NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|123593429|sp|Q3J7M5|]
View 

RecName: Full=Putative HAD-like hydrolase Noc_2718

Protein Classification

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
HAD_SPP cd02605
sucrose-phosphatase, similar to Synechocystis sp PCC 6803 SPP; Sucrose-phosphatase (SPP; EC 3. ...
 6-269 1.98e-92

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: 276.92  E-value: 1.98e-92
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123593429   6 LLCSDLDRTLLPNGHQaesPQARLRLQRLAQR----PGIILAYVSGRHKALIQSAIREYDLPLPDFAIGDVGTTIYQITD 81
Cdd:cd02605    1 LLVSDLDETLVGHDTN---LQALERLQDLLEQltadNDVILVYATGRSPESVLELIKEVMLPKPDFIISDVGTEIYYGES 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123593429  82 NQWHPWEDWSKEISQDWQGinqaglaKLFADITPLRL----QEPEKQNRYKLSYYAPPElDWENLIPQLAQRLQAQGIQA 157
Cdd:cd02605   78 GYLEPDTYWNEVLSEGWER-------FLFEAIADLFKqlkpQSELEQNPHKISFYLDPQ-NDAAVIEQLEEMLLKAGLTV 149

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123593429 158 SFIWSVDEtaqIGLLDILPKRANKLHAIRFLMERQHFDKSHTVFAGDSGNDLEVLASGLQAILVRNAQEEVRQEALRRLP 237
Cdd:cd02605  150 RIIYSSGL---AYDLDILPLGAGKGEALRYLQEKWNFPPERTLVCGDSGNDIALLSTGTRGVIVGNAQPELLKWADRVTR 226

                        250       260       270
                 ....*....|....*....|....*....|..
gi 123593429 238 PEHSQqlylarggfmglnGYYSAGVLEGLAHF 269
Cdd:cd02605  227 SRLAK-------------GPYAGGILEGLAHF 245
YcgL COG3100
Uncharacterized conserved protein YcgL, UPF0745 family [Function unknown];
293-363 1.72e-31

Uncharacterized conserved protein YcgL, UPF0745 family [Function unknown];


:

Pssm-ID: 442334  Cd Length: 85  Bit Score: 114.12  E-value: 1.72e-31
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 123593429 293 CAIYRSCKRNDSYLYVESQDDFSRVPGKLLEMLGKLEFVMRLELRPEISLAQANTREVMQMLREKGYFLQL 363
Cdd:COG3100    3 CAIYKSPKKDETYLYVEKRDDFSRVPEALLQMFGKPEFVMDLLLTPERKLARADAEKVLAALEEQGFYLQM 73
 
Name Accession Description Interval E-value
HAD_SPP cd02605
sucrose-phosphatase, similar to Synechocystis sp PCC 6803 SPP; Sucrose-phosphatase (SPP; EC 3. ...
 6-269 1.98e-92

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: 276.92  E-value: 1.98e-92
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123593429   6 LLCSDLDRTLLPNGHQaesPQARLRLQRLAQR----PGIILAYVSGRHKALIQSAIREYDLPLPDFAIGDVGTTIYQITD 81
Cdd:cd02605    1 LLVSDLDETLVGHDTN---LQALERLQDLLEQltadNDVILVYATGRSPESVLELIKEVMLPKPDFIISDVGTEIYYGES 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123593429  82 NQWHPWEDWSKEISQDWQGinqaglaKLFADITPLRL----QEPEKQNRYKLSYYAPPElDWENLIPQLAQRLQAQGIQA 157
Cdd:cd02605   78 GYLEPDTYWNEVLSEGWER-------FLFEAIADLFKqlkpQSELEQNPHKISFYLDPQ-NDAAVIEQLEEMLLKAGLTV 149

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123593429 158 SFIWSVDEtaqIGLLDILPKRANKLHAIRFLMERQHFDKSHTVFAGDSGNDLEVLASGLQAILVRNAQEEVRQEALRRLP 237
Cdd:cd02605  150 RIIYSSGL---AYDLDILPLGAGKGEALRYLQEKWNFPPERTLVCGDSGNDIALLSTGTRGVIVGNAQPELLKWADRVTR 226

                        250       260       270
                 ....*....|....*....|....*....|..
gi 123593429 238 PEHSQqlylarggfmglnGYYSAGVLEGLAHF 269
Cdd:cd02605  227 SRLAK-------------GPYAGGILEGLAHF 245
S6PP pfam05116
Sucrose-6F-phosphate phosphohydrolase; This family consists of Sucrose-6F-phosphate ...
 6-269 9.09e-56

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: 182.85  E-value: 9.09e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123593429    6 LLCSDLDRTLLPnghqaESPQARLRLQRL--AQRPGIILAYVSGRHKALIQSAIREYDLPLPDFAIGDVGTTIYQITDNQ 83
Cdd:pfam05116   4 LLVSDLDNTLVD-----GDNEALARLNQLleAYRPDVGLVFATGRSLDSAKELLKEKPLPTPDYLITSVGTEIYYGPSLV 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123593429   84 whPWEDWSKEISQDWQGinQAgLAKLFADITPLRLQEPEKQNRYKLSYYAPPElDWENLIPQLAQRLQAQGIQASFIWSV 163
Cdd:pfam05116  79 --PDQSWQEHLDYHWDR--QA-VVEALAKFPGLTLQPEEEQRPHKVSYFLDPE-AAAAVLAELEQLLRKRGLDVKVIYSS 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123593429  164 DetaqiGLLDILPKRANKLHAIRFLMERQHFDKSHTVFAGDSGNDLEVLASGLQAILVRNAQEEVRQ---EALRRLPPeh 240
Cdd:pfam05116 153 G-----RDLDILPLRASKGEALRYLALKLGLPLENTLVCGDSGNDEELFIGGTRGVVVGNAQPELLQwylENARDNPR-- 225

