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Conserved domains on  [gi|15233665|ref|NP_194699|]
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Alkaline-phosphatase-like family protein [Arabidopsis thaliana]

Protein Classification

nucleotide pyrophosphatase/phosphodiesterase family protein( domain architecture ID 12025720)

nucleotide pyrophosphatase/phosphodiesterase family protein catalyzes the cleavage of phosphodiester and phosphosulfate bonds in NAD, deoxynucleotides and/or nucleotide sugars; belongs to the alkaline phosphatase superfamily

CATH:  3.40.720.10
EC:  3.-.-.-
Gene Ontology:  GO:0016787

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
Phosphodiest pfam01663
Type I phosphodiesterase / nucleotide pyrophosphatase; This family consists of ...
60-394 3.46e-119

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: 352.11  E-value: 3.46e-119
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233665    60 VLMISCDGFRFGYQFK-TDTPNIDLLISGGTEAKHgLIPVFPTMTFPNHYSIATGLYPAYHGIIMNKFTDPVTGEVFN-- 136
Cdd:pfam01663   1 LLVISLDGFRADYLDRfELTPNLAALAKEGVSAPN-LTPVFPTLTFPNHYTLVTGLYPGSHGIVGNTFYDPKTGEYLVfv 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233665   137 --KGLQPKWWLGEPLWVTAVNQGLKAVTYFWPGSEVLKSSW-TCPEGYC-PHFNLSVPLEERVDSVLS------HFDHLE 206
Cdd:pfam01663  80 isDPEDPRWWQGEPIWDTAAKAGVRAAALFWPGSEVDYSTYyGTPPRYLkDDYNNSVPFEDRVDTAVLqtwldlPFADVA 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233665   207 DEVPDLLMLYFDEPDQSGHNYGPDDPRVTTAVSRVDKMIGRVIKGLKQREIFDEVHVILLGDHGMVTNceCNEKAIYIDD 286
Cdd:pfam01663 160 AERPDLLLVYLEEPDYAGHRYGPDSPEVEDALRRVDRAIGDLLEALDERGLFEDTNVIVVSDHGMTPV--SDDKVIFLND 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233665   287 LAD---WIKIPAAWiqaysPVLAINPQWGKDVENQSEKNAEVVAKMNEALSSGKVKNGEFLKVYLKEKLPERLHFSEsyR 363
Cdd:pfam01663 238 YLRekgLLHLVDGG-----PVVAIYPKARELGHVPPGEVEEVYAELKEKLLGLRIQDGEHLAVYLKEEIPGRLHYNP--R 310
                         330       340       350
                  ....*....|....*....|....*....|...
gi 15233665   364 IPPIIGIVGEGLMVRQNRTNAQVCY--GDHGYD 394
Cdd:pfam01663 311 IPDLVLVADPGWYITGKDGGDKEAAihGTHGYD 343
 
Name Accession Description Interval E-value
Phosphodiest pfam01663
Type I phosphodiesterase / nucleotide pyrophosphatase; This family consists of ...
60-394 3.46e-119

