NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1210264372|dbj|BAZ83367|]
View 

type I phosphodiesterase/nucleotide pyrophosphatase [Sphaerospermopsis kisseleviana NIES-73]

Protein Classification

alkaline phosphatase family protein( domain architecture ID 11445914)

alkaline phosphatase family protein catalyzes the hydrolysis of phosphate monoesters or diesters; similar to Saccharomyces cerevisiae ectonucleotide pyrophosphatase/phosphodiesterase 2, which mediates extracellular nucleotide derived phosphate hydrolysis along with NPP1 and PHO5

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
AtaC COG1524
c-di-AMP phosphodiesterase AtaC or nucleotide pyrophosphatase, AlkP superfamily [Signal ...
 14-386 7.05e-26

c-di-AMP phosphodiesterase AtaC or nucleotide pyrophosphatase, AlkP superfamily [Signal transduction mechanisms];


:

Pssm-ID: 441133 [Multi-domain]  Cd Length: 370  Bit Score: 109.45  E-value: 7.05e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210264372  14 LVCLIAVFSGFQVFAKPPQPHNAVIFVTDGLRPMTVNATDTPTLQSIKEQGVNFVNSHSLFPTFTTANASVIATGHYLGD 93
Cdd:COG1524     4 GLSLLLASLLAAAAAAAPPAKKVVLILVDGLRADLLERAHAPNLAALAARGVYARPLTSVFPSTTAPAHTTLLTGLYPGE 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210264372  94 TGDFSNNikVNVPVKSAKNTIVPFLENDAVLrevnqqfgNNFLNEISLLAIAKKSGFSTAAVGklgpvliqditqetgkp 173
Cdd:COG1524    84 HGIVGNG--WYDPELGRVVNSLSWVEDGFGS--------NSLLPVPTIFERARAAGLTTAAVF----------------- 136

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210264372 174 tiiiddatgtstgiPLSEEISKlLTQNSLPLitPSRGENGKAGdsqnpgakvaNIKQQQYFVDAITKVIlplfkQRKKP- 252
Cdd:COG1524   137 --------------WPSFEGSG-LIDAARPY--PYDGRKPLLG----------NPAADRWIAAAALELL-----REGRPd 184

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210264372 253 FVLVYWSrDPDGTQHNHgdslnqlvpGINGSTVQAAKRNVDNNLAQIIATLKKLDLAKNTNIFVTADHGFSTISKESKTS 332
Cdd:COG1524   185 LLLVYLP-DLDYAGHRY---------GPDSPEYRAALREVDAALGRLLDALKARGLYEGTLVIVTADHGMVDVPPDIDLN 254

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1210264372 333 YAASLSYENVPAGFLPPGFLGIDLADDLELALFNPDQENTQFEPTQGQFSTNSI 386
Cdd:COG1524   255 RLRLAGLLAVRAGESAHLYLKDGADAEVRALLGLPARVLTREELAAGHFGPHRI 308
 
Name Accession Description Interval E-value
AtaC COG1524
c-di-AMP phosphodiesterase AtaC or nucleotide pyrophosphatase, AlkP superfamily [Signal ...
 14-386 7.05e-26

c-di-AMP phosphodiesterase AtaC or nucleotide pyrophosphatase, AlkP superfamily [Signal transduction mechanisms];


Pssm-ID: 441133 [Multi-domain]  Cd Length: 370  Bit Score: 109.45  E-value: 7.05e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210264372  14 LVCLIAVFSGFQVFAKPPQPHNAVIFVTDGLRPMTVNATDTPTLQSIKEQGVNFVNSHSLFPTFTTANASVIATGHYLGD 93
Cdd:COG1524     4 GLSLLLASLLAAAAAAAPPAKKVVLILVDGLRADLLERAHAPNLAALAARGVYARPLTSVFPSTTAPAHTTLLTGLYPGE 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210264372  94 TGDFSNNikVNVPVKSAKNTIVPFLENDAVLrevnqqfgNNFLNEISLLAIAKKSGFSTAAVGklgpvliqditqetgkp 173
Cdd:COG1524    84 HGIVGNG--WYDPELGRVVNSLSWVEDGFGS--------NSLLPVPTIFERARAAGLTTAAVF----------------- 136

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210264372 174 tiiiddatgtstgiPLSEEISKlLTQNSLPLitPSRGENGKAGdsqnpgakvaNIKQQQYFVDAITKVIlplfkQRKKP- 252
Cdd:COG1524   137 --------------WPSFEGSG-LIDAARPY--PYDGRKPLLG----------NPAADRWIAAAALELL-----REGRPd 184

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210264372 253 FVLVYWSrDPDGTQHNHgdslnqlvpGINGSTVQAAKRNVDNNLAQIIATLKKLDLAKNTNIFVTADHGFSTISKESKTS 332
Cdd:COG1524   185 LLLVYLP-DLDYAGHRY---------GPDSPEYRAALREVDAALGRLLDALKARGLYEGTLVIVTADHGMVDVPPDIDLN 254