                         250       260
                  ....*....|....*....|....*....
gi 123593429  241 sqqLYLArggfmglNGYYSAGVLEGLAHF 269
Cdd:pfam05116 226 ---IYFA-------SGRCAGGILEGIRHF 244
Cof COG0561
Hydroxymethylpyrimidine pyrophosphatase and other HAD family phosphatases [Coenzyme transport ...
 6-269 3.26e-32

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: 119.47  E-value: 3.26e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123593429   6 LLCSDLDRTLLPNGHQAeSPQARLRLQRLAQRpGIILAYVSGRHKALIQSAIREydLPLPDFAIGDVGTTIYQITDNQWH 85
Cdd:COG0561    4 LIALDLDGTLLNDDGEI-SPRTKEALRRLREK-GIKVVIATGRPLRSALPLLEE--LGLDDPLITSNGALIYDPDGEVLY 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123593429  86 pwedwSKEISQDwqginqaglaklfaditplrlqepekqnryklsyyappeldwenLIPQLAQRLQAQGIQASFIWSvde 165
Cdd:COG0561   80 -----ERPLDPE--------------------------------------------DVREILELLREHGLHLQVVVR--- 107

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123593429 166 tAQIGLLDILPKRANKLHAIRFLMERQHFDKSHTVFAGDSGNDLEVLASGLQAILVRNAQEEVRQEALRRLPPEHsqqly 245
Cdd:COG0561  108 -SGPGFLEILPKGVSKGSALKKLAERLGIPPEEVIAFGDSGNDLEMLEAAGLGVAMGNAPPEVKAAADYVTGSND----- 181

                        250       260
                 ....*....|....*....|....
gi 123593429 246 larggfmglngyySAGVLEGLAHF 269
Cdd:COG0561  182 -------------EDGVAEALEKL 192
YcgL COG3100
Uncharacterized conserved protein YcgL, UPF0745 family [Function unknown];
293-363 1.72e-31

Uncharacterized conserved protein YcgL, UPF0745 family [Function unknown];


Pssm-ID: 442334  Cd Length: 85  Bit Score: 114.12  E-value: 1.72e-31
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 123593429 293 CAIYRSCKRNDSYLYVESQDDFSRVPGKLLEMLGKLEFVMRLELRPEISLAQANTREVMQMLREKGYFLQL 363
Cdd:COG3100    3 CAIYKSPKKDETYLYVEKRDDFSRVPEALLQMFGKPEFVMDLLLTPERKLARADAEKVLAALEEQGFYLQM 73
SPP_plant-cyano TIGR01485
sucrose-6F-phosphate phosphohydrolase; This model describes the sucrose phosphate ...
 4-269 2.45e-31

sucrose-6F-phosphate phosphohydrolase; This model describes the sucrose phosphate phosphohydrolase from plants and cyanobacteria (SPP). SPP is a member of the Class IIB subfamily (TIGR01484) of the Haloacid Dehalogenase (HAD) superfamily of aspartate-nucleophile hydrolases. SPP catalyzes the final step in the biosynthesis of sucrose, a critically important molecule for plants. Sucrose phosphate synthase (SPS), the prior step in the biosynthesis of sucrose, contains a domain which exhibits considerable similarity to SPP albeit without conservation of the catalytic residues. The catalytic machinery of the synthase resides in another domain. It seems likely that the phosphatase-like domain is involved in substrate binding, possibly binding both substrates in a "product-like" orientation prior to ligation by the synthase catalytic domain.


Pssm-ID: 130549  Cd Length: 249  Bit Score: 119.15  E-value: 2.45e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123593429    4 KILLCSDLDRTLLPngHQAESPQARLRLQRLAQR---PGIILAYVSGRHKALIQSAIREYDLPLPDFAIGDVGTTIYQit 80
Cdd:TIGR01485   1 RLLLVSDLDNTLVD--HTDGDNQALLRLNALLEDhrgEDSLLVYSTGRSPHSYKELQKQKPLLTPDIWVTSVGSEIYY-- 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123593429   81 DNQWHPWEDWSKEISQDWQ-GINQAGLAKLFAditpLRLQEPEKQNRYKLSYYAPPElDWENLIPQLAQRLQAQGIQASF 159
Cdd:TIGR01485  77 GGAEVPDQHWAEYLSEKWQrDIVVAITDKFEE----LKPQPDLEQRPHKVSFFLDPE-AAPEVIKQLTEMLKETGLDVKL 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123593429  160 IWSVDETaqiglLDILPKRANKLHAIRFLMERQHFDKSHTVFAGDSGNDLEVLA-SGLQAILVRNAQEEVRQealrrLPP 238
Cdd:TIGR01485 152 IYSSGKD-----LDILPQGSGKGQALQYLLQKLAMEPSQTLVCGDSGNDIELFEiGSVRGVIVSNAQEELLQ-----WYD 221

                         250       260       270
                  ....*....|....*....|....*....|..
gi 123593429  239 EHS-QQLYLArggfmglNGYYSAGVLEGLAHF 269
Cdd:TIGR01485 222 ENAkDKIYHA-------SERCAGGIIEAIAHF 246
YcgL pfam05166
YcgL domain; This family of proteins formerly called DUF709 includes the E. coli gene ycgL. ...
 293-363 7.94e-30

YcgL domain; This family of proteins formerly called DUF709 includes the E. coli gene ycgL. homologs of YcgL are found in gammaproteobacteria. The structure of this protein shows a novel alpha/beta/alpha sandwich structure.