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: 352.11  E-value: 3.46e-119
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233665    60 VLMISCDGFRFGYQFK-TDTPNIDLLISGGTEAKHgLIPVFPTMTFPNHYSIATGLYPAYHGIIMNKFTDPVTGEVFN-- 136
Cdd:pfam01663   1 LLVISLDGFRADYLDRfELTPNLAALAKEGVSAPN-LTPVFPTLTFPNHYTLVTGLYPGSHGIVGNTFYDPKTGEYLVfv 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233665   137 --KGLQPKWWLGEPLWVTAVNQGLKAVTYFWPGSEVLKSSW-TCPEGYC-PHFNLSVPLEERVDSVLS------HFDHLE 206
Cdd:pfam01663  80 isDPEDPRWWQGEPIWDTAAKAGVRAAALFWPGSEVDYSTYyGTPPRYLkDDYNNSVPFEDRVDTAVLqtwldlPFADVA 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233665   207 DEVPDLLMLYFDEPDQSGHNYGPDDPRVTTAVSRVDKMIGRVIKGLKQREIFDEVHVILLGDHGMVTNceCNEKAIYIDD 286
Cdd:pfam01663 160 AERPDLLLVYLEEPDYAGHRYGPDSPEVEDALRRVDRAIGDLLEALDERGLFEDTNVIVVSDHGMTPV--SDDKVIFLND 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233665   287 LAD---WIKIPAAWiqaysPVLAINPQWGKDVENQSEKNAEVVAKMNEALSSGKVKNGEFLKVYLKEKLPERLHFSEsyR 363
Cdd:pfam01663 238 YLRekgLLHLVDGG-----PVVAIYPKARELGHVPPGEVEEVYAELKEKLLGLRIQDGEHLAVYLKEEIPGRLHYNP--R 310
                         330       340       350
                  ....*....|....*....|....*....|...
gi 15233665   364 IPPIIGIVGEGLMVRQNRTNAQVCY--GDHGYD 394
Cdd:pfam01663 311 IPDLVLVADPGWYITGKDGGDKEAAihGTHGYD 343
Enpp cd16018
Ectonucleotide pyrophosphatase/phosphodiesterase, also called autotaxin; Ecto-nucleotide ...
58-434 5.60e-95

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: 287.17  E-value: 5.60e-95
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233665  58 PVVLMISCDGFRFGY-QFKTDTPNIDLLISGGTEAKhGLIPVFPTMTFPNHYSIATGLYPAYHGIIMNKFTDPVTGEVFN 136
Cdd:cd16018   1 PPLIVISIDGFRWDYlDRAGLTPNLKRLAEEGVRAK-YVKPVFPTLTFPNHYSIVTGLYPESHGIVGNYFYDPKTNEEFS 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233665 137 KGL---QPKWWLGEPLWVTAVNQGLKAVTYFWPGSEVLKSSWTCPE----GYCPHFNLSVPLEERVDSVLSHFDhleDEV 209
Cdd:cd16018  80 DSDwvwDPWWIGGEPIWVTAEKAGLKTASYFWPGSEVAIIGYNPTPiplgGYWQPYNDSFPFEERVDTILEWLD---LER 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233665 210 PDLLMLYFDEPDQSGHNYGPDDPRVTTAVSRVDKMIGRVIKGLKQREIFDEVHVILLGDHGMVTncecnekaiyiddlad 289
Cdd:cd16018 157 PDLILLYFEEPDSAGHKYGPDSPEVNEALKRVDRRLGYLIEALKERGLLDDTNIIVVSDHGMTD---------------- 220
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233665 290 wikipaawiqayspvlainpqwgkdvenqseknaevvakmnealssgkvkngeflkvylkeklperlhfsesyrippiig 369
Cdd:cd16018     --------------------------------------------------------------------------------
                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15233665 370 ivgeglmvrqnrtnaqvcYGDHGYDNELFSMRTIFVGHGSRFSRGKKVPSFENVQIYNVVAELLG 434
Cdd:cd16018 221 ------------------VGTHGYDNELPDMRAIFIARGPAFKKGKKLGPFRNVDIYPLMCNLLG 267
AtaC COG1524
c-di-AMP phosphodiesterase AtaC or nucleotide pyrophosphatase, AlkP superfamily [Signal ...
60-435 6.27e-70

