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Conserved domains on  [gi|71834482|ref|NP_001025339|]
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ectonucleotide pyrophosphatase/phosphodiesterase family member 1 [Danio rerio]

Protein Classification

nucleotide pyrophosphatase/phosphodiesterase family protein( domain architecture ID 12013799)

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

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 ...
 179-505 5.14e-111

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: 344.02  E-value: 5.14e-111
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71834482   179 LLLVSLDGFRAGYMNAYsALLPAIRKLRECGTSTPYMRPAYPTKTFPNHYTIVTGLYPETHGIVDNKMYDVNRNASFSLK 258
Cdd:pfam01663   1 LLVISLDGFRADYLDRF-ELTPNLAALAKEGVSAPNLTPVFPTLTFPNHYTLVTGLYPGSHGIVGNTFYDPKTGEYLVFV 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71834482   259 VDEKFNPLWYQGEPVWITAMKNHLKTATFFWPGSDVKVHGRY---PDYWIK-YNRNILFEKRIAQIF--QWLHLPE---- 328
Cdd:pfam01663  80 ISDPEDPRWWQGEPIWDTAAKAGVRAAALFWPGSEVDYSTYYgtpPRYLKDdYNNSVPFEDRVDTAVlqTWLDLPFadva 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71834482   329 GERPDFYTLYFEEPDASGHKYGPMSTQVIEALINVDRLIGMLMDGLKERNLHKCVNVVLVSDHGMEEASCKKAAYVSNYL 408
Cdd:pfam01663 160 AERPDLLLVYLEEPDYAGHRYGPDSPEVEDALRRVDRAIGDLLEALDERGLFEDTNVIVVSDHGMTPVSDDKVIFLNDYL 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71834482   409 DNINDITVI-QGPAARVRPR-----HVPEEFFSFDYEGLVKNLSCR--EPNQPMKPYLKEHLPKRLHFAKniRIERAHLY 480
Cdd:pfam01663 240 REKGLLHLVdGGPVVAIYPKarelgHVPPGEVEEVYAELKEKLLGLriQDGEHLAVYLKEEIPGRLHYNP--RIPDLVLV 317

                         330       340
                  ....*....|....*....|....*.
gi 71834482   481 MQPQWQAALKPSEIKYCR-GGFHGSD 505
Cdd:pfam01663 318 ADPGWYITGKDGGDKEAAiHGTHGYD 343
NUC super family cl00089
DNA/RNA non-specific endonuclease; prokaryotic and eukaryotic double- and single-stranded DNA ...
 642-860 1.28e-48

DNA/RNA non-specific endonuclease; prokaryotic and eukaryotic double- and single-stranded DNA and RNA endonucleases also present in phosphodiesterases. They exists as monomers and homodimers.


The actual alignment was detected with superfamily member smart00477:

Pssm-ID: 469610  Cd Length: 210  Bit Score: 171.39  E-value: 1.28e-48
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71834482    642 HSSYISGYSRDILMPLWVSYSLNTTVVLHPsAEW---CVRADVRVQASDRQSCSIYKNnSSMSFGLLHPPNFSPAGTEP- 717
Cdd:smart00477   1 RNQYVLGYNRSTRMPNWVAYHITGELLTSG-AERksdCFKPDTRIPEKFQAKLSDYKG-SGYDRGHLAPAADHKFSSEAm 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71834482    718 -DSLITSNMVPMYPGFK-DIWTHFHNFLLIKFSEEMNGINVVSGPIFDNDFDGNYD--FMNKGVL--NGAPIPTHFFIIL 791
Cdd:smart00477  79 aDTFYLSNIVPQYPDFNrGAWAYLEDYLRKLTASERNGVYVVSGPLFLPNYDGKGDklEVKYQVIgsKNVAIPTHFFKVI 158

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 71834482    792 TSCKNSSlsvrqcegPLDAVSFILPHRPDHLETChngtdyswfqdwVQLHVARIRDIELLTGLSFYHDR 860
Cdd:smart00477 159 TAEKADS--------YLEVAAFILPNDPINDESP------------LTNFRVPVDEIERLTGLDFFRNL 207
Somatomedin_B pfam01033
Somatomedin B domain;
114-154 5.01e-11

Somatomedin B domain;


:

Pssm-ID: 460034  Cd Length: 40  Bit Score: 58.08  E-value: 5.01e-11
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 71834482   114 WTCsKFRCGEDRLPSSLCSCSADCVKVGDCCANYKRTCEGE 154
Cdd:pfam01033   1 ESC-KGRCGESFDRGRLCQCDDDCVKYGDCCPDYESLCLGE 40
Somatomedin_B pfam01033
Somatomedin B domain;
70-108 2.48e-09

Somatomedin B domain;


:

Pssm-ID: 460034  Cd Length: 40  Bit Score: 53.46  E-value: 2.48e-09
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 71834482    70 DSCKNRCISKSHDGNaGCRCDAACVNEGTCCLDYEEVCL 108
Cdd:pfam01033   1 ESCKGRCGESFDRGR-LCQCDDDCVKYGDCCPDYESLCL 38
 
Name Accession Description Interval E-value
Phosphodiest pfam01663
Type I phosphodiesterase / nucleotide pyrophosphatase; This family consists of ...
 179-505 5.14e-111