Pssm-ID: 428344  Cd Length: 73  Bit Score: 109.51  E-value: 7.94e-30
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 123593429  293 CAIYRSCKRNDSYLYVESQDDFSRVPGKLLEMLGKLEFVMRLELRPEISLAQANTREVMQMLREKGYFLQL 363
Cdd:pfam05166   1 CAIYKSSKKDETYLYVEKRDDFSRVPEALLAMFGKPQFVMLLNLTPERKLARADIEKVLAALKEQGFYLQL 71
PLN02382 PLN02382
probable sucrose-phosphatase
 4-230 7.88e-21

probable sucrose-phosphatase


Pssm-ID: 178008 [Multi-domain]  Cd Length: 413  Bit Score: 93.13  E-value: 7.88e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123593429   4 KILLCSDLDRTLLpnGHQAESPQARLRLQRLAQ---RPGIILAYVSGRHKALIQSAIREYDLPLPDFAIGDVGTTI-Yqi 79
Cdd:PLN02382   9 RLMIVSDLDHTMV--DHHDPENLSLLRFNALWEaeyRHDSLLVFSTGRSPTLYKELRKEKPLLTPDITIMSVGTEIaY-- 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123593429  80 tDNQWHPWEDWSKEISQDWqgiNQAGLAKLFADITPLRLQEPEKQNRYKLSYYAPPElDWENLIPQLAQRLQAQGIQASF 159
Cdd:PLN02382  85 -GESMVPDHGWVEYLNKKW---DREIVVEETSKFPELKLQPETEQRPHKVSFYVDKK-KAQEVIKELSERLEKRGLDVKI 159

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 123593429 160 IWS--VDetaqiglLDILPKRANKLHAIRFLMERqhFD-----KSHTVFAGDSGNDLEVLA-SGLQAILVRNAQEEVRQ 230
Cdd:PLN02382 160 IYSggID-------LDVLPQGAGKGQALAYLLKK--LKaegkaPVNTLVCGDSGNDAELFSvPDVYGVMVSNAQEELLQ 229
 
Name Accession Description Interval E-value
HAD_SPP cd02605
sucrose-phosphatase, similar to Synechocystis sp PCC 6803 SPP; Sucrose-phosphatase (SPP; EC 3. ...
 6-269 1.98e-92

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: 276.92  E-value: 1.98e-92
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123593429   6 LLCSDLDRTLLPNGHQaesPQARLRLQRLAQR----PGIILAYVSGRHKALIQSAIREYDLPLPDFAIGDVGTTIYQITD 81
Cdd:cd02605    1 LLVSDLDETLVGHDTN---LQALERLQDLLEQltadNDVILVYATGRSPESVLELIKEVMLPKPDFIISDVGTEIYYGES 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123593429  82 NQWHPWEDWSKEISQDWQGinqaglaKLFADITPLRL----QEPEKQNRYKLSYYAPPElDWENLIPQLAQRLQAQGIQA 157
Cdd:cd02605   78 GYLEPDTYWNEVLSEGWER-------FLFEAIADLFKqlkpQSELEQNPHKISFYLDPQ-NDAAVIEQLEEMLLKAGLTV 149

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123593429 158 SFIWSVDEtaqIGLLDILPKRANKLHAIRFLMERQHFDKSHTVFAGDSGNDLEVLASGLQAILVRNAQEEVRQEALRRLP 237
Cdd:cd02605  150 RIIYSSGL---AYDLDILPLGAGKGEALRYLQEKWNFPPERTLVCGDSGNDIALLSTGTRGVIVGNAQPELLKWADRVTR 226

                        250       260       270
                 ....*....|....*....|....*....|..
gi 123593429 238 PEHSQqlylarggfmglnGYYSAGVLEGLAHF 269
Cdd:cd02605  227 SRLAK-------------GPYAGGILEGLAHF 245
S6PP pfam05116
Sucrose-6F-phosphate phosphohydrolase; This family consists of Sucrose-6F-phosphate ...
 6-269 9.09e-56

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: 182.85  E-value: 9.09e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123593429    6 LLCSDLDRTLLPnghqaESPQARLRLQRL--AQRPGIILAYVSGRHKALIQSAIREYDLPLPDFAIGDVGTTIYQITDNQ 83
Cdd:pfam05116   4 LLVSDLDNTLVD-----GDNEALARLNQLleAYRPDVGLVFATGRSLDSAKELLKEKPLPTPDYLITSVGTEIYYGPSLV 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123593429   84 whPWEDWSKEISQDWQGinQAgLAKLFADITPLRLQEPEKQNRYKLSYYAPPElDWENLIPQLAQRLQAQGIQASFIWSV 163
Cdd:pfam05116  79 --PDQSWQEHLDYHWDR--QA-VVEALAKFPGLTLQPEEEQRPHKVSYFLDPE-AAAAVLAELEQLLRKRGLDVKVIYSS 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123593429  164 DetaqiGLLDILPKRANKLHAIRFLMERQHFDKSHTVFAGDSGNDLEVLASGLQAILVRNAQEEVRQ---EALRRLPPeh 240
Cdd:pfam05116 153 G-----RDLDILPLRASKGEALRYLALKLGLPLENTLVCGDSGNDEELFIGGTRGVVVGNAQPELLQwylENARDNPR-- 225

                         250       260
                  ....*....|....*....|....*....
gi 123593429  241 sqqLYLArggfmglNGYYSAGVLEGLAHF 269
Cdd:pfam05116 226 ---IYFA-------SGRCAGGILEGIRHF 244
Cof COG0561
Hydroxymethylpyrimidine pyrophosphatase and other HAD family phosphatases [Coenzyme transport ...
 6-269 3.26e-32

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: 119.47  E-value: 3.26e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123593429   6 LLCSDLDRTLLPNGHQAeSPQARLRLQRLAQRpGIILAYVSGRHKALIQSAIREydLPLPDFAIGDVGTTIYQITDNQWH 85
Cdd:COG0561    4 LIALDLDGTLLNDDGEI-SPRTKEALRRLREK-GIKVVIATGRPLRSALPLLEE--LGLDDPLITSNGALIYDPDGEVLY 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123593429  86 pwedwSKEISQDwqginqaglaklfaditplrlqepekqnryklsyyappeldwenLIPQLAQRLQAQGIQASFIWSvde 165
Cdd:COG0561   80 -----ERPLDPE--------------------------------------------DVREILELLREHGLHLQVVVR--- 107

