/endoplasmic reticulum Ca(2+)-ATPase (SERCA), similar to mammalian ATP2A1-3/SERCA1-3; ...
 203-251 7.48e-03

sarco/endoplasmic reticulum Ca(2+)-ATPase (SERCA), similar to mammalian ATP2A1-3/SERCA1-3; SERCA is a transmembrane (Ca2+)-ATPase and a major regulator of Ca(2+) homeostasis and contractility in cardiac and skeletal muscle. It re-sequesters cytoplasmic Ca(2+) to the sarco/endoplasmic reticulum store, thereby also terminating Ca(2+)-induced signaling such as in muscle contraction. Three genes (ATP2A1-3/SERCA1-3) encode SERCA pumps in mammals, further isoforms exist due to alternative splicing of transcripts. The activity of SERCA is regulated by two small membrane proteins called phospholamban and sarcolipin. This subfamily belongs to the P-type ATPases, a large family of integral membrane transporters that are of critical importance in all kingdoms of life. They generate and maintain (electro-) chemical gradients across cellular membranes, by translocating cations, heavy metals and lipids, and are distinguished from other main classes of transport ATPases (F- , V- , and ABC- type) by the formation of a phosphorylated (P-) intermediate state in the catalytic cycle.


Pssm-ID: 319778 [Multi-domain]  Cd Length: 979  Bit Score: 37.66  E-value: 7.48e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 494884502 203 KISDYYQVPRErIIAF-GDEDNDLEMLRFAGCGVAMGNGTDEVKQAADRV 251
Cdd:cd02083  676 KIVELLQSQGE-ITAMtGDGVNDAPALKKAEIGIAMGSGTAVAKSASDMV 724
PTZ00174 PTZ00174
phosphomannomutase; Provisional
 1-46 7.61e-03

phosphomannomutase; Provisional


Pssm-ID: 240305  Cd Length: 247  Bit Score: 36.85  E-value: 7.61e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 494884502   1 METKPYLIALDLDGTLLKDDKTISPETARTIQTLKEAGHHVCISTG 46
Cdd:PTZ00174   1 MEMKKTILLFDVDGTLTKPRNPITQEMKDTLAKLKSKGFKIGVVGG 46
 
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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