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Conserved domains on  [gi|1907110803|ref|XP_036015143|]
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ectonucleotide pyrophosphatase/phosphodiesterase family member 2 isoform X11 [Mus musculus]

Protein Classification

nucleotide pyrophosphatase/phosphodiesterase family protein( domain architecture ID 12193408)

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 ...
227-591 7.80e-101

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: 318.21  E-value: 7.80e-101
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907110803 227 LIIFSVDGFRASYMKKGsKVMPNIEKLRSCGTHAPYMRPVYPTKTFPNLYTLATGLYPESHGIVGNSMYDPVFDATFHLR 306
Cdd:pfam01663   1 LLVISLDGFRADYLDRF-ELTPNLAALAKEGVSAPNLTPVFPTLTFPNHYTLVTGLYPGSHGIVGNTFYDPKTGEYLVFV 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907110803 307 GREKFNHRWWGGQPLWITATKQGVRAGTFFW----------------------SVSIPHERRILTIL--QWLSLPD---- 358
Cdd:pfam01663  80 ISDPEDPRWWQGEPIWDTAAKAGVRAAALFWpgsevdystyygtpprylkddyNNSVPFEDRVDTAVlqTWLDLPFadva 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907110803 359 NERPSVYAFYSEQPDFSGHKYGPFGPEessygspltpakrpkrkvapkrrqerpvappkkrrrklhrmdhytaetrqdkM 438
Cdd:pfam01663 160 AERPDLLLVYLEEPDYAGHRYGPDSPE----------------------------------------------------V 187
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907110803 439 TNPLREIDKTVGQLMDGLKQLKLHRCVNVIFVGDHGMEDVTCDRTEFLSNYLTNVDDITLV-PGTLGRIRPKI------- 510
Cdd:pfam01663 188 EDALRRVDRAIGDLLEALDERGLFEDTNVIVVSDHGMTPVSDDKVIFLNDYLREKGLLHLVdGGPVVAIYPKArelghvp 267
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907110803 511 PNNLKYDPKAIIANLTC--KKPDQHFKPYMKQHLPKRLHYanNRRIEDLHLLVERRWHVARKpldvyKKPSGKCFFQGDH 588
Cdd:pfam01663 268 PGEVEEVYAELKEKLLGlrIQDGEHLAVYLKEEIPGRLHY--NPRIPDLVLVADPGWYITGK-----DGGDKEAAIHGTH 340