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


Pssm-ID: 441133 [Multi-domain]  Cd Length: 370  Bit Score: 226.55  E-value: 6.27e-70
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233665  60 VLMISCDGFRFGYQFKTDTPNIDLLISGGTEAKhGLIPVFPTMTFPNHYSIATGLYPAYHGIIMNKFTDPVTGEVFN--- 136
Cdd:COG1524  26 VVLILVDGLRADLLERAHAPNLAALAARGVYAR-PLTSVFPSTTAPAHTTLLTGLYPGEHGIVGNGWYDPELGRVVNsls 104
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233665 137 ----KGLQPKWWLGEPLWVTAVNQGLKAVTYFWPGSEVLKSS-WTCPEGYCPHFNLSVPLEERVDSVLSHFDHLEDEVPD 211
Cdd:COG1524 105 wvedGFGSNSLLPVPTIFERARAAGLTTAAVFWPSFEGSGLIdAARPYPYDGRKPLLGNPAADRWIAAAALELLREGRPD 184
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233665 212 LLMLYFDEPDQSGHNYGPDDPRVTTAVSRVDKMIGRVIKGLKQREIFDEVHVILLGDHGMVTncecNEKAIYIDDLADwi 291
Cdd:COG1524 185 LLLVYLPDLDYAGHRYGPDSPEYRAALREVDAALGRLLDALKARGLYEGTLVIVTADHGMVD----VPPDIDLNRLRL-- 258
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233665 292 kipAAWIQAYSPVLAinpqwgkDVENQSEKNAEVVAKMnealssgkvknGEFLKVYLKEKLpERLHFSESyRIPPIIgiv 371
Cdd:COG1524 259 ---AGLLAVRAGESA-------HLYLKDGADAEVRALL-----------GLPARVLTREEL-AAGHFGPH-RIGDLV--- 312
                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15233665 372 gegLMVRQNRTNAQVCYGDHGYDNELfSMRTIFVGHGSRFSRGkkvpsFENVQIYNVVAELLGL 435
Cdd:COG1524 313 ---LVAKPGWALDAPLKGSHGGLPDE-EMRVPLLASGPGFRPG-----VRNVDVAPTIARLLGL 367
 
Name Accession Description Interval E-value
Phosphodiest pfam01663
Type I phosphodiesterase / nucleotide pyrophosphatase; This family consists of ...
60-394 3.46e-119

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: 352.11  E-value: 3.46e-119
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233665    60 VLMISCDGFRFGYQFK-TDTPNIDLLISGGTEAKHgLIPVFPTMTFPNHYSIATGLYPAYHGIIMNKFTDPVTGEVFN-- 136
Cdd:pfam01663   1 LLVISLDGFRADYLDRfELTPNLAALAKEGVSAPN-LTPVFPTLTFPNHYTLVTGLYPGSHGIVGNTFYDPKTGEYLVfv 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233665   137 --KGLQPKWWLGEPLWVTAVNQGLKAVTYFWPGSEVLKSSW-TCPEGYC-PHFNLSVPLEERVDSVLS------HFDHLE 206
Cdd:pfam01663  80 isDPEDPRWWQGEPIWDTAAKAGVRAAALFWPGSEVDYSTYyGTPPRYLkDDYNNSVPFEDRVDTAVLqtwldlPFADVA 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233665   207 DEVPDLLMLYFDEPDQSGHNYGPDDPRVTTAVSRVDKMIGRVIKGLKQREIFDEVHVILLGDHGMVTNceCNEKAIYIDD 286
Cdd:pfam01663 160 AERPDLLLVYLEEPDYAGHRYGPDSPEVEDALRRVDRAIGDLLEALDERGLFEDTNVIVVSDHGMTPV--SDDKVIFLND 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233665   287 LAD---WIKIPAAWiqaysPVLAINPQWGKDVENQSEKNAEVVAKMNEALSSGKVKNGEFLKVYLKEKLPERLHFSEsyR 363
Cdd:pfam01663 238 YLRekgLLHLVDGG-----PVVAIYPKARELGHVPPGEVEEVYAELKEKLLGLRIQDGEHLAVYLKEEIPGRLHYNP--R 310
                         330       340       350
                  ....*....|....*....|....*....|...
gi 15233665   364 IPPIIGIVGEGLMVRQNRTNAQVCY--GDHGYD 394
Cdd:pfam01663 311 IPDLVLVADPGWYITGKDGGDKEAAihGTHGYD 343
Enpp cd16018
Ectonucleotide pyrophosphatase/phosphodiesterase, also called autotaxin; Ecto-nucleotide ...
58-434 5.60e-95