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1210264372 333 YAASLSYENVPAGFLPPGFLGIDLADDLELALFNPDQENTQFEPTQGQFSTNSI 386
Cdd:COG1524   255 RLRLAGLLAVRAGESAHLYLKDGADAEVRALLGLPARVLTREELAAGHFGPHRI 308
Phosphodiest pfam01663
Type I phosphodiesterase / nucleotide pyrophosphatase; This family consists of ...
 37-328 4.39e-23

Type I phosphodiesterase / nucleotide pyrophosphatase; This family consists of phosphodiesterases, including human plasma-cell membrane glycoprotein PC-1 / alkaline phosphodiesterase i / nucleotide pyrophosphatase (nppase). These enzymes catalyze the cleavage of phosphodiester and phosphosulfate bonds in NAD, deoxynucleotides and nucleotide sugars. Also in this family is ATX an autotaxin, tumour cell motility-stimulating protein which exhibits type I phosphodiesterases activity. The alignment encompasses the active site. Also present with in this family is 60-kDa Ca2+-ATPase form F. odoratum.


Pssm-ID: 396300 [Multi-domain]  Cd Length: 343  Bit Score: 100.96  E-value: 4.39e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210264372  37 VIFVTDGLRPMTVNA-TDTPTLQSIKEQGVNFVNSHSLFPTFTTANASVIATGHYLGDTGDFSNNIkvnvpvksakntIV 115
Cdd:pfam01663   2 LVISLDGFRADYLDRfELTPNLAALAKEGVSAPNLTPVFPTLTFPNHYTLVTGLYPGSHGIVGNTF------------YD 69

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210264372 116 PFLENDAVLREVNQQFGNNFLNEIsLLAIAKKSGFSTAAVGKLGPVLIQDITQETgKPTIIIDDATgtstgiplseeisk 195
Cdd:pfam01663  70 PKTGEYLVFVISDPEDPRWWQGEP-IWDTAAKAGVRAAALFWPGSEVDYSTYYGT-PPRYLKDDYN-------------- 133

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210264372 196 lltqNSLPLITpsrgengkagdsqnpgaKVANIKQQQYFVDAITKVILplfkqrKKPFVLVYWSRDPDGTQHNHGdslnq 275
Cdd:pfam01663 134 ----NSVPFED-----------------RVDTAVLQTWLDLPFADVAA------ERPDLLLVYLEEPDYAGHRYG----- 181

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1210264372 276 lvpgINGSTVQAAKRNVDNNLAQIIATLKKLDLAKNTNIFVTADHGFSTISKE 328
Cdd:pfam01663 182 ----PDSPEVEDALRRVDRAIGDLLEALDERGLFEDTNVIVVSDHGMTPVSDD 230
Enpp cd16018
Ectonucleotide pyrophosphatase/phosphodiesterase, also called autotaxin; Ecto-nucleotide ...
 42-325 1.15e-14

Ectonucleotide pyrophosphatase/phosphodiesterase, also called autotaxin; Ecto-nucleotide pyrophosphatases/phosphodiesterases (ENPPs) hydrolyze 5'-phosphodiester bonds in nucleotides and their derivatives, resulting in the release of 5'-nucleotide monophosphates. ENPPs have multiple physiological roles, including nucleotide recycling, modulation of purinergic receptor signaling, regulation of extracellular pyrophosphate levels, stimulation of cell motility, and possible roles in regulation of insulin receptor (IR) signaling and activity of ecto-kinases. The eukaryotic ENPP family contains at least five members that have different tissue distribution and physiological roles.


Pssm-ID: 293742 [Multi-domain]  Cd Length: 267  Bit Score: 74.54  E-value: 1.15e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210264372  42 DGLRPMTVN-ATDTPTLQSIKEQGVNFVNSHSLFPTFT-TANASvIATGHYLGDTGdFSNNIKVNVPVKSakntivPFLE 119
Cdd:cd16018     9 DGFRWDYLDrAGLTPNLKRLAEEGVRAKYVKPVFPTLTfPNHYS-IVTGLYPESHG-IVGNYFYDPKTNE------EFSD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210264372 120 NDAVLRevnqqfgNNFLNEISLLAIAKKSGFSTAAV---GKLGPVLIQDITQetgkptIIIDDATGTSTGIPLSEEIskl 196
Cdd:cd16018    81 SDWVWD-------PWWIGGEPIWVTAEKAGLKTASYfwpGSEVAIIGYNPTP------IPLGGYWQPYNDSFPFEER--- 144

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210264372 197 ltqnslplitpsrgengkagdsqnpgakvanikqqqyfVDAITKvilplFKQRKKP-FVLVYWSrDPDGTQHNHGdslnq 275
Cdd:cd16018   145 --------------------------------------VDTILE-----WLDLERPdLILLYFE-EPDSAGHKYG----- 175