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: 344.02  E-value: 5.14e-111
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71834482   179 LLLVSLDGFRAGYMNAYsALLPAIRKLRECGTSTPYMRPAYPTKTFPNHYTIVTGLYPETHGIVDNKMYDVNRNASFSLK 258
Cdd:pfam01663   1 LLVISLDGFRADYLDRF-ELTPNLAALAKEGVSAPNLTPVFPTLTFPNHYTLVTGLYPGSHGIVGNTFYDPKTGEYLVFV 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71834482   259 VDEKFNPLWYQGEPVWITAMKNHLKTATFFWPGSDVKVHGRY---PDYWIK-YNRNILFEKRIAQIF--QWLHLPE---- 328
Cdd:pfam01663  80 ISDPEDPRWWQGEPIWDTAAKAGVRAAALFWPGSEVDYSTYYgtpPRYLKDdYNNSVPFEDRVDTAVlqTWLDLPFadva 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71834482   329 GERPDFYTLYFEEPDASGHKYGPMSTQVIEALINVDRLIGMLMDGLKERNLHKCVNVVLVSDHGMEEASCKKAAYVSNYL 408
Cdd:pfam01663 160 AERPDLLLVYLEEPDYAGHRYGPDSPEVEDALRRVDRAIGDLLEALDERGLFEDTNVIVVSDHGMTPVSDDKVIFLNDYL 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71834482   409 DNINDITVI-QGPAARVRPR-----HVPEEFFSFDYEGLVKNLSCR--EPNQPMKPYLKEHLPKRLHFAKniRIERAHLY 480
Cdd:pfam01663 240 REKGLLHLVdGGPVVAIYPKarelgHVPPGEVEEVYAELKEKLLGLriQDGEHLAVYLKEEIPGRLHYNP--RIPDLVLV 317

                         330       340
                  ....*....|....*....|....*.
gi 71834482   481 MQPQWQAALKPSEIKYCR-GGFHGSD 505
Cdd:pfam01663 318 ADPGWYITGKDGGDKEAAiHGTHGYD 343
Enpp cd16018
Ectonucleotide pyrophosphatase/phosphodiesterase, also called autotaxin; Ecto-nucleotide ...
 177-545 2.55e-110

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: 339.18  E-value: 2.55e-110
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71834482 177 SPLLLVSLDGFRAGYMNaYSALLPAIRKLRECGTSTPYMRPAYPTKTFPNHYTIVTGLYPETHGIVDNKMYDVNRNASFS 256
Cdd:cd16018   1 PPLIVISIDGFRWDYLD-RAGLTPNLKRLAEEGVRAKYVKPVFPTLTFPNHYSIVTGLYPESHGIVGNYFYDPKTNEEFS 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71834482 257 lKVDEKFNPLWYQGEPVWITAMKNHLKTATFFWPGSDVKVHGRYPD------YWIKYNRNILFEKRIAQIFQWLHLpegE 330
Cdd:cd16018  80 -DSDWVWDPWWIGGEPIWVTAEKAGLKTASYFWPGSEVAIIGYNPTpiplggYWQPYNDSFPFEERVDTILEWLDL---E 155

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71834482 331 RPDFYTLYFEEPDASGHKYGPMSTQVIEALINVDRLIGMLMDGLKERNLHKCVNVVLVSDHGMEEAsckkaayvsnyldn 410
Cdd:cd16018 156 RPDLILLYFEEPDSAGHKYGPDSPEVNEALKRVDRRLGYLIEALKERGLLDDTNIIVVSDHGMTDV-------------- 221

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71834482 411 inditviqgpaarvrprhvpeeffsfdyeglvknlscrepnqpmkpylkehlpkrlhfaknirierahlymqpqwqaalk 490
Cdd:cd16018     --------------------------------------------------------------------------------

                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|....*
gi 71834482 491 pseikycrgGFHGSDNVFKNMQAIFIGYGPGIHYNTTVPPFENIEVYNLLCDLLG 545
Cdd:cd16018 222 ---------GTHGYDNELPDMRAIFIARGPAFKKGKKLGPFRNVDIYPLMCNLLG 267
AtaC COG1524
c-di-AMP phosphodiesterase AtaC or nucleotide pyrophosphatase, AlkP superfamily [Signal ...
 171-547 2.38e-65

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


Pssm-ID: 441133 [Multi-domain]  Cd Length: 370  Bit Score: 223.47  E-value: 2.38e-65
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71834482 171 PAGFSKSPLLLVSLDGFRAGYMNAYSAllPAIRKLRECGTSTPYMRPAYPTKTFPNHYTIVTGLYPETHGIVDNKMYDVN 250
Cdd:COG1524  18 AAAPPAKKVVLILVDGLRADLLERAHA--PNLAALAARGVYARPLTSVFPSTTAPAHTTLLTGLYPGEHGIVGNGWYDPE 95

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71834482 251 RNASF---SLKVDEKFNPLWYQGEPVWITAMKNHLKTATFFWPGSDVkvhgrypDYWIKYNRNILFEKRIA--------- 318
Cdd:COG1524  96 LGRVVnslSWVEDGFGSNSLLPVPTIFERARAAGLTTAAVFWPSFEG-------SGLIDAARPYPYDGRKPllgnpaadr 168