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: 287.17  E-value: 5.60e-95
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233665  58 PVVLMISCDGFRFGY-QFKTDTPNIDLLISGGTEAKhGLIPVFPTMTFPNHYSIATGLYPAYHGIIMNKFTDPVTGEVFN 136
Cdd:cd16018   1 PPLIVISIDGFRWDYlDRAGLTPNLKRLAEEGVRAK-YVKPVFPTLTFPNHYSIVTGLYPESHGIVGNYFYDPKTNEEFS 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233665 137 KGL---QPKWWLGEPLWVTAVNQGLKAVTYFWPGSEVLKSSWTCPE----GYCPHFNLSVPLEERVDSVLSHFDhleDEV 209
Cdd:cd16018  80 DSDwvwDPWWIGGEPIWVTAEKAGLKTASYFWPGSEVAIIGYNPTPiplgGYWQPYNDSFPFEERVDTILEWLD---LER 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233665 210 PDLLMLYFDEPDQSGHNYGPDDPRVTTAVSRVDKMIGRVIKGLKQREIFDEVHVILLGDHGMVTncecnekaiyiddlad 289
Cdd:cd16018 157 PDLILLYFEEPDSAGHKYGPDSPEVNEALKRVDRRLGYLIEALKERGLLDDTNIIVVSDHGMTD---------------- 220
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233665 290 wikipaawiqayspvlainpqwgkdvenqseknaevvakmnealssgkvkngeflkvylkeklperlhfsesyrippiig 369
Cdd:cd16018     --------------------------------------------------------------------------------
                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15233665 370 ivgeglmvrqnrtnaqvcYGDHGYDNELFSMRTIFVGHGSRFSRGKKVPSFENVQIYNVVAELLG 434
Cdd:cd16018 221 ------------------VGTHGYDNELPDMRAIFIARGPAFKKGKKLGPFRNVDIYPLMCNLLG 267
AtaC COG1524
c-di-AMP phosphodiesterase AtaC or nucleotide pyrophosphatase, AlkP superfamily [Signal ...
60-435 6.27e-70

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


Pssm-ID: 441133 [Multi-domain]  Cd Length: 370  Bit Score: 226.55  E-value: 6.27e-70
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233665  60 VLMISCDGFRFGYQFKTDTPNIDLLISGGTEAKhGLIPVFPTMTFPNHYSIATGLYPAYHGIIMNKFTDPVTGEVFN--- 136
Cdd:COG1524  26 VVLILVDGLRADLLERAHAPNLAALAARGVYAR-PLTSVFPSTTAPAHTTLLTGLYPGEHGIVGNGWYDPELGRVVNsls 104
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233665 137 ----KGLQPKWWLGEPLWVTAVNQGLKAVTYFWPGSEVLKSS-WTCPEGYCPHFNLSVPLEERVDSVLSHFDHLEDEVPD 211
Cdd:COG1524 105 wvedGFGSNSLLPVPTIFERARAAGLTTAAVFWPSFEGSGLIdAARPYPYDGRKPLLGNPAADRWIAAAALELLREGRPD 184
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233665 212 LLMLYFDEPDQSGHNYGPDDPRVTTAVSRVDKMIGRVIKGLKQREIFDEVHVILLGDHGMVTncecNEKAIYIDDLADwi 291
Cdd:COG1524 185 LLLVYLPDLDYAGHRYGPDSPEYRAALREVDAALGRLLDALKARGLYEGTLVIVTADHGMVD----VPPDIDLNRLRL-- 258
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233665 292 kipAAWIQAYSPVLAinpqwgkDVENQSEKNAEVVAKMnealssgkvknGEFLKVYLKEKLpERLHFSESyRIPPIIgiv 371
Cdd:COG1524 259 ---AGLLAVRAGESA-------HLYLKDGADAEVRALL-----------GLPARVLTREEL-AAGHFGPH-RIGDLV--- 312
                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15233665 372 gegLMVRQNRTNAQVCYGDHGYDNELfSMRTIFVGHGSRFSRGkkvpsFENVQIYNVVAELLGL 435
Cdd:COG1524 313 ---LVAKPGWALDAPLKGSHGGLPDE-EMRVPLLASGPGFRPG-----VRNVDVAPTIARLLGL 367
ALP_like cd00016
alkaline phosphatases and sulfatases; This family includes alkaline phosphatases and ...
57-271 8.79e-26