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 1210264372 276 lvpgINGSTVQAAKRNVDNNLAQIIATLKKLDLAKNTNIFVTADHGFSTI 325
Cdd:cd16018   176 ----PDSPEVNEALKRVDRRLGYLIEALKERGLLDDTNIIVVSDHGMTDV 221
TIGR02687 TIGR02687
TIGR02687 family protein; Members of this family are uncharacterized proteins sporadically ...
 267-322 3.95e-03

TIGR02687 family protein; Members of this family are uncharacterized proteins sporadically distributed in bacteria and archaea, about 880 amino acids in length. This protein is repeatedly found upstream of another uncharacterized protein of about 470 amino acids in length, modeled by TIGR02688.


Pssm-ID: 274259  Cd Length: 844  Bit Score: 40.20  E-value: 3.95e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1210264372 267 HNHGDSLnqlvpGINGSTVQAAKRNVDNNLAQIIATLKKL-DLAKNTNIFVTADHGF 322
Cdd:TIGR02687 577 HNKIDAT-----GDKQSSEENVFEAVEETIVELKKLVKYLiNRLNGTNIIVTADHGF 628
 
Name Accession Description Interval E-value
AtaC COG1524
c-di-AMP phosphodiesterase AtaC or nucleotide pyrophosphatase, AlkP superfamily [Signal ...
 14-386 7.05e-26

c-di-AMP phosphodiesterase AtaC or nucleotide pyrophosphatase, AlkP superfamily [Signal transduction mechanisms];


Pssm-ID: 441133 [Multi-domain]  Cd Length: 370  Bit Score: 109.45  E-value: 7.05e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210264372  14 LVCLIAVFSGFQVFAKPPQPHNAVIFVTDGLRPMTVNATDTPTLQSIKEQGVNFVNSHSLFPTFTTANASVIATGHYLGD 93
Cdd:COG1524     4 GLSLLLASLLAAAAAAAPPAKKVVLILVDGLRADLLERAHAPNLAALAARGVYARPLTSVFPSTTAPAHTTLLTGLYPGE 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210264372  94 TGDFSNNikVNVPVKSAKNTIVPFLENDAVLrevnqqfgNNFLNEISLLAIAKKSGFSTAAVGklgpvliqditqetgkp 173
Cdd:COG1524    84 HGIVGNG--WYDPELGRVVNSLSWVEDGFGS--------NSLLPVPTIFERARAAGLTTAAVF----------------- 136

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210264372 174 tiiiddatgtstgiPLSEEISKlLTQNSLPLitPSRGENGKAGdsqnpgakvaNIKQQQYFVDAITKVIlplfkQRKKP- 252
Cdd:COG1524   137 --------------WPSFEGSG-LIDAARPY--PYDGRKPLLG----------NPAADRWIAAAALELL-----REGRPd 184

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210264372 253 FVLVYWSrDPDGTQHNHgdslnqlvpGINGSTVQAAKRNVDNNLAQIIATLKKLDLAKNTNIFVTADHGFSTISKESKTS 332
Cdd:COG1524   185 LLLVYLP-DLDYAGHRY---------GPDSPEYRAALREVDAALGRLLDALKARGLYEGTLVIVTADHGMVDVPPDIDLN 254

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1210264372 333 YAASLSYENVPAGFLPPGFLGIDLADDLELALFNPDQENTQFEPTQGQFSTNSI 386
Cdd:COG1524   255 RLRLAGLLAVRAGESAHLYLKDGADAEVRALLGLPARVLTREELAAGHFGPHRI 308
Phosphodiest pfam01663
Type I phosphodiesterase / nucleotide pyrophosphatase; This family consists of ...
 37-328 4.39e-23

Type I phosphodiesterase / nucleotide pyrophosphatase; This family consists of phosphodiesterases, including human plasma-cell membrane glycoprotein PC-1 / alkaline phosphodiesterase i / nucleotide pyrophosphatase (nppase). These enzymes catalyze the cleavage of phosphodiester and phosphosulfate bonds in NAD, deoxynucleotides and nucleotide sugars. Also in this family is ATX an autotaxin, tumour cell motility-stimulating protein which exhibits type I phosphodiesterases activity. The alignment encompasses the active site. Also present with in this family is 60-kDa Ca2+-ATPase form F. odoratum.