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71834482 319 -QIFQWLHLPEGERPDFYTLYFEEPDASGHKYGPMSTQVIEALINVDRLIGMLMDGLKERNLHKCVNVVLVSDHGMEEAS 397
Cdd:COG1524 169 wIAAAALELLREGRPDLLLVYLPDLDYAGHRYGPDSPEYRAALREVDAALGRLLDALKARGLYEGTLVIVTADHGMVDVP 248

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71834482 398 ckkAAYVSNYLDNINDITVIQGPAARVRPRHVPEEFFsfdYEGLvknlscrepNQPMKPYLKEHLpKRLHFAKNiRIERA 477
Cdd:COG1524 249 ---PDIDLNRLRLAGLLAVRAGESAHLYLKDGADAEV---RALL---------GLPARVLTREEL-AAGHFGPH-RIGDL 311

                       330       340       350       360       370       380       390
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71834482 478 HLYMQPQWQAALKPseikycrGGFHGSDNvFKNMQAIFIGYGPGIHynttvPPFENIEVYNLLCDLLGIS 547
Cdd:COG1524 312 VLVAKPGWALDAPL-------KGSHGGLP-DEEMRVPLLASGPGFR-----PGVRNVDVAPTIARLLGLP 368
NUC smart00477
DNA/RNA non-specific endonuclease; prokaryotic and eukaryotic double- and single-stranded DNA ...
 642-860 1.28e-48

DNA/RNA non-specific endonuclease; prokaryotic and eukaryotic double- and single-stranded DNA and RNA endonucleases also present in phosphodiesterases


Pssm-ID: 214683  Cd Length: 210  Bit Score: 171.39  E-value: 1.28e-48
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71834482    642 HSSYISGYSRDILMPLWVSYSLNTTVVLHPsAEW---CVRADVRVQASDRQSCSIYKNnSSMSFGLLHPPNFSPAGTEP- 717
Cdd:smart00477   1 RNQYVLGYNRSTRMPNWVAYHITGELLTSG-AERksdCFKPDTRIPEKFQAKLSDYKG-SGYDRGHLAPAADHKFSSEAm 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71834482    718 -DSLITSNMVPMYPGFK-DIWTHFHNFLLIKFSEEMNGINVVSGPIFDNDFDGNYD--FMNKGVL--NGAPIPTHFFIIL 791
Cdd:smart00477  79 aDTFYLSNIVPQYPDFNrGAWAYLEDYLRKLTASERNGVYVVSGPLFLPNYDGKGDklEVKYQVIgsKNVAIPTHFFKVI 158

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 71834482    792 TSCKNSSlsvrqcegPLDAVSFILPHRPDHLETChngtdyswfqdwVQLHVARIRDIELLTGLSFYHDR 860
Cdd:smart00477 159 TAEKADS--------YLEVAAFILPNDPINDESP------------LTNFRVPVDEIERLTGLDFFRNL 207
NUC cd00091
DNA/RNA non-specific endonuclease; prokaryotic and eukaryotic double- and single-stranded DNA ...
 623-871 2.95e-43

DNA/RNA non-specific endonuclease; prokaryotic and eukaryotic double- and single-stranded DNA and RNA endonucleases also present in phosphodiesterases. They exists as monomers and homodimers.


Pssm-ID: 238043  Cd Length: 241  Bit Score: 157.15  E-value: 2.95e-43
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71834482 623 LPFGIPRVLQDQsdyCILHHSSYISGYSRDILMPLWVSYSLNTTVVLHPSAEW--CVRADVRVQASDRQSCSIYKNNSSM 700
Cdd:cd00091   1 LQYGRPGVLADT---EVLSYTHYVLSYNRATRLPLWVAEHIDKEDLGKNVDRKydQFKQDPRIPPLFSATNSDYKGSGSL 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71834482 701 SFGLLHP---PNFSPAgTEPDSLITSNMVPMYPGF-KDIWTHFHNFLLIKFSEEMNGINVVSGPIFDNDFDGNYDFMNKG 776
Cdd:cd00091  78 DRGHLAPaadPVWSQD-AQDATFYLTNMAPQVQGFnQGNWAYLEDYLRDLAASEGKDVYVVTGPLFLPDLDGDGGSYLST 156

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71834482 777 VLNGA---PIPTHFFIILTSCKNSslsvrqceGPLDAVSFILPHRPDHLETCHNGTDYSWFqdwvQLHVARIRDIellTG 853
Cdd:cd00091 157 QVINNgkvAVPTHFWKVIIDEKAP--------GNLSVGAFVLPNNNPHDTLEFILCVEKTF----QVPVASVEKA---TG 221

                       250
                ....*....|....*....
gi 71834482 854 LSFYHDRI-SVAETLQLKT 871
Cdd:cd00091 222 LSFFCNVPdSVSAVLELKK 240
Somatomedin_B pfam01033
Somatomedin B domain;
114-154 5.01e-11

Somatomedin B domain;


Pssm-ID: 460034  Cd Length: 40  Bit Score: 58.08  E-value: 5.01e-11
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 71834482   114 WTCsKFRCGEDRLPSSLCSCSADCVKVGDCCANYKRTCEGE 154
Cdd:pfam01033   1 ESC-KGRCGESFDRGRLCQCDDDCVKYGDCCPDYESLCLGE 40
SO smart00201
Somatomedin B -like domains; Somatomedin-B is a peptide, proteolytically excised from ...
 112-155 1.19e-09

Somatomedin B -like domains; Somatomedin-B is a peptide, proteolytically excised from vitronectin, that is a growth hormone-dependent serum factor with protease-inhibiting activity.