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: 105.20  E-value: 8.79e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233665  57 KPVVLmISCDGFRFGYQFKTD-----TPNIDLLISGGTEAK-HGLIPvfPTMTFPNHYSIATGLYPAYHGIIMNKFTDPV 130
Cdd:cd00016   1 KHVVL-IVLDGLGADDLGKAGnpaptTPNLKRLASEGATFNfRSVSP--PTSSAPNHAALLTGAYPTLHGYTGNGSADPE 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233665 131 TGEVFNKglqpKWWLGEPLWVTAVNQGLKAVTYFwpgsevlksswtcpegycphfnlsvpleervdsVLSHFDHLEDEVP 210
Cdd:cd00016  78 LPSRAAG----KDEDGPTIPELLKQAGYRTGVIG---------------------------------LLKAIDETSKEKP 120
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15233665 211 DLLMLYFDEPDQSGHNYGPDDPRVTTAVSRVDKMIGRVIKGLKQREIFDEVHVILLGDHGM 271
Cdd:cd00016 121 FVLFLHFDGPDGPGHAYGPNTPEYYDAVEEIDERIGKVLDALKKAGDADDTVIIVTADHGG 181
sulfatase_like cd16148
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ...
60-270 3.41e-13

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: 69.50  E-value: 3.41e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233665  60 VLMISCDGFRF------GYQFKTdTPNIDLLISGGTEAKHGLIPVFPTMtfPNHYSIATGLYPAYHGIIMNKFT--DPVT 131
Cdd:cd16148   3 VILIVIDSLRAdhlgcyGYDRVT-TPNLDRLAAEGVVFDNHYSGSNPTL--PSRFSLFTGLYPFYHGVWGGPLEpdDPTL 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233665 132 GEVFNKglqpkwwLGeplWVTAvnqglkAVT---YFWPGSEVLK--SSWTCPEGYC--PHFNLSVPLEERVDSVLSHFDH 204
Cdd:cd16148  80 AEILRK-------AG---YYTA------AVSsnpHLFGGPGFDRgfDTFEDFRGQEgdPGEEGDERAERVTDRALEWLDR 143
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15233665 205 LEDEVPDLLMLYFDEPdqsgHN-YGPDdprvtTAVSRVDKMIGRVIKGLKQREIFDEVHVILLGDHG 270
Cdd:cd16148 144 NADDDPFFLFLHYFDP----HEpYLYD-----AEVRYVDEQIGRLLDKLKELGLLEDTLVIVTSDHG 201
AslA COG3119
Arylsulfatase A or related enzyme, AlkP superfamily [Inorganic ion transport and metabolism];
57-270 5.34e-08

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


Pssm-ID: 442353 [Multi-domain]  Cd Length: 393  Bit Score: 54.88  E-value: 5.34e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233665  57 KPVVLMISCDGFRFGY-----QFKTDTPNIDLLisggteAKHGlipvfptMTFPNHY-----------SIATGLYPAYHG 120
Cdd:COG3119  23 RPNILFILADDLGYGDlgcygNPLIKTPNIDRL------AAEG-------VRFTNAYvtspvcspsraSLLTGRYPHRTG 89
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233665 121 IIMNKF-------TDPVT-GEVFNK--------GlqpKWWLGEPLWVTAvnqglKAVT--------------YFWPGSev 170
Cdd:COG3119  90 VTDNGEgyngglpPDEPTlAELLKEagyrtalfG---KWHLYLTDLLTD-----KAIDflerqadkdkpfflYLAFNA-- 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233665 171 lksswtcpegycPHFNLSVPlEERVDsvlsHFDHLEDEVPDLLMLYFDEPDQSG---HNYGpddprvtTAVSRVDKMIGR 247
Cdd:COG3119 160 ------------PHAPYQAP-EEYLD----KYDGKDIPLPPNLAPRDLTEEELRrarAAYA-------AMIEEVDDQVGR 215
                       250       260
                ....*....|....*....|...
gi 15233665 248 VIKGLKQREIFDEVHVILLGDHG 270
Cdd:COG3119 216 LLDALEELGLADNTIVVFTSDNG 238
SGSH cd16027
N-sulfoglucosamine sulfohydrolase (SGSH; sulfamidase); N-sulfoglucosamine sulfohydrolase (SGSH) ...
60-272 8.33e-08