Pssm-ID: 396300 [Multi-domain]  Cd Length: 343  Bit Score: 100.96  E-value: 4.39e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210264372  37 VIFVTDGLRPMTVNA-TDTPTLQSIKEQGVNFVNSHSLFPTFTTANASVIATGHYLGDTGDFSNNIkvnvpvksakntIV 115
Cdd:pfam01663   2 LVISLDGFRADYLDRfELTPNLAALAKEGVSAPNLTPVFPTLTFPNHYTLVTGLYPGSHGIVGNTF------------YD 69

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210264372 116 PFLENDAVLREVNQQFGNNFLNEIsLLAIAKKSGFSTAAVGKLGPVLIQDITQETgKPTIIIDDATgtstgiplseeisk 195
Cdd:pfam01663  70 PKTGEYLVFVISDPEDPRWWQGEP-IWDTAAKAGVRAAALFWPGSEVDYSTYYGT-PPRYLKDDYN-------------- 133

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210264372 196 lltqNSLPLITpsrgengkagdsqnpgaKVANIKQQQYFVDAITKVILplfkqrKKPFVLVYWSRDPDGTQHNHGdslnq 275
Cdd:pfam01663 134 ----NSVPFED-----------------RVDTAVLQTWLDLPFADVAA------ERPDLLLVYLEEPDYAGHRYG----- 181

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1210264372 276 lvpgINGSTVQAAKRNVDNNLAQIIATLKKLDLAKNTNIFVTADHGFSTISKE 328
Cdd:pfam01663 182 ----PDSPEVEDALRRVDRAIGDLLEALDERGLFEDTNVIVVSDHGMTPVSDD 230
Enpp cd16018
Ectonucleotide pyrophosphatase/phosphodiesterase, also called autotaxin; Ecto-nucleotide ...
 42-325 1.15e-14

Ectonucleotide pyrophosphatase/phosphodiesterase, also called autotaxin; Ecto-nucleotide pyrophosphatases/phosphodiesterases (ENPPs) hydrolyze 5'-phosphodiester bonds in nucleotides and their derivatives, resulting in the release of 5'-nucleotide monophosphates. ENPPs have multiple physiological roles, including nucleotide recycling, modulation of purinergic receptor signaling, regulation of extracellular pyrophosphate levels, stimulation of cell motility, and possible roles in regulation of insulin receptor (IR) signaling and activity of ecto-kinases. The eukaryotic ENPP family contains at least five members that have different tissue distribution and physiological roles.


Pssm-ID: 293742 [Multi-domain]  Cd Length: 267  Bit Score: 74.54  E-value: 1.15e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210264372  42 DGLRPMTVN-ATDTPTLQSIKEQGVNFVNSHSLFPTFT-TANASvIATGHYLGDTGdFSNNIKVNVPVKSakntivPFLE 119
Cdd:cd16018     9 DGFRWDYLDrAGLTPNLKRLAEEGVRAKYVKPVFPTLTfPNHYS-IVTGLYPESHG-IVGNYFYDPKTNE------EFSD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210264372 120 NDAVLRevnqqfgNNFLNEISLLAIAKKSGFSTAAV---GKLGPVLIQDITQetgkptIIIDDATGTSTGIPLSEEIskl 196
Cdd:cd16018    81 SDWVWD-------PWWIGGEPIWVTAEKAGLKTASYfwpGSEVAIIGYNPTP------IPLGGYWQPYNDSFPFEER--- 144

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210264372 197 ltqnslplitpsrgengkagdsqnpgakvanikqqqyfVDAITKvilplFKQRKKP-FVLVYWSrDPDGTQHNHGdslnq 275
Cdd:cd16018   145 --------------------------------------VDTILE-----WLDLERPdLILLYFE-EPDSAGHKYG----- 175

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 1210264372 276 lvpgINGSTVQAAKRNVDNNLAQIIATLKKLDLAKNTNIFVTADHGFSTI 325
Cdd:cd16018   176 ----PDSPEVNEALKRVDRRLGYLIEALKERGLLDDTNIIVVSDHGMTDV 221
ALP_like cd00016
alkaline phosphatases and sulfatases; This family includes alkaline phosphatases and ...
 198-321 3.88e-08

alkaline phosphatases and sulfatases; This family includes alkaline phosphatases and sulfatases. Alkaline phosphatases are non-specific phosphomonoesterases that catalyze the hydrolysis reaction via a phosphoseryl intermediate to produce inorganic phosphate and the corresponding alcohol, optimally at high pH. Alkaline phosphatase exists as a dimer, each monomer binding 2 zinc atoms and one magnesium atom, which are essential for enzymatic activity. Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. Both alkaline phosphatase and sulfatase are essential for human metabolism. Deficiency of individual enzyme cause genetic diseases.