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123593429 166 tAQIGLLDILPKRANKLHAIRFLMERQHFDKSHTVFAGDSGNDLEVLASGLQAILVRNAQEEVRQEALRRLPPEHsqqly 245
Cdd:COG0561  108 -SGPGFLEILPKGVSKGSALKKLAERLGIPPEEVIAFGDSGNDLEMLEAAGLGVAMGNAPPEVKAAADYVTGSND----- 181

                        250       260
                 ....*....|....*....|....
gi 123593429 246 larggfmglngyySAGVLEGLAHF 269
Cdd:COG0561  182 -------------EDGVAEALEKL 192
YcgL COG3100
Uncharacterized conserved protein YcgL, UPF0745 family [Function unknown];
293-363 1.72e-31

Uncharacterized conserved protein YcgL, UPF0745 family [Function unknown];


Pssm-ID: 442334  Cd Length: 85  Bit Score: 114.12  E-value: 1.72e-31
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 123593429 293 CAIYRSCKRNDSYLYVESQDDFSRVPGKLLEMLGKLEFVMRLELRPEISLAQANTREVMQMLREKGYFLQL 363
Cdd:COG3100    3 CAIYKSPKKDETYLYVEKRDDFSRVPEALLQMFGKPEFVMDLLLTPERKLARADAEKVLAALEEQGFYLQM 73
SPP_plant-cyano TIGR01485
sucrose-6F-phosphate phosphohydrolase; This model describes the sucrose phosphate ...
 4-269 2.45e-31

sucrose-6F-phosphate phosphohydrolase; This model describes the sucrose phosphate phosphohydrolase from plants and cyanobacteria (SPP). SPP is a member of the Class IIB subfamily (TIGR01484) of the Haloacid Dehalogenase (HAD) superfamily of aspartate-nucleophile hydrolases. SPP catalyzes the final step in the biosynthesis of sucrose, a critically important molecule for plants. Sucrose phosphate synthase (SPS), the prior step in the biosynthesis of sucrose, contains a domain which exhibits considerable similarity to SPP albeit without conservation of the catalytic residues. The catalytic machinery of the synthase resides in another domain. It seems likely that the phosphatase-like domain is involved in substrate binding, possibly binding both substrates in a "product-like" orientation prior to ligation by the synthase catalytic domain.


Pssm-ID: 130549  Cd Length: 249  Bit Score: 119.15  E-value: 2.45e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123593429    4 KILLCSDLDRTLLPngHQAESPQARLRLQRLAQR---PGIILAYVSGRHKALIQSAIREYDLPLPDFAIGDVGTTIYQit 80
Cdd:TIGR01485   1 RLLLVSDLDNTLVD--HTDGDNQALLRLNALLEDhrgEDSLLVYSTGRSPHSYKELQKQKPLLTPDIWVTSVGSEIYY-- 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123593429   81 DNQWHPWEDWSKEISQDWQ-GINQAGLAKLFAditpLRLQEPEKQNRYKLSYYAPPElDWENLIPQLAQRLQAQGIQASF 159
Cdd:TIGR01485  77 GGAEVPDQHWAEYLSEKWQrDIVVAITDKFEE----LKPQPDLEQRPHKVSFFLDPE-AAPEVIKQLTEMLKETGLDVKL 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123593429  160 IWSVDETaqiglLDILPKRANKLHAIRFLMERQHFDKSHTVFAGDSGNDLEVLA-SGLQAILVRNAQEEVRQealrrLPP 238
Cdd:TIGR01485 152 IYSSGKD-----LDILPQGSGKGQALQYLLQKLAMEPSQTLVCGDSGNDIELFEiGSVRGVIVSNAQEELLQ-----WYD 221

                         250       260       270
                  ....*....|....*....|....*....|..
gi 123593429  239 EHS-QQLYLArggfmglNGYYSAGVLEGLAHF 269
Cdd:TIGR01485 222 ENAkDKIYHA-------SERCAGGIIEAIAHF 246
sucr_syn_bact_C TIGR02471
sucrose-phosphate synthase, sucrose phosphatase-like domain, bacterial; Sucrose phosphate ...
 6-269 8.84e-31

sucrose-phosphate synthase, sucrose phosphatase-like domain, bacterial; Sucrose phosphate synthase (SPS) and sucrose phosphate phosphatase (SPP) are the last two enzymes of sucrose biosynthesis. In cyanobacteria and plants, the C-terminal region of most or all versions of SPS has a domain homologous to the known SPP. This domain may serve a binding or regulatory rather than catalytic function. Sequences in this family are bacterial C-terminal regions found in all but two of the putative bacterial sucrose phosphate synthases described by TIGR02472.