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: 54.05  E-value: 8.33e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233665  60 VLMISCD--GFRFGYQFKTD--TPNIDLLisggteAKHGlipvfptMTFPNHY-----------SIATGLYPAYHGIIMN 124
Cdd:cd16027   3 ILWIIADdlSPDLGGYGGNVvkTPNLDRL------AAEG-------VRFTNAFttapvcspsrsALLTGLYPHQNGAHGL 69
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233665 125 -----KFTDPVTG--EVFNK-----GLQPKWWLG---EPLWVTAVNQGLKAVTYFWPGSEVLKSSWTCPEG---YCPHFN 186
Cdd:cd16027  70 rsrgfPLPDGVKTlpELLREagyytGLIGKTHYNpdaVFPFDDEMRGPDDGGRNAWDYASNAADFLNRAKKgqpFFLWFG 149
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233665 187 LSVPLE--ERVDSVLSHFDHLEDEVPDllmlyfdepdqsghnYGPDDPRV-------TTAVSRVDKMIGRVIKGLKQREI 257
Cdd:cd16027 150 FHDPHRpyPPGDGEEPGYDPEKVKVPP---------------YLPDTPEVredladyYDEIERLDQQVGEILDELEEDGL 214
                       250
                ....*....|....*
gi 15233665 258 FDEVHVILLGDHGMV 272
Cdd:cd16027 215 LDNTIVIFTSDHGMP 229
Sulfatase pfam00884
Sulfatase;
59-270 1.47e-07

Sulfatase;


Pssm-ID: 459979 [Multi-domain]  Cd Length: 298  Bit Score: 52.81  E-value: 1.47e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233665    59 VVLMIScDGFRFG----YQFKT-DTPNIDLLisggteAKHGLipvfptmTFPNHYS-----------IATGLYPAYHGII 122
Cdd:pfam00884   3 VVLVLG-ESLRAPdlglYGYPRpTTPFLDRL------AEEGL-------LFSNFYSggtltapsrfaLLTGLPPHNFGSY 68
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233665   123 MNKFTDPVTGEV----------FNKGLQPKWWLGePLWVTAV-NQGLKAVTYFWPGSEVLKSSWTCPEGYCPHFNLSVPL 191
Cdd:pfam00884  69 VSTPVGLPRTEPslpdllkragYNTGAIGKWHLG-WYNNQSPcNLGFDKFFGRNTGSDLYADPPDVPYNCSGGGVSDEAL 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233665   192 EERVDSVLSHFDHledevPDLLMLYFDEPdQSGHNYGPDDPRVT------------------TAVSRVDKMIGRVIKGLK 253
Cdd:pfam00884 148 LDEALEFLDNNDK-----PFFLVLHTLGS-HGPPYYPDRYPEKYatfkpsscseeqllnsydNTLLYTDDAIGRVLDKLE 221
                         250
                  ....*....|....*..
gi 15233665   254 QREIFDEVHVILLGDHG 270
Cdd:pfam00884 222 ENGLLDNTLVVYTSDHG 238
sulfatase_like cd16022
sulfatase; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, ...
60-270 1.49e-07