Pssm-ID: 293732 [Multi-domain]  Cd Length: 237  Bit Score: 54.35  E-value: 3.88e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210264372 198 TQNSLPLITPSRGENGKAGDSQNPGAKvanIKQQQY------FVDAITkvilplFKQRKKPFVLVYWSRDPDGTQHNHGd 271
Cdd:cd00016    69 TGNGSADPELPSRAAGKDEDGPTIPEL---LKQAGYrtgvigLLKAID------ETSKEKPFVLFLHFDGPDGPGHAYG- 138

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1210264372 272 slnQLVPGiNGSTVQAakrnVDNNLAQIIATLKKLDLAKNTNIFVTADHG 321
Cdd:cd00016   139 ---PNTPE-YYDAVEE----IDERIGKVLDALKKAGDADDTVIIVTADHG 180
Sulfatase pfam00884
Sulfatase;
35-324 8.07e-06

Sulfatase;


Pssm-ID: 459979 [Multi-domain]  Cd Length: 298  Bit Score: 48.19  E-value: 8.07e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210264372  35 NAVIFVTDGLRPMTVNAT-----DTPTLQSIKEQGVNFVNSHSlfPTFTTANaSVIATghyLgdTGDFSNNIKVNVPVKS 109
Cdd:pfam00884   2 NVVLVLGESLRAPDLGLYgyprpTTPFLDRLAEEGLLFSNFYS--GGTLTAP-SRFAL---L--TGLPPHNFGSYVSTPV 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210264372 110 AKNTIVPflendavlrevnqqfgnnflneiSLLAIAKKSGFSTAAVGKLgpvliqditqetgkptiiidDATGTSTGIPL 189
Cdd:pfam00884  74 GLPRTEP-----------------------SLPDLLKRAGYNTGAIGKW--------------------HLGWYNNQSPC 110

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210264372 190 SEEISKLLtqnslplitpsrGENGKAGDSQNPGAKVANIKQQQYFVDAITKVILPLFKQRKKPFVLVYwsrdpdGTQHNH 269
Cdd:pfam00884 111 NLGFDKFF------------GRNTGSDLYADPPDVPYNCSGGGVSDEALLDEALEFLDNNDKPFFLVL------HTLGSH 172

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1210264372 270 G--DSLNQLVPGINGSTVQAAKRN------------VDNNLAQIIATLKKLDLAKNTNIFVTADHGFST 324
Cdd:pfam00884 173 GppYYPDRYPEKYATFKPSSCSEEqllnsydntllyTDDAIGRVLDKLEENGLLDNTLVVYTSDHGESL 241
AslA COG3119
Arylsulfatase A or related enzyme, AlkP superfamily [Inorganic ion transport and metabolism];
13-323 2.44e-05

Arylsulfatase A or related enzyme, AlkP superfamily [Inorganic ion transport and metabolism];


Pssm-ID: 442353 [Multi-domain]  Cd Length: 393  Bit Score: 46.80  E-value: 2.44e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210264372  13 LLVCLIAVFSGFQVFAKPPQPhNAVIFVTDGLRPMTVNA-----TDTPTLQSIKEQGVNFVNSHSLFPTFTTANASVIaT 87
Cdd:COG3119     4 LLLLLLALLAAAAAAAAAKRP-NILFILADDLGYGDLGCygnplIKTPNIDRLAAEGVRFTNAYVTSPVCSPSRASLL-T 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210264372  88 GHYLGDTGDFSNNIKVNVPVKSAKNTIVpflendavlrevnqqfgnnflneiSLLaiaKKSGFSTAAVGKLGPVLIQDIT 167
Cdd:COG3119    82 GRYPHRTGVTDNGEGYNGGLPPDEPTLA------------------------ELL---KEAGYRTALFGKWHLYLTDLLT 134

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210264372 168 QETgkptiiiddatgtstgiplseeisklltqnslplitpsrgengkagdsqnpgakVANIKQQqyfvdaitkvilplfK 247
Cdd:COG3119   135 DKA------------------------------------------------------IDFLERQ---------------A 145

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210264372 248 QRKKPFVLVYWSRDP--------------DGTQHNHGDSLnqlVPGINGSTVQAAKR--------NVDNNLAQIIATLKK 305
Cdd:COG3119   146 DKDKPFFLYLAFNAPhapyqapeeyldkyDGKDIPLPPNL---APRDLTEEELRRARaayaamieEVDDQVGRLLDALEE 222

                         330
                  ....*....|....*...
gi 1210264372 306 LDLAKNTNIFVTADHGFS 323
Cdd:COG3119   223 LGLADNTIVVFTSDNGPS 240
sulfatase_like cd16148
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ...
 292-323 5.21e-05

uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.


Pssm-ID: 293767 [Multi-domain]  Cd Length: 271  Bit Score: 45.23  E-value: 5.21e-05
                          10        20        30
                  ....*....|....*....|....*....|..
gi 1210264372 292 VDNNLAQIIATLKKLDLAKNTNIFVTADHGFS 323
Cdd:cd16148   172 VDEQIGRLLDKLKELGLLEDTLVIVTSDHGEE 203
sulfatase_like cd16034
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ...
 227-321 6.08e-05

uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.