Pssm-ID: 131524  Cd Length: 236  Bit Score: 117.17  E-value: 8.84e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123593429    6 LLCSDLDRTLLPNGHQAESPQARLRLQRLAQRPGIilayVSGRHKALIQSAIREYDLPLPDFAIGDVGTTIYQITDNQwh 85
Cdd:TIGR02471   1 LIITDLDNTLLGDDEGLASFVELLRGSGDAVGFGI----ATGRSVESAKSRYAKLNLPSPDVLIARVGTEIYYGPELQ-- 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123593429   86 PWEDWSKEISQDWQginQAGLAKLFADITPLRLQEPEKQNRYKLSYYAPPELdwENLIPQLAQRLQAQGIQASFIWSVDE 165
Cdd:TIGR02471  75 PDRFWQKHIDHDWR---RQAVVEALADIPGLTLQDDQEQGPFKISYLLDPEG--EPILPQIRQRLRQQSQAAKVILSCGW 149

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123593429  166 taqigLLDILPKRANKLHAIRFLMERQHFDKSHTVFAGDSGNDLEVLASGLQAILVRNAQEEVrqEALRRLPpehsqQLY 245
Cdd:TIGR02471 150 -----FLDVLPLRASKGLALRYLSYRWGLPLEQILVAGDSGNDEEMLRGLTLGVVVGNHDPEL--EGLRHQQ-----RIY 217

                         250       260
                  ....*....|....*....|....
gi 123593429  246 LArggfmglNGYYSAGVLEGLAHF 269
Cdd:TIGR02471 218 FA-------NNPHAFGILEGINHY 234
YcgL pfam05166
YcgL domain; This family of proteins formerly called DUF709 includes the E. coli gene ycgL. ...
 293-363 7.94e-30

YcgL domain; This family of proteins formerly called DUF709 includes the E. coli gene ycgL. homologs of YcgL are found in gammaproteobacteria. The structure of this protein shows a novel alpha/beta/alpha sandwich structure.


Pssm-ID: 428344  Cd Length: 73  Bit Score: 109.51  E-value: 7.94e-30
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 123593429  293 CAIYRSCKRNDSYLYVESQDDFSRVPGKLLEMLGKLEFVMRLELRPEISLAQANTREVMQMLREKGYFLQL 363
Cdd:pfam05166   1 CAIYKSSKKDETYLYVEKRDDFSRVPEALLAMFGKPQFVMLLNLTPERKLARADIEKVLAALKEQGFYLQL 71
HAD-SF-IIB TIGR01484
HAD-superfamily hydrolase, subfamily IIB; This subfamily falls within the Haloacid ...
 6-221 1.63e-22

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: 93.98  E-value: 1.63e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123593429    6 LLCSDLDRTLLPNGHQAESPQARLRLQRLAQRpGIILAYVSGRHKALIQSAIREYDLPLPdfAIGDVGTTIYQITDNQWH 85
Cdd:TIGR01484   1 LLFFDLDGTLLDPNAHELSPETIEALERLREA-GVKVVIVTGRSLAEIKELLKQLNLPLP--LIAENGALIFYPGEILYI 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123593429   86 PWEDWSKEISQDWQGINQAgLAKLFADITPLRLQEpekQNRYKLSYYAPPELDWENLIPQLAQRLQaqgiqasFIWSVDE 165
Cdd:TIGR01484  78 EPSDVFEEILGIKFEEIGA-ELKSLSEHYVGTFIE---DKAIAVAIHYVGAELGQELDSKMRERLE-------KIGRNDL 146

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 123593429  166 TAQI-----GLLDILPKRANKLHAIRFLMERQHFDKSHTVFAGDSGNDLEVLASGLQAILV 221
Cdd:TIGR01484 147 ELEAiysgkTDLEVLPAGVNKGSALQALLQELNGKKDEILAFGDSGNDEEMFEVAGLAVAV 207
PLN02382 PLN02382
probable sucrose-phosphatase
 4-230 7.88e-21

probable sucrose-phosphatase


Pssm-ID: 178008 [Multi-domain]  Cd Length: 413  Bit Score: 93.13  E-value: 7.88e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123593429   4 KILLCSDLDRTLLpnGHQAESPQARLRLQRLAQ---RPGIILAYVSGRHKALIQSAIREYDLPLPDFAIGDVGTTI-Yqi 79
Cdd:PLN02382   9 RLMIVSDLDHTMV--DHHDPENLSLLRFNALWEaeyRHDSLLVFSTGRSPTLYKELRKEKPLLTPDITIMSVGTEIaY-- 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123593429  80 tDNQWHPWEDWSKEISQDWqgiNQAGLAKLFADITPLRLQEPEKQNRYKLSYYAPPElDWENLIPQLAQRLQAQGIQASF 159
Cdd:PLN02382  85 -GESMVPDHGWVEYLNKKW---DREIVVEETSKFPELKLQPETEQRPHKVSFYVDKK-KAQEVIKELSERLEKRGLDVKI 159

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 123593429 160 IWS--VDetaqiglLDILPKRANKLHAIRFLMERqhFD-----KSHTVFAGDSGNDLEVLA-SGLQAILVRNAQEEVRQ 230
Cdd:PLN02382 160 IYSggID-------LDVLPQGAGKGQALAYLLKK--LKaegkaPVNTLVCGDSGNDAELFSvPDVYGVMVSNAQEELLQ 229
SPP-subfamily TIGR01482
sucrose-phosphate phosphatase subfamily; This model includes both the members of the SPP ...
 7-241 1.61e-18

sucrose-phosphate phosphatase subfamily; This model includes both the members of the SPP equivalog model (TIGR01485), encompassing plants and cyanobacteria, as well as those archaeal sequences which are the closest relatives (TIGR01487). It remains to be shown whether these archaeal sequences catalyze the same reaction as SPP.