Pssm-ID: 197571  Cd Length: 43  Bit Score: 54.30  E-value: 1.19e-09
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 71834482    112 QLWTCsKFRCGEDRLPSSLCSCSADCVKVGDCCANYKRTCEGEK 155
Cdd:smart00201   1 AIGSC-KGRCGESFNEGNACRCDALCLSYGDCCTDYESVCKKEV 43
Somatomedin_B pfam01033
Somatomedin B domain;
70-108 2.48e-09

Somatomedin B domain;


Pssm-ID: 460034  Cd Length: 40  Bit Score: 53.46  E-value: 2.48e-09
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 71834482    70 DSCKNRCISKSHDGNaGCRCDAACVNEGTCCLDYEEVCL 108
Cdd:pfam01033   1 ESCKGRCGESFDRGR-LCQCDDDCVKYGDCCPDYESLCL 38
SO smart00201
Somatomedin B -like domains; Somatomedin-B is a peptide, proteolytically excised from ...
 69-111 3.19e-09

Somatomedin B -like domains; Somatomedin-B is a peptide, proteolytically excised from vitronectin, that is a growth hormone-dependent serum factor with protease-inhibiting activity.


Pssm-ID: 197571  Cd Length: 43  Bit Score: 53.15  E-value: 3.19e-09
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|...
gi 71834482     69 IDSCKNRCISKSHDGNAgCRCDAACVNEGTCCLDYEEVCLQPT 111
Cdd:smart00201   2 IGSCKGRCGESFNEGNA-CRCDALCLSYGDCCTDYESVCKKEV 43
Endonuclease_NS pfam01223
DNA/RNA non-specific endonuclease;
723-856 1.14e-06

DNA/RNA non-specific endonuclease;


Pssm-ID: 460120  Cd Length: 220  Bit Score: 50.51  E-value: 1.14e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71834482   723 SNMVPMYPGF-KDIWTHFHNFLLiKFSEEMNG-INVVSGPIFDNDFDGNydfmnkgvlNGAPIPTHFFIILTSCKNSSls 800
Cdd:pfam01223 106 TNIAPQWAGFnQGNWAYLENYVR-DLAARHNNsVYVYTGPLYVPNLLDK---------NKVAVPTHFWKVILSEDGDG-- 173

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 71834482   801 vrqcEGPLDAVSFILPHrpdhlETCHNGTDYSWFQdwvqlhvARIRDIELLTGLSF 856
Cdd:pfam01223 174 ----GGGLNAPAFVLPN-----KYILDDGPLRTFQ-------VPVDELERLTGLDF 213
 
Name Accession Description Interval E-value
Phosphodiest pfam01663
Type I phosphodiesterase / nucleotide pyrophosphatase; This family consists of ...
 179-505 5.14e-111

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: 344.02  E-value: 5.14e-111
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71834482   179 LLLVSLDGFRAGYMNAYsALLPAIRKLRECGTSTPYMRPAYPTKTFPNHYTIVTGLYPETHGIVDNKMYDVNRNASFSLK 258
Cdd:pfam01663   1 LLVISLDGFRADYLDRF-ELTPNLAALAKEGVSAPNLTPVFPTLTFPNHYTLVTGLYPGSHGIVGNTFYDPKTGEYLVFV 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71834482   259 VDEKFNPLWYQGEPVWITAMKNHLKTATFFWPGSDVKVHGRY---PDYWIK-YNRNILFEKRIAQIF--QWLHLPE---- 328
Cdd:pfam01663  80 ISDPEDPRWWQGEPIWDTAAKAGVRAAALFWPGSEVDYSTYYgtpPRYLKDdYNNSVPFEDRVDTAVlqTWLDLPFadva 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71834482   329 GERPDFYTLYFEEPDASGHKYGPMSTQVIEALINVDRLIGMLMDGLKERNLHKCVNVVLVSDHGMEEASCKKAAYVSNYL 408
Cdd:pfam01663 160 AERPDLLLVYLEEPDYAGHRYGPDSPEVEDALRRVDRAIGDLLEALDERGLFEDTNVIVVSDHGMTPVSDDKVIFLNDYL 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71834482   409 DNINDITVI-QGPAARVRPR-----HVPEEFFSFDYEGLVKNLSCR--EPNQPMKPYLKEHLPKRLHFAKniRIERAHLY 480
Cdd:pfam01663 240 REKGLLHLVdGGPVVAIYPKarelgHVPPGEVEEVYAELKEKLLGLriQDGEHLAVYLKEEIPGRLHYNP--RIPDLVLV 317

                         330       340
                  ....*....|....*....|....*.
gi 71834482   481 MQPQWQAALKPSEIKYCR-GGFHGSD 505
Cdd:pfam01663 318 ADPGWYITGKDGGDKEAAiHGTHGYD 343
Enpp cd16018
Ectonucleotide pyrophosphatase/phosphodiesterase, also called autotaxin; Ecto-nucleotide ...
 177-545 2.55e-110

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: 339.18  E-value: 2.55e-110
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71834482 177 SPLLLVSLDGFRAGYMNaYSALLPAIRKLRECGTSTPYMRPAYPTKTFPNHYTIVTGLYPETHGIVDNKMYDVNRNASFS 256
Cdd:cd16018   1 PPLIVISIDGFRWDYLD-RAGLTPNLKRLAEEGVRAKYVKPVFPTLTFPNHYSIVTGLYPESHGIVGNYFYDPKTNEEFS 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71834482 257 lKVDEKFNPLWYQGEPVWITAMKNHLKTATFFWPGSDVKVHGRYPD------YWIKYNRNILFEKRIAQIFQWLHLpegE 330
Cdd:cd16018  80 -DSDWVWDPWWIGGEPIWVTAEKAGLKTASYFWPGSEVAIIGYNPTpiplggYWQPYNDSFPFEERVDTILEWLDL---E 155

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71834482 331 RPDFYTLYFEEPDASGHKYGPMSTQVIEALINVDRLIGMLMDGLKERNLHKCVNVVLVSDHGMEEAsckkaayvsnyldn 410
Cdd:cd16018 156 RPDLILLYFEEPDSAGHKYGPDSPEVNEALKRVDRRLGYLIEALKERGLLDDTNIIVVSDHGMTDV-------------- 221

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71834482 411 inditviqgpaarvrprhvpeeffsfdyeglvknlscrepnqpmkpylkehlpkrlhfaknirierahlymqpqwqaalk 490
Cdd:cd16018     --------------------------------------------------------------------------------

                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|....*
gi 71834482 491 pseikycrgGFHGSDNVFKNMQAIFIGYGPGIHYNTTVPPFENIEVYNLLCDLLG 545
Cdd:cd16018 222 ---------GTHGYDNELPDMRAIFIARGPAFKKGKKLGPFRNVDIYPLMCNLLG 267
AtaC COG1524
c-di-AMP phosphodiesterase AtaC or nucleotide pyrophosphatase, AlkP superfamily [Signal ...
 171-547 2.38e-65

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


Pssm-ID: 441133 [Multi-domain]  Cd Length: 370  Bit Score: 223.47  E-value: 2.38e-65
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71834482 171 PAGFSKSPLLLVSLDGFRAGYMNAYSAllPAIRKLRECGTSTPYMRPAYPTKTFPNHYTIVTGLYPETHGIVDNKMYDVN 250
Cdd:COG1524  18 AAAPPAKKVVLILVDGLRADLLERAHA--PNLAALAARGVYARPLTSVFPSTTAPAHTTLLTGLYPGEHGIVGNGWYDPE 95

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71834482 251 RNASF---SLKVDEKFNPLWYQGEPVWITAMKNHLKTATFFWPGSDVkvhgrypDYWIKYNRNILFEKRIA--------- 318
Cdd:COG1524  96 LGRVVnslSWVEDGFGSNSLLPVPTIFERARAAGLTTAAVFWPSFEG-------SGLIDAARPYPYDGRKPllgnpaadr 168

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71834482 319 -QIFQWLHLPEGERPDFYTLYFEEPDASGHKYGPMSTQVIEALINVDRLIGMLMDGLKERNLHKCVNVVLVSDHGMEEAS 397
Cdd:COG1524 169 wIAAAALELLREGRPDLLLVYLPDLDYAGHRYGPDSPEYRAALREVDAALGRLLDALKARGLYEGTLVIVTADHGMVDVP 248

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71834482 398 ckkAAYVSNYLDNINDITVIQGPAARVRPRHVPEEFFsfdYEGLvknlscrepNQPMKPYLKEHLpKRLHFAKNiRIERA 477
Cdd:COG1524 249 ---PDIDLNRLRLAGLLAVRAGESAHLYLKDGADAEV---RALL---------GLPARVLTREEL-AAGHFGPH-RIGDL 311

                       330       340       350       360       370       380       390
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71834482 478 HLYMQPQWQAALKPseikycrGGFHGSDNvFKNMQAIFIGYGPGIHynttvPPFENIEVYNLLCDLLGIS 547
Cdd:COG1524 312 VLVAKPGWALDAPL-------KGSHGGLP-DEEMRVPLLASGPGFR-----PGVRNVDVAPTIARLLGLP 368
NUC smart00477
DNA/RNA non-specific endonuclease; prokaryotic and eukaryotic double- and single-stranded DNA ...
 642-860 1.28e-48

DNA/RNA non-specific endonuclease; prokaryotic and eukaryotic double- and single-stranded DNA and RNA endonucleases also present in phosphodiesterases


Pssm-ID: 214683  Cd Length: 210  Bit Score: 171.39  E-value: 1.28e-48
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71834482    642 HSSYISGYSRDILMPLWVSYSLNTTVVLHPsAEW---CVRADVRVQASDRQSCSIYKNnSSMSFGLLHPPNFSPAGTEP- 717
Cdd:smart00477   1 RNQYVLGYNRSTRMPNWVAYHITGELLTSG-AERksdCFKPDTRIPEKFQAKLSDYKG-SGYDRGHLAPAADHKFSSEAm 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71834482    718 -DSLITSNMVPMYPGFK-DIWTHFHNFLLIKFSEEMNGINVVSGPIFDNDFDGNYD--FMNKGVL--NGAPIPTHFFIIL 791
Cdd:smart00477  79 aDTFYLSNIVPQYPDFNrGAWAYLEDYLRKLTASERNGVYVVSGPLFLPNYDGKGDklEVKYQVIgsKNVAIPTHFFKVI 158