Pssm-ID: 293758 [Multi-domain]  Cd Length: 399  Bit Score: 45.64  E-value: 6.08e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210264372 227 NIKQQQYFVDAITKVILPLFKQRK---KPFVLVyWS---------RDPDGTQHNHGDSLNQL---VPGINGSTVQAAK-- 289
Cdd:cd16034   148 RIYIKGYSPDAETDLAIEYLENQAdkdKPFALV-LSwnpphdpytTAPEEYLDMYDPKKLLLrpnVPEDKKEEAGLREdl 226

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1210264372 290 -------RNVDNNLAQIIATLKKLDLAKNTNIFVTADHG 321
Cdd:cd16034   227 rgyyamiTALDDNIGRLLDALKELGLLENTIVVFTSDHG 265
sulfatase_like cd16149
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ...
 287-323 9.18e-05

uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.


Pssm-ID: 293768 [Multi-domain]  Cd Length: 257  Bit Score: 44.54  E-value: 9.18e-05
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 1210264372 287 AAKRNVDNNLAQIIATLKKLDLAKNTNIFVTADHGFS 323
Cdd:cd16149   146 AAVTGVDRNVGRLLDELEELGLTENTLVIFTSDNGFN 182
G6S cd16147
glucosamine (N-acetyl)-6-sulfatase(G6S, GNS) AND sulfatase 1(SULF1); ...
 284-322 3.82e-04

glucosamine (N-acetyl)-6-sulfatase(G6S, GNS) AND sulfatase 1(SULF1); N-acetylglucosamine-6-sulfatase also known as glucosamine (N-acetyl)-6-sulfatase hydrolyzes of the 6-sulfate groups of the N-acetyl-D-glucosamine 6-sulfate units of heparan sulfate and keratan sulfate. Deficient of N-acetylglucosamine-6-sulfatase results in disease of Sanfilippo Syndrome type IIId or Mucopolysaccharidosis III (MPS-III), a rare autosomal recessive lysosomal storage disease. SULF1 encodes an extracellular heparan sulfate endosulfatase, that removes 6-O-sulfate groups from heparan sulfate chains of heparan sulfate proteoglycans (HSPGs).


Pssm-ID: 293766 [Multi-domain]  Cd Length: 396  Bit Score: 43.31  E-value: 3.82e-04
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 1210264372 284 TVQAakrnVDNNLAQIIATLKKLDLAKNTNIFVTADHGF 322
Cdd:cd16147   247 TLQS----VDDLVERLVNTLEATGQLDNTYIIYTSDNGY 281
MdoB COG1368
Phosphoglycerol transferase MdoB/OpgB, AlkP superfamily [Cell wall/membrane/envelope ...
 242-374 4.34e-04

Phosphoglycerol transferase MdoB/OpgB, AlkP superfamily [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 440979 [Multi-domain]  Cd Length: 576  Bit Score: 43.10  E-value: 4.34e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210264372 242 ILPLFKQRKKPFVLVYWsrdpdgTQHNHG----DSLNQLVPGINGSTVQ---AAKRNVDNNLAQIIATLKKLDLAKNTNI 314
Cdd:COG1368   375 ALEELEKLKKPFFAFLI------TLSNHGpytlPEEDKKIPDYGKTTLNnylNAVRYADQALGEFIEKLKKSGWYDNTIF 448

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210264372 315 FVTADHGFSTiskESKTSYAASLSYENVPAGFLPPGFLG----------IDLADDLeLALFNPDQENTQF 374
Cdd:COG1368   449 VIYGDHGPRS---PGKTDYENPLERYRVPLLIYSPGLKKpkvidtvgsqIDIAPTL-LDLLGIDYPSYYA 514
PglZ pfam08665
PglZ domain; This family is a member of the Alkaline phosphatase clan.
 267-322 5.21e-04

PglZ domain; This family is a member of the Alkaline phosphatase clan.


Pssm-ID: 430139 [Multi-domain]  Cd Length: 176  Bit Score: 41.19  E-value: 5.21e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1210264372 267 HNHGDSLnqlvpGINGSTVQAAKRNVDNNLAQIIATLKKLDLAKNTNIFVTADHGF 322
Cdd:pfam08665 119 HNKIDAL-----GDKQSTEQKSFEAVEEALVELSDLVRRLLNRLGYRVYLTADHGF 169
G6S_like cd16031
unchracterized sulfatase homologous to glucosamine (N-acetyl)-6-sulfatase(G6S, GNS); ...
 292-322 6.93e-04

unchracterized sulfatase homologous to glucosamine (N-acetyl)-6-sulfatase(G6S, GNS); N-acetylglucosamine-6-sulfatase also known as glucosamine (N-acetyl)-6-sulfatase hydrolyzes of the 6-sulfate groups of the N-acetyl-D-glucosamine 6-sulfate units of heparan sulfate and keratan sulfate. Deficiency of N-acetylglucosamine-6-sulfatase results in the disease of Sanfilippo Syndrome type IIId or Mucopolysaccharidosis III (MPS-III), a rare autosomal recessive lysosomal storage disease.