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: 52.05  E-value: 1.49e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233665  60 VLMISCDGFRFG----YQFKT-DTPNIDLLISGGTeakhglipvfptmTFPNHY-----------SIATGLYPAYHGIim 123
Cdd:cd16022   3 ILLIMTDDLGYDdlgcYGNPDiKTPNLDRLAAEGV-------------RFTNAYvaspvcspsraSLLTGRYPHRHGV-- 67
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233665 124 nkftdpvtgeVFNKGLQPKWWLGEPLWVtavnqglkavtyfwpgsEVLKSSwtcpeGY-CPHF----NLSVP-LEERvds 197
Cdd:cd16022  68 ----------RGNVGNGGGLPPDEPTLA-----------------ELLKEA-----GYrTALIgkwhDEAIDfIERR--- 112
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15233665 198 vlshfdhlEDEVPDLLMLYFDEPdqsgHN----YGpddprvttAVSRVDKMIGRVIKGLKQREIFDEVHVILLGDHG 270
Cdd:cd16022 113 --------DKDKPFFLYVSFNAP----HPpfayYA--------MVSAIDDQIGRILDALEELGLLDNTLIVFTSDHG 169
sulfatase_like cd16034
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ...
57-270 4.94e-07

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: 51.80  E-value: 4.94e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233665  57 KPVVLMISCDGFRF---GYQFKTD--TPNIDLLisggteAKHGLIpvfptmtFPNHYS-----------IATGLYPAYHG 120
Cdd:cd16034   1 KPNILFIFADQHRAqalGCAGDDPvkTPNLDRL------AKEGVV-------FTNAVSnypvcspyrasLLTGQYPLTNG 67
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233665 121 IIMNKFT---DPVT-GEVFNK--------GlqpKWWLGEPlwvtaVNQGLKAVTYFWP-----GSEVLKSSWTCPEGYCP 183
Cdd:cd16034  68 VFGNDVPlppDAPTiADVLKDagyrtgyiG---KWHLDGP-----ERNDGRADDYTPPperrhGFDYWKGYECNHDHNNP 139
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233665 184 HFNLSVP--------------------LEERVDS------VLS----HFDHleDEVPDLLMLYFDepdQSGHNYGPDDPR 233
Cdd:cd16034 140 HYYDDDGkriyikgyspdaetdlaieyLENQADKdkpfalVLSwnppHDPY--TTAPEEYLDMYD---PKKLLLRPNVPE 214
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|.
gi 15233665 234 VTT--------------AVSRVDKMIGRVIKGLKQREIFDEVHVILLGDHG 270
Cdd:cd16034 215 DKKeeaglredlrgyyaMITALDDNIGRLLDALKELGLLENTIVVFTSDHG 265
ARS_like cd16144
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ...
63-270 1.85e-06

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: 49.85  E-value: 1.85e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233665  63 ISCDGFRFgYQfktdTPNIDLLisggteAKHGlipvfptMTFPNHY-----------SIATGLYPAYHGIimnkfTDPVT 131
Cdd:cd16144  16 LGCYGSKF-YE----TPNIDRL------AKEG-------MRFTQAYaaapvcspsraSILTGQYPARLGI-----TDVIP 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233665 132 GEVFNKGLQPkwwLGEPLWVTAVNqgLKAVTYfwpgSEVLK---------------------------------SSWTCP 178
Cdd:cd16144  73 GRRGPPDNTK---LIPPPSTTRLP--LEEVTI----AEALKdagyatahfgkwhlggeggygpedqgfdvniggTGNGGP 143
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233665 179 EGYCPHFNLSVPLEE-------RVDSV-------------------LSHFD-HLEDEVPDLLMLYFDEpDQSGHNYGPDD 231
Cdd:cd16144 144 PSYYFPPGKPNPDLEdgpegeyLTDRLtdeaidfieqnkdkpfflyLSHYAvHTPIQARPELIEKYEK-KKKGLRKGQKN 222
                       250       260       270
                ....*....|....*....|....*....|....*....
gi 15233665 232 PRVTTAVSRVDKMIGRVIKGLKQREIFDEVHVILLGDHG 270
Cdd:cd16144 223 PVYAAMIESLDESVGRILDALEELGLADNTLVIFTSDNG 261
AP-SPAP cd16016
SPAP is a subclass of alkaline phosphatase (AP); Alkaline phosphatases are non-specific ...
84-133 1.71e-05

SPAP is a subclass of alkaline phosphatase (AP); 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. Although SPAP is a subclass of alkaline phosphatase, SPAP has many differences from other APs: 1) the catalytic residue is a threonine instead of serine, 2) there is no binding pocket for the third metal ion, and 3) the arginine residue forming bidentate hydrogen bonding is deleted in SPAP. A lysine and an asparagine residue, recruited together for the first time into the active site, bind the substrate phosphoryl group in a manner not observed before in any other AP.