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 71834482    792 TSCKNSSlsvrqcegPLDAVSFILPHRPDHLETChngtdyswfqdwVQLHVARIRDIELLTGLSFYHDR 860
Cdd:smart00477 159 TAEKADS--------YLEVAAFILPNDPINDESP------------LTNFRVPVDEIERLTGLDFFRNL 207
NUC cd00091
DNA/RNA non-specific endonuclease; prokaryotic and eukaryotic double- and single-stranded DNA ...
 623-871 2.95e-43

DNA/RNA non-specific endonuclease; prokaryotic and eukaryotic double- and single-stranded DNA and RNA endonucleases also present in phosphodiesterases. They exists as monomers and homodimers.


Pssm-ID: 238043  Cd Length: 241  Bit Score: 157.15  E-value: 2.95e-43
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71834482 623 LPFGIPRVLQDQsdyCILHHSSYISGYSRDILMPLWVSYSLNTTVVLHPSAEW--CVRADVRVQASDRQSCSIYKNNSSM 700
Cdd:cd00091   1 LQYGRPGVLADT---EVLSYTHYVLSYNRATRLPLWVAEHIDKEDLGKNVDRKydQFKQDPRIPPLFSATNSDYKGSGSL 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71834482 701 SFGLLHP---PNFSPAgTEPDSLITSNMVPMYPGF-KDIWTHFHNFLLIKFSEEMNGINVVSGPIFDNDFDGNYDFMNKG 776
Cdd:cd00091  78 DRGHLAPaadPVWSQD-AQDATFYLTNMAPQVQGFnQGNWAYLEDYLRDLAASEGKDVYVVTGPLFLPDLDGDGGSYLST 156

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71834482 777 VLNGA---PIPTHFFIILTSCKNSslsvrqceGPLDAVSFILPHRPDHLETCHNGTDYSWFqdwvQLHVARIRDIellTG 853
Cdd:cd00091 157 QVINNgkvAVPTHFWKVIIDEKAP--------GNLSVGAFVLPNNNPHDTLEFILCVEKTF----QVPVASVEKA---TG 221

                       250
                ....*....|....*....
gi 71834482 854 LSFYHDRI-SVAETLQLKT 871
Cdd:cd00091 222 LSFFCNVPdSVSAVLELKK 240
ALP_like cd00016
alkaline phosphatases and sulfatases; This family includes alkaline phosphatases and ...
 178-394 1.53e-25

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: 105.97  E-value: 1.53e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71834482 178 PLLLVSLDGFRAGYMNAY---SALLPAIRKLRECGTSTpYMRPAYP-TKTFPNHYTIVTGLYPETHGIVDNKMYDVNRNa 253
Cdd:cd00016   2 HVVLIVLDGLGADDLGKAgnpAPTTPNLKRLASEGATF-NFRSVSPpTSSAPNHAALLTGAYPTLHGYTGNGSADPELP- 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71834482 254 sfslkvdEKFNPLWYQGEPVWITAMKNHLKTATFFwpgsdvkvhgrypdywikynrnilfekrIAQIFQWLHLpegERPD 333
Cdd:cd00016  80 -------SRAAGKDEDGPTIPELLKQAGYRTGVIG----------------------------LLKAIDETSK---EKPF 121

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 71834482 334 FYTLYFEEPDASGHKYGPMSTQVIEALINVDRLIGMLMDGLKERNLHKCVNVVLVSDHGME 394
Cdd:cd00016 122 VLFLHFDGPDGPGHAYGPNTPEYYDAVEEIDERIGKVLDALKKAGDADDTVIIVTADHGGI 182
Endonuclease_NS smart00892
DNA/RNA non-specific endonuclease; A family of bacterial and eukaryotic endonucleases share ...
 642-859 2.60e-22

DNA/RNA non-specific endonuclease; A family of bacterial and eukaryotic endonucleases share the following characteristics: they act on both DNA and RNA, cleave double-stranded and single-stranded nucleic acids and require a divalent ion such as magnesium for their activity. An histidine has been shown to be essential for the activity of the Serratia marcescens nuclease. This residue is located in a conserved region which also contains an aspartic acid residue that could be implicated in the binding of the divalent ion.