Pssm-ID: 293755 [Multi-domain]  Cd Length: 429  Bit Score: 42.52  E-value: 6.93e-04
                          10        20        30
                  ....*....|....*....|....*....|.
gi 1210264372 292 VDNNLAQIIATLKKLDLAKNTNIFVTADHGF 322
Cdd:cd16031   246 VDDNVGRILDYLEEQGLADNTIIIYTSDNGF 276
choline-sulfatase cd16032
choline-sulfatase; Choline-sulphatase is involved in the synthesis of glycine betaine from ...
 285-321 9.06e-04

choline-sulfatase; Choline-sulphatase is involved in the synthesis of glycine betaine from choline. The symbiotic soil bacterium Rhizobium meliloti can synthesize glycine betaine from choline-O-sulphate and choline to protect itself from osmotic stress. This biosynthetic pathway is encoded by the betICBA locus, which comprises a regulatory gene, betI, and three structural genes, betC (choline sulfatase), betB (betaine aldehyde dehydrogenase), and betA (choline dehydrogenase). betICBA genes constitute a single operon.


Pssm-ID: 293756 [Multi-domain]  Cd Length: 327  Bit Score: 41.80  E-value: 9.06e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 1210264372 285 VQAAKRN-------VDNNLAQIIATLKKLDLAKNTNIFVTADHG 321
Cdd:cd16032   159 VRRARRAyygmvsyVDDKVGQLLDTLERTGLADDTIVIFTSDHG 202
sulfatase_like cd16022
sulfatase; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, ...
 291-321 1.45e-03

sulfatase; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.


Pssm-ID: 293746 [Multi-domain]  Cd Length: 236  Bit Score: 40.50  E-value: 1.45e-03
                          10        20        30
                  ....*....|....*....|....*....|.
gi 1210264372 291 NVDNNLAQIIATLKKLDLAKNTNIFVTADHG 321
Cdd:cd16022   139 AIDDQIGRILDALEELGLLDNTLIVFTSDHG 169
GALNS cd16157
galactosamine-6-sulfatase; also known as N-acetylgalactosamine-6-sulfatase (GALNS); Lysosomal ...
 248-326 2.41e-03

galactosamine-6-sulfatase; also known as N-acetylgalactosamine-6-sulfatase (GALNS); Lysosomal galactosamine-6-sulfatase removes sulfate groups from a terminal N-acetylgalactosamine-6-sulfate (or galactose-6-sulfate) in mucopolysaccharides such as keratan sulfate and chondroitin-6-sulfate. Defects in GALNS lead to accumulation of substrates, resulting in the development of the lysosomal storage disease mucopolysaccharidosis IV A.


Pssm-ID: 293776 [Multi-domain]  Cd Length: 466  Bit Score: 40.91  E-value: 2.41e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210264372 248 QRKKPFVLvYWSrdPDGTQHNHGDS---LNQLVPGINGSTVqaakRNVDNNLAQIIATLKKLDLAKNTNIFVTADHGFST 324
Cdd:cd16157   193 DAQKPFFL-YWA--PDATHAPVYASkpfLGTSQRGLYGDAV----MELDSSVGKILESLKSLGIENNTFVFFSSDNGAAL 265


                  ..
gi 1210264372 325 IS 326
Cdd:cd16157   266 IS 267
SGSH cd16027
N-sulfoglucosamine sulfohydrolase (SGSH; sulfamidase); N-sulfoglucosamine sulfohydrolase (SGSH) ...
 293-321 3.77e-03

N-sulfoglucosamine sulfohydrolase (SGSH; sulfamidase); N-sulfoglucosamine sulfohydrolase (SGSH) belongs to the sulfatase family and catalyses the cleavage of N-linked sulfate groups from the GAGs heparin sulfate and heparin. The active site is characterized by the amino-acid sequence motif C(X)PSR that is highly conserved among most sulfatases. The cysteine residue is post-translationally converted to a formylglycine (FGly) residue, which is crucial for the catalytic process. Loss of function of SGSH results a disease called mucopolysaccharidosis type IIIA (Sanfilippo A syndrome), a fatal childhood-onset neurodegenerative disease with mild facial, visceral and skeletal abnormalities.


Pssm-ID: 293751 [Multi-domain]  Cd Length: 373  Bit Score: 39.80  E-value: 3.77e-03
                          10        20
                  ....*....|....*....|....*....
gi 1210264372 293 DNNLAQIIATLKKLDLAKNTNIFVTADHG 321
Cdd:cd16027   199 DQQVGEILDELEEDGLLDNTIVIFTSDHG 227
TIGR02687 TIGR02687
TIGR02687 family protein; Members of this family are uncharacterized proteins sporadically ...
 267-322 3.95e-03

TIGR02687 family protein; Members of this family are uncharacterized proteins sporadically distributed in bacteria and archaea, about 880 amino acids in length. This protein is repeatedly found upstream of another uncharacterized protein of about 470 amino acids in length, modeled by TIGR02688.