Pssm-ID: 273650 [Multi-domain]  Cd Length: 225  Bit Score: 83.28  E-value: 1.61e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123593429    7 LCSDLDRTLLpNGHQAESPQArLRLQRLAQRPGIILAYVSGRHKALIQSAIREydLPLPDFAIGDVGTTIYQITDNQWHp 86
Cdd:TIGR01482   1 IASDIDGTLT-DPNRAINESA-LEAIRKAESKGIPVVLVTGNSVQFARALAKL--IGTPDPVIAENGGEISYNEGLDDI- 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123593429   87 WEDWSKEisqDWQGINQAGLAKLFADitpLRLQEPEKQNRYKLSYYAPPELDWEnLIPQLAQRLQAqgIQASFIWsvdet 166
Cdd:TIGR01482  76 FLAYLEE---EWFLDIVIAKTFPFSR---LKVQYPRRASLVKMRYGIDVDTVRE-IIKELGLNLVA--VDSGFDI----- 141

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 123593429  167 aqigllDILPKRANKLHAIRFLMERQHFDKSHTVFAGDSGNDLEVLASGLQAILVRNAQEEVRQEALRRLPPEHS 241
Cdd:TIGR01482 142 ------HILPQGVNKGVAVKKLKEKLGIKPGETLVCGDSENDIDLFEVPGFGVAVANAQPELKEWADYVTESPYG 210
Hydrolase_3 pfam08282
haloacid dehalogenase-like hydrolase; This family contains haloacid dehalogenase-like ...
 7-232 2.52e-16

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


Pssm-ID: 429897 [Multi-domain]  Cd Length: 255  Bit Score: 77.66  E-value: 2.52e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123593429    7 LCSDLDRTLLPNGHQAeSPQARLRLQRLAQRpGIILAYVSGRHKALIQSAIREydLPLPDFAIGDVGTTIYQITDN--QW 84
Cdd:pfam08282   1 IASDLDGTLLNSDKKI-SEKTKEAIKKLKEK-GIKFVIATGRPYRAILPVIKE--LGLDDPVICYNGALIYDENGKilYS 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123593429   85 HPWE--------DWSKEISQDWQ--------GINQAGLAK--------LFADITPLRLQEPEKQNRYKLSYYAPPElDWE 140
Cdd:pfam08282  77 NPISkeavkeiiEYLKENNLEILlytddgvyILNDNELEKilkelnytKSFVPEIDDFELLEDEDINKILILLDEE-DLD 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123593429  141 NLIPQLAQRLqaqGIQASFIWSvdetaQIGLLDILPKRANKLHAIRFLMERQHFDKSHTVFAGDSGNDLEVL-ASGLqAI 219
Cdd:pfam08282 156 ELEKELKELF---GSLITITSS-----GPGYLEIMPKGVSKGTALKALAKHLNISLEEVIAFGDGENDIEMLeAAGL-GV 226

                         250
                  ....*....|...
gi 123593429  220 LVRNAQEEVRQEA 232
Cdd:pfam08282 227 AMGNASPEVKAAA 239
HAD_Pase cd07516
phosphatase, similar to Escherichia coli Cof and Thermotoga maritima TM0651; belongs to the ...
 6-232 2.75e-12

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: 66.08  E-value: 2.75e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123593429   6 LLCSDLDRTLLPNGHQAeSPQARLRLQRLAQRpGIILAYVSGRHKALIQSAIREydLPLPDFAIGDVGTTIYQITDNQ-- 83
Cdd:cd07516    1 LIALDLDGTLLNSDKEI-SPRTKEAIKKAKEK-GIKVVIATGRPLRGAQPYLEE--LGLDSPLITFNGALVYDPTGKEil 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123593429  84 -WHPWEDWSKEISQdwQGINQAGLAKLFAD-------ITPLRLQEPEKQNRYKLSYYAPPELDW---------ENLIPQL 146
Cdd:cd07516   77 eRLISKEDVKELEE--FLRKLGIGINIYTNddwadtiYEENEDDEIIKPAEILDDLLLPPDEDItkilfvgedEELDELI 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123593429 147 AQRLQAQGIQASFIWSVDEtaqigLLDILPKRANKLHAIRFLMERQHFDKSHTVFAGDSGNDLEVL-ASGLqAILVRNAQ 225
Cdd:cd07516  155 AKLPEEFFDDLSVVRSAPF-----YLEIMPKGVSKGNALKKLAEYLGISLEEVIAFGDNENDLSMLeYAGL-GVAMGNAI 228


                 ....*..
gi 123593429 226 EEVRQEA 232
Cdd:cd07516  229 DEVKEAA 235
Cof-subfamily TIGR00099
Cof subfamily of IIB subfamily of haloacid dehalogenase superfamily; This subfamily of ...
 6-232 1.11e-11

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: 64.21  E-value: 1.11e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123593429    6 LLCSDLDRTLLPNGHQAeSPQARLRLQRLAQRpGIILAYVSGRHKALIQSAIREYDLPLPdfAIG--------DVGTTIY 77
Cdd:TIGR00099   1 LIFIDLDGTLLNDDHTI-SPSTKEALAKLREK-GIKVVLATGRPYKEVKNILKELGLDTP--FITangaavidDQGEILY 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123593429   78 Q--ITDNQWHPWEDWSKE------ISQDWQ--------GINQAGLAKLFADITPLRLQEPEKQNRYKLSYYAPPELDWen 141
Cdd:TIGR00099  77 KkpLDLDLVEEILNFLKKhgldviLYGDDSiyaskndpEYFTIFKKFLGEPKLEVVDIQYLPDDILKILLLFLDPEDL-- 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123593429  142 liPQLAQRLQAQGI--QASFIWSVDetaqiGLLDILPKRANKLHAIRFLMERQHFDKSHTVFAGDSGNDLEVL-ASGLqA 218
Cdd:TIGR00099 155 --DLLIEALNKLELeeNVSVVSSGP-----YSIEITAKGVSKGSALQSLAEALGISLEDVIAFGDGMNDIEMLeAAGY-G 226

                         250
                  ....*....|....
gi 123593429  219 ILVRNAQEEVRQEA 232
Cdd:TIGR00099 227 VAMGNADEELKALA 240
HAD_YbiV-Like cd07518
Escherichia coli YbiV sugar phosphatase/phosphotransferase and related proteins; belongs to ...
 6-238 1.50e-08

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: 53.74  E-value: 1.50e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123593429   6 LLCSDLDRTLLPNGHQAESPQARLRLQRLAQRpGIILAYVSGRHKALIQSAIREYDLPLpDFaIGDVGTTIYqitdnqwh 85
Cdd:cd07518    2 LIATDMDGTFLNDDKTYDHERFFAILDQLLKK-GIKFVVASGRQYYQLISFFPEIKDEM-SF-VAENGAVVY-------- 70