Pssm-ID: 214889 [Multi-domain]  Cd Length: 198  Bit Score: 95.55  E-value: 2.60e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71834482    642 HSSYISGYSRDILMPLWVSYSLNTTVVLHPSAE----WCVRADVRVQASDRQSCSIYKNnSSMSFGLLHPPNFSPAGTEP 717
Cdd:smart00892   1 YKHYALCYDERRRLPLWVAYHLTGSTRQGKNTGrkrpWFKPDGWHLPAIFQAVNSDYTG-SGYDRGHLAPAADHGVSQEA 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71834482    718 --DSLITSNMVPMYPGF-KDIWTHFHNFLLIKFSEEMNGINVVSGPIFDNDFDGnydfmnkgvlNGAPIPTHFFIILTSC 794
Cdd:smart00892  80 maATFYLTNIVPQTAGFnQGNWNRLENYVRKLLAKNKDTVYVVTGPIYLPTLPD----------NNVAVPSHFWKVILSE 149

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 71834482    795 KNSSlsvrqceGPLDAVSFILPHRPDhletcHNGTDYSWFQDwvqlhvaRIRDIELLTGLSFYHD 859
Cdd:smart00892 150 DGSN-------GGLAAIAFNLPNAPI-----NEDYPLCEFQV-------PVDNIERLTGLDFFCG 195
Somatomedin_B pfam01033
Somatomedin B domain;
114-154 5.01e-11

Somatomedin B domain;


Pssm-ID: 460034  Cd Length: 40  Bit Score: 58.08  E-value: 5.01e-11
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 71834482   114 WTCsKFRCGEDRLPSSLCSCSADCVKVGDCCANYKRTCEGE 154
Cdd:pfam01033   1 ESC-KGRCGESFDRGRLCQCDDDCVKYGDCCPDYESLCLGE 40
SO smart00201
Somatomedin B -like domains; Somatomedin-B is a peptide, proteolytically excised from ...
 112-155 1.19e-09

Somatomedin B -like domains; Somatomedin-B is a peptide, proteolytically excised from vitronectin, that is a growth hormone-dependent serum factor with protease-inhibiting activity.


Pssm-ID: 197571  Cd Length: 43  Bit Score: 54.30  E-value: 1.19e-09
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 71834482    112 QLWTCsKFRCGEDRLPSSLCSCSADCVKVGDCCANYKRTCEGEK 155
Cdd:smart00201   1 AIGSC-KGRCGESFNEGNACRCDALCLSYGDCCTDYESVCKKEV 43
Somatomedin_B pfam01033
Somatomedin B domain;
70-108 2.48e-09

Somatomedin B domain;


Pssm-ID: 460034  Cd Length: 40  Bit Score: 53.46  E-value: 2.48e-09
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 71834482    70 DSCKNRCISKSHDGNaGCRCDAACVNEGTCCLDYEEVCL 108
Cdd:pfam01033   1 ESCKGRCGESFDRGR-LCQCDDDCVKYGDCCPDYESLCL 38
SO smart00201
Somatomedin B -like domains; Somatomedin-B is a peptide, proteolytically excised from ...
 69-111 3.19e-09

Somatomedin B -like domains; Somatomedin-B is a peptide, proteolytically excised from vitronectin, that is a growth hormone-dependent serum factor with protease-inhibiting activity.


Pssm-ID: 197571  Cd Length: 43  Bit Score: 53.15  E-value: 3.19e-09
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|...
gi 71834482     69 IDSCKNRCISKSHDGNAgCRCDAACVNEGTCCLDYEEVCLQPT 111
Cdd:smart00201   2 IGSCKGRCGESFNEGNA-CRCDALCLSYGDCCTDYESVCKKEV 43
Sulfatase pfam00884
Sulfatase;
179-392 3.62e-08

Sulfatase;


Pssm-ID: 459979 [Multi-domain]  Cd Length: 298  Bit Score: 55.89  E-value: 3.62e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71834482   179 LLLVSLDGFRAGYMNAYSALLPAIRKLRecgtstpymRPAYPTKTFPNHYT-----------IVTGLYPETHGIVDN--- 244
Cdd:pfam00884   3 VVLVLGESLRAPDLGLYGYPRPTTPFLD---------RLAEEGLLFSNFYSggtltapsrfaLLTGLPPHNFGSYVStpv 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71834482   245 -KMYDVN------RNASFSLKVDEKFNPLWYqgepvWITAMKNH-LKTATFFWPGSDVKVHGRYPDYWIKYNR---NILF 313
Cdd:pfam00884  74 gLPRTEPslpdllKRAGYNTGAIGKWHLGWY-----NNQSPCNLgFDKFFGRNTGSDLYADPPDVPYNCSGGGvsdEALL 148

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71834482   314 EKRIAQI-------FQWLHLPEGERPDFYTLYFEEPDASGHKYGPMSTQVIE----ALINVDRLIGMLMDGLKERNLHKC 382
Cdd:pfam00884 149 DEALEFLdnndkpfFLVLHTLGSHGPPYYPDRYPEKYATFKPSSCSEEQLLNsydnTLLYTDDAIGRVLDKLEENGLLDN 228

                         250
                  ....*....|
gi 71834482   383 VNVVLVSDHG 392
Cdd:pfam00884 229 TLVVYTSDHG 238
Endonuclease_NS pfam01223
DNA/RNA non-specific endonuclease;
723-856 1.14e-06

DNA/RNA non-specific endonuclease;


Pssm-ID: 460120  Cd Length: 220  Bit Score: 50.51  E-value: 1.14e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71834482   723 SNMVPMYPGF-KDIWTHFHNFLLiKFSEEMNG-INVVSGPIFDNDFDGNydfmnkgvlNGAPIPTHFFIILTSCKNSSls 800
Cdd:pfam01223 106 TNIAPQWAGFnQGNWAYLENYVR-DLAARHNNsVYVYTGPLYVPNLLDK---------NKVAVPTHFWKVILSEDGDG-- 173

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 71834482   801 vrqcEGPLDAVSFILPHrpdhlETCHNGTDYSWFQdwvqlhvARIRDIELLTGLSF 856
Cdd:pfam01223 174 ----GGGLNAPAFVLPN-----KYILDDGPLRTFQ-------VPVDELERLTGLDF 213
AP-SPAP cd16016
SPAP is a subclass of alkaline phosphatase (AP); Alkaline phosphatases are non-specific ...
 178-408 1.35e-06

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: 51.76  E-value: 1.35e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71834482 178 PLLLV--SLDGFRAGYMNAYSALLPA---IRKLREcGTSTPYMRPAY-PTKTFPNHYTIVTGLYPETHGIVDNKMYDVNR 251
Cdd:cd16016   2 PKLVVgiVVDQMRADYLYRYRDRFGEggfKRLLNE-GFVFENAHYNYaPTDTAPGHATIYTGTTPAIHGIIGNDWYDRET 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71834482 252 NASFSLKVDEKFNPL--WYQGEPV-----WITAMKNHLKTATFFwpgsDVKVH-------------GRYPD--YWI---- 305
Cdd:cd16016  81 GREVYCVEDSTVTTVggNSTAGKMsprnlLVTTIGDELKLATNG----RSKVIgvalkdraailpaGHAADaaYWFddet 156

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71834482 306 ------------------KYNRNIL-----FEKRIA-QIFQWLHLPEGERPDFYTLYFEEPDASGHKYGPMSTQVIEALI 361
Cdd:cd16016 157 gkfitstyymkelpawveKFNAKKLpfgntLTLDFAkAALENEKLGKDDVTDLLAVSFSATDYIGHAFGPNSVEMEDTYL 236

                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*..
gi 71834482 362 NVDRLIGMLMDGLKERNLHKCVNVVLVSDHGmeeasckkAAYVSNYL 408
Cdd:cd16016 237 RLDRDLARLLDALDKKVGKGNYLVFLTADHG--------AADNPEFL 275
COG3379 COG3379
Predicted phosphohydrolase or phosphomutase, AlkP superfamily [General function prediction ...
 199-393 4.79e-05

Predicted phosphohydrolase or phosphomutase, AlkP superfamily [General function prediction only];


Pssm-ID: 442606 [Multi-domain]  Cd Length: 472  Bit Score: 46.82  E-value: 4.79e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71834482 199 LPAIRKLRECGTSTPyMRPAYPTKTFPNHYTIVTGLYPETHGIvdnkmYD-VNRNA-SFSLKVdekFNPLWYQGEPVW-- 274
Cdd:COG3379  29 LPNLARLAEEGAYGR-LRSTIPPITPPAWTSMMTGRNPGEHGV-----YGfRDREPgSYDTRV---ANSRDVRAPTLWdi 99

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71834482 275 -------ITAMkN----------------------HLKTATffWPGS--------------DV--KVHGRYPDYWIKYNR 309
Cdd:COG3379 100 lsragkrVTVL-NvpvtypprpvngvmvsgfltpdLLGDAT--YPPEladelealvgdyriDVnaKLRPDDKEELLEDLY 176

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71834482 310 NiLFEKRiAQIFqwLHLPEGERPDFYTLYFEEPDASGH---KY-----------GPMSTQVIEALINVDRLIGMLMDGLK 375
Cdd:COG3379 177 E-TLEKR-FEAA--RHLLEEDDWDLFMVVFMGTDRVQHflwHYydpdhplydpdGPYRDAILDYYRALDRYIGELLELAG 252

                       250
                ....*....|....*...
gi 71834482 376 ERnlhkcVNVVLVSDHGM 393
Cdd:COG3379 253 DD-----TTVVVVSDHGF 265
GPI_EPT cd16019
GPI ethanolamine phosphate transferase; Ethanolamine phosphate transferase is involved in ...
 175-393 1.97e-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: 44.27  E-value: 1.97e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71834482 175 SKSPLLLVSLDGFRAGYM---NAYSALLPAIRKLRECGTSTPYMRP--AYPTKTFPNHYTIVTGLYPETHGIVDNKmydv 249
Cdd:cd16019   3 KYDKVVLIVIDGLRYDLAvnvNKQSSFFSFLQKLNEQPNNSFLALSfaDPPTVTGPRLKALTTGNPPTFLDLISNF---- 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71834482 250 nrnASFSLKVDEkfnplwyqgepvWITAMKNHLKTATFFwpgSDVKVHGRYPDYWIKYNRNILFEKR---------IAQI 320
Cdd:cd16019  79 ---ASSEIKEDN------------IIRQLKKNGKKILFY---GDDTWLDLFPEIFTYKFTITSFNIRdmhdvdpifYNHI 140

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 71834482 321 FQWL-HLPEGERPDFYTLYFEEPDASGHKYGPMSTQVIE-ALINVDRLIGMLMDGLKERNLhkcvnVVLVSDHGM 393
Cdd:cd16019 141 NDNLdENIYYDNWDFIILHFLGLDHLGHKHNTTSSPELEkKLDQMDNLIRDIYDRMDNDTL-----LVVVSDHGM 210
 
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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