Pssm-ID: 274259  Cd Length: 844  Bit Score: 40.20  E-value: 3.95e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1210264372 267 HNHGDSLnqlvpGINGSTVQAAKRNVDNNLAQIIATLKKL-DLAKNTNIFVTADHGF 322
Cdd:TIGR02687 577 HNKIDAT-----GDKQSSEENVFEAVEETIVELKKLVKYLiNRLNGTNIIVTADHGF 628
sulfatase_like cd16037
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ...
 292-321 4.53e-03

uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.


Pssm-ID: 293760 [Multi-domain]  Cd Length: 321  Bit Score: 39.45  E-value: 4.53e-03
                          10        20        30
                  ....*....|....*....|....*....|
gi 1210264372 292 VDNNLAQIIATLKKLDLAKNTNIFVTADHG 321
Cdd:cd16037   171 LDENIGRVLDALEELGLLDNTLIIYTSDHG 200
iduronate-2-sulfatase cd16030
iduronate-2-sulfatase; Iduronate 2-sulfatase is a sulfatase enzyme that catalyze the ...
 292-323 4.60e-03

iduronate-2-sulfatase; Iduronate 2-sulfatase is a sulfatase enzyme that catalyze the hydrolysis of sulfate ester bonds from a wide variety of substrates, including steroids, carbohydrates and proteins. Iduronate 2-sulfatase is required for the lysosomal degradation of heparan sulfate and dermatan sulfate. Mutations in the iduronate 2-sulfatase gene that result in enzymatic deficiency lead to the sex-linked mucopolysaccharidosis type II, also known as Hunter syndrome.


Pssm-ID: 293754 [Multi-domain]  Cd Length: 435  Bit Score: 39.86  E-value: 4.60e-03
                          10        20        30
                  ....*....|....*....|....*....|..
gi 1210264372 292 VDNNLAQIIATLKKLDLAKNTNIFVTADHGFS 323
Cdd:cd16030   270 VDAQVGRVLDALEELGLADNTIVVLWSDHGWH 301
sulfatase_like cd16035
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ...
 290-321 4.69e-03

uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.


Pssm-ID: 293759 [Multi-domain]  Cd Length: 311  Bit Score: 39.50  E-value: 4.69e-03
                          10        20        30
                  ....*....|....*....|....*....|..
gi 1210264372 290 RNVDNNLAQIIATLKKLDLAKNTNIFVTADHG 321
Cdd:cd16035   174 RDVDRQIGRVLDALDASGLADNTIVVFTSDHG 205
ARSA cd16158
Arylsulfatase A or cerebroside-sulfatase; Arylsulfatase A breaks down sulfatides, namely ...
 248-362 6.36e-03

Arylsulfatase A or cerebroside-sulfatase; Arylsulfatase A breaks down sulfatides, namely cerebroside 3-sulfate into cerebroside and sulfate. It is a member of the sulfatase family. The arylsulfatase A was located in lysosome-like structures and transported to dense lysosomes in a mannose 6-phosphate receptor-dependent manner. Deficiency of arylsulfatase A leads to the accumulation of cerebroside sulfate, which causes a lethal progressive demyelination. Arylsulfatase A requires the posttranslational oxidation of the -CH2SH group of a conserved cysteine to an aldehyde, yielding a formylglycine to be in an active form.


Pssm-ID: 293777 [Multi-domain]  Cd Length: 479  Bit Score: 39.35  E-value: 6.36e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210264372 248 QRKKPFVLVYWSRDPDGTQHNHGDSLNQLVPGINGStvqaAKRNVDNNLAQIIATLKKLDLAKNTNIFVTADHGFSTISK 327
Cdd:cd16158   195 KEGKPFFLYYASHHTHYPQFAGQKFAGRSSRGPFGD----ALAELDGSVGELLQTLKENGIDNNTLVFFTSDNGPSTMRK 270

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1210264372 328 ESKTSY-----AASLSYEN---VPA-----GFLPPGfLGIDLADDLEL 362
Cdd:cd16158   271 SRGGNAgllkcGKGTTYEGgvrEPAiaywpGRIKPG-VTHELASTLDI 317
ARS_like cd16144
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ...
 291-321 7.77e-03

uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.


Pssm-ID: 293763 [Multi-domain]  Cd Length: 421  Bit Score: 39.06  E-value: 7.77e-03
                          10        20        30
                  ....*....|....*....|....*....|.
gi 1210264372 291 NVDNNLAQIIATLKKLDLAKNTNIFVTADHG 321
Cdd:cd16144   231 SLDESVGRILDALEELGLADNTLVIFTSDNG 261
 
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