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123593429  86 pwedwskeisqdwqginqaglaklfaditplrlqepekqnrYKLSYYAPPELDwENLIPQLAQRL--QAQGIQASFIWsv 163
Cdd:cd07518   71 -----------------------------------------FKFTLNVPDEAA-PDIIDELNQKFggILRAVTSGFGS-- 106

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 123593429 164 detaqiglLDILPKRANKLHAIRFLMERQHFDKSHTVFAGDSGNDLEVLASGLQAILVRNAQEEVRQEALRRLPP 238
Cdd:cd07518  107 --------IDIIPPGVNKATGLKQLLKHWGISPDEVMAFGDGGNDIEMLKYAGYSYAMENAPEEVKAAAKYVAPS 173
HAD_Pase cd07507
haloacid dehalogenase-like superfamily phosphatase similar to Pyrococcus horikoshii ...
 6-237 6.65e-06

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: 46.97  E-value: 6.65e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123593429   6 LLCSDLDRTLLPngHQAESPQ-ARLRLQRLAQRpGIILAYVSGRHKALIQsAIREyDLPLPDFAIGDVGTTIYqitdnqw 84
Cdd:cd07507    1 VIFTDLDGTLLD--HHTYSFDpARPALERLKER-GIPVVPCTSKTRAEVE-YLRK-ELGIEDPFIVENGGAIF------- 68

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123593429  85 hPWEDWSKEisqDWQGINQAG-----LAKLFADITPlRLQEPEKQNRYKLSYYAppELD------WENLIPQLAQRLQAQ 153
Cdd:cd07507   69 -IPRGYFKF---PGRCKSEGGyevieLGKPYREIRA-ALEKIREETGFKITGFG--DLTeeeiaeLTGLPRERAALAKER 141

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123593429 154 GIQASFIWSVDET---------AQIGLL--------DILPKRANKLHAIRFLME--RQHFDKSHTVFAGDSGNDLEVLAS 214
Cdd:cd07507  142 EYSETIILRSDEEedekvlealEERGLKitkggrfyHVLGAGADKGKAVAILAAlyRQLYEAIVTVGLGDSPNDLPMLEA 221

                        250       260
                 ....*....|....*....|...
gi 123593429 215 GLQAILVRNAQeevRQEALRRLP 237
Cdd:cd07507  222 VDIAFVVKSLN---GKYESVILP 241
HAD_TPP cd01627
trehalose-phosphate phosphatase similar to Escherichia coli trehalose-6-phosphate phosphatase ...
 6-204 1.25e-05

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: 45.74  E-value: 1.25e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123593429   6 LLCSDLDRTLLP---NGHQAE-SPQARLRLQRLAQRPGIILAYVSGRHKALIQSAIREYDLPLpdfaIGDVGttiYQITD 81
Cdd:cd01627    1 LLFLDYDGTLAPivpDPDAAVpSPELLEALKKLAADPKNAVAIVSGRDLDDLDKWLGLPGIGL----AGEHG---AEIRL 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123593429  82 NQWHPWEDWSKEISQDWQGINQAgLAKLFADITPLRLQEpEKqnryKLSYyappELDWENLIPQLAQRLQAQGI-QASFI 160
Cdd:cd01627   74 PGGGEWVTLAPKADLEWKEEVEA-IFKYFTERTPGSLVE-DK----GASL----AWHYRNADPEGARAALELALhLASDL 143

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 123593429 161 WSVDEtAQIG--LLDILPKRANKLHAIRFLMERQHFDKSHTVFAGD 204
Cdd:cd01627  144 LKALE-VVPGkkVVEVRPVGVNKGEAVERILGELPFAGDFVLCAGD 188
HAD-SF-IIB-MPGP TIGR01486
mannosyl-3-phosphoglycerate phosphatase family; This small group of proteins is a member of ...
 9-248 2.53e-05

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: 45.09  E-value: 2.53e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123593429    9 SDLDRTLLPNGHQAESPQAR--LRLQRLaqrpGIILAYVSGRHKALIQSAIREYDLPLPdfAIGDVGTTIYQITDNQWHP 86
Cdd:TIGR01486   4 TDLDGTLLDPHGYDWGPAKEvlERLQEL----GIPVIPCTSKTAAEVEYLRKELGLEDP--FIVENGGAIYGPRGWRPEP 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123593429   87 wEDWSKEisqdwqginqagLAKLFADITPlRLQEPEKQNRYKLSYYAppELD------WENLIPQLAQRLQAQGIQASFI 160
Cdd:TIGR01486  78 -EYPVIA------------LGIPYEKIRA-RLRELSEELGFKFRGLG--DLTdeeiaeLTGLSRELARLAQRREYSETIL 141

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123593429  161 WSVDETAQI-------GL-----------LDILPKRANKLHAIRFLMERQHFDKShTVFAGDSGNDLEVLASGLQAILVR 222
Cdd:TIGR01486 142 WSEERRERFtealvavGLevthggrfyhvLGAGSDKGKAVNALKAFYNQPGGAIK-VVGLGDSPNDLPLLEVVDLAVVVP 220