Pssm-ID: 293740 [Multi-domain]  Cd Length: 457  Bit Score: 47.14  E-value: 1.71e-05
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|
gi 15233665  84 LISGGTEAKHGLIPVFPTMTFPNHYSIATGLYPAYHGIIMNKFTDPVTGE 133
Cdd:cd16016  33 LLNEGFVFENAHYNYAPTDTAPGHATIYTGTTPAIHGIIGNDWYDRETGR 82
GPI_EPT_3 cd16023
GPI ethanolamine phosphate transferase 3, PIG-O; Ethanolamine phosphate transferase is ...
198-271 2.09e-04

GPI ethanolamine phosphate transferase 3, PIG-O; Ethanolamine phosphate transferase is involved in glycosylphosphatidylinositol-anchor biosynthesis. It catalyzes the transfer of ethanolamine phosphate to the first alpha-1,4-linked mannose of the glycosylphosphatidylinositol precursor of GPI-anchor. It may act as suppressor of replication stress and chromosome missegregation.


Pssm-ID: 293747  Cd Length: 289  Bit Score: 42.93  E-value: 2.09e-04
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15233665 198 VLSH-FDHLEDEVP-DLLMLYFDEPDQSGHNYGPDDPRVTTAVSRVDKMIGRVIKGLKQREIFdevhvILLGDHGM 271
Cdd:cd16023 146 VLKHlFPELQSEDDwDLLIAHFLGVDHVGHRYGPNHPEMARKLTQMDQFIRDIIERLDDDTLL-----LVFGDHGM 216
GPI_EPT cd16019
GPI ethanolamine phosphate transferase; Ethanolamine phosphate transferase is involved in ...
201-271 4.38e-04

GPI ethanolamine phosphate transferase; Ethanolamine phosphate transferase is involved in glycosylphosphatidylinositol-anchor biosynthesis. It catalyzes the transfer of ethanolamine phosphate to the first alpha-1,4-linked mannose of the glycosylphosphatidylinositol precursor of GPI-anchor. It may act as suppressor of replication stress and chromosome missegregation.


Pssm-ID: 293743 [Multi-domain]  Cd Length: 292  Bit Score: 41.96  E-value: 4.38e-04
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15233665 201 HFDHLEDEVP-----DLLMLYFDEPDQSGHNYG-PDDPRVTTAVSRVDKMIGRVIKGLKQREIFdevhvILLGDHGM 271
Cdd:cd16019 139 HINDNLDENIyydnwDFIILHFLGLDHLGHKHNtTSSPELEKKLDQMDNLIRDIYDRMDNDTLL-----VVVSDHGM 210
sulfatase_like cd16150
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ...
238-270 9.42e-04

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: 293769 [Multi-domain]  Cd Length: 423  Bit Score: 41.45  E-value: 9.42e-04
                        10        20        30
                ....*....|....*....|....*....|...
gi 15233665 238 VSRVDKMIGRVIKGLKQREIFDEVHVILLGDHG 270
Cdd:cd16150 206 VSRLDHQFGRLLEALKETGLYDDTAVFFFSDHG 238
ARS_like cd16145
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ...
204-270 8.94e-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: 293764 [Multi-domain]  Cd Length: 415  Bit Score: 38.34  E-value: 8.94e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233665 204 HLEDEVPDL-LMLYFDEPDQSGHNYGPDDPRVTTA--VSRVDKMIGRVIKGLKQREIFDEVHVILLGDHG 270
Cdd:cd16145 200 HAPLQVPDDgPYKYKPKDPGIYAYLPWPQPEKAYAamVTRLDRDVGRILALLKELGIDENTLVVFTSDNG 269
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

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