                         250       260
                  ....*....|....*....|....*.
gi 123593429  223 NAQEEVrqealRRLPPEHSQQLYLAR 248
Cdd:TIGR01486 221 GPNGPN-----VSLKPGDPGSFLLTP 241
HAD_SPS cd16419
sucrose-phosphate synthase; belongs to the haloalcanoic acid dehalogenase (HAD) superfamily; ...
 131-221 1.03e-04

sucrose-phosphate synthase; belongs to the haloalcanoic acid dehalogenase (HAD) superfamily; Sucrose phosphate synthase (SPS; EC 2.4.1.14) also known as UDP-glucose-fructose-phosphate glucosyltransferase, catalyzes the transfer of a hexosyl group from UDP-glucose to D-fructose 6-phosphate to form UDP and D-sucrose-6-phosphate, this is the rate limiting step of sucrose synthesis. 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 (C-Cl bond hydrolysis), azetidine hydrolase (C-N bond hydrolysis); phosphonoacetaldehyde hydrolase (C-P bond hydrolysis), phosphoserine phosphatase and phosphomannomutase (CO-P bond hydrolysis), P-type ATPases (PO-P bond hydrolysis) 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: 319856  Cd Length: 174  Bit Score: 42.61  E-value: 1.03e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123593429 131 YYAPPELD---WENLIP----QLAQRLQAQGIQASFIWSVDETAqiglLDILPKRANKLHAIRFLMERQHFDKSHT-VFA 202
Cdd:cd16419   75 YYPSPSGDddsDYELIPdpvkELRKLLRMRGLRCHLVYCRNGTR----LHVLPLLASRSQALRYLFVRWGIDLSNMvVFV 150

                         90       100
                 ....*....|....*....|
gi 123593429 203 GDSGN-DLEVLASGLQAILV 221
Cdd:cd16419  151 GESGDtDYEELLGGLHKTVI 170
HAD_HPP cd07517
phosphatase, similar to Bacteroides thetaiotaomicron VPI-5482 BT4131 hexose phosphate ...
 173-232 1.07e-04

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: 42.98  E-value: 1.07e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 123593429 173 DILPKRANKLHAIRFLMERQHFDKSHTVFAGDSGNDLEVL-ASGLqAILVRNAQEEVRQEA 232
Cdd:cd07517  134 DVIPKGGSKAKGIQKVIEHLGIKKEETMAFGDGLNDIEMLeAVGI-GIAMGNAHEELKEIA 193
SerB COG0560
Phosphoserine phosphatase [Amino acid transport and metabolism]; Phosphoserine phosphatase is ...
 178-235 1.57e-04

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: 42.52  E-value: 1.57e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 123593429 178 RANKLHAIRFLMERQHFDKSHTVFAGDSGNDLEVL-ASGLqAILVrNAQEEVRQEALRR 235
Cdd:COG0560  153 GEGKAEALRELAAELGIDLEQSYAYGDSANDLPMLeAAGL-PVAV-NPDPALREAADRE 209
PRK00192 PRK00192
mannosyl-3-phosphoglycerate phosphatase; Reviewed
 1-249 2.43e-04

mannosyl-3-phosphoglycerate phosphatase; Reviewed


Pssm-ID: 234684 [Multi-domain]  Cd Length: 273  Bit Score: 42.24  E-value: 2.43e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123593429   1 MKQKILLCSDLDRTLLpnGHQAESPQ-ARLRLQRLAQRpGIILAYVSGRHKALIQSaIREyDLPLPDFAIGDVGTTIYqI 79
Cdd:PRK00192   1 DMMKLLVFTDLDGTLL--DHHTYSYEpAKPALKALKEK-GIPVIPCTSKTAAEVEV-LRK-ELGLEDPFIVENGAAIY-I 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123593429  80 TDNQWHPWEDWSKEISQDWQGInqagLAKLFADITPLrLQEPEKQNRYKLSYYAppELDWENLI------PQLAQRLQAQ 153
Cdd:PRK00192  75 PKNYFPFQPDGERLKGDYWVIE----LGPPYEELREI-LDEISDELGYPLKGFG--DLSAEEVAeltglsGESARLAKDR 147

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123593429 154 GIQASFIWSVDETAQIGLLDILPKR----------------ANKLHAIRFLmeRQHFDKSHTVFA---GDSGNDLEVLAS 214
Cdd:PRK00192 148 EFSEPFLWNGSEAAKERFEEALKRLglkvtrggrflhllggGDKGKAVRWL--KELYRRQDGVETialGDSPNDLPMLEA 225

                        250       260       270
                 ....*....|....*....|....*....|....*
gi 123593429 215 GLQAILVRNAQEevrqEALRRLPPEHSQQLYLARG 249
Cdd:PRK00192 226 ADIAVVVPGPDG----PNPPLLPGIADGEFILASA 256
HAD_KDO-like cd01630
haloacid dehalogenase-like (HAD) hydrolase, similar to Escherichia coli ...
 148-232 6.88e-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: 39.43  E-value: 6.88e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123593429 148 QRLQAQGIQASFIW-----SVDETAQ-IGLLDILPKRANKLHAIRFLMERQHFDKSHTVFAGDSGNDLEVL-ASGLqAIL 220
Cdd:cd01630   38 KLLQKSGIEVAIITgrqseAVRRRAKeLGIEDLFQGVKDKLEALEELLEKLGLSDEEVAYMGDDLPDLPVMkRVGL-SVA 116

                         90
                 ....*....|..
gi 123593429 221 VRNAQEEVRQEA 232
Cdd:cd01630  117 PADAHPEVREAA 128
YedP COG3769
Mannosyl-3-phosphoglycerate phosphatase YedP/MpgP, HAD superfamily [Carbohydrate transport and ...
 145-223 3.83e-03

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


Pssm-ID: 442983 [Multi-domain]  Cd Length: 268  Bit Score: 38.66  E-value: 3.83e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123593429 145 QLAQRLQAQGIQASF---IWSVdetaqIGlldilpkRANKLHAIRFLME--RQHFDKSHTVFA-GDSGNDLEVLASGLQA 218
Cdd:COG3769  162 RFIAALAALGLTVLRggrFLHL-----MG-------GADKGKAVRWLVEqyRQRFGKNVVTIAlGDSPNDIPMLEAADIA 229


                 ....*
gi 123593429 219 ILVRN 223
Cdd:COG3769  230 VVIRS 234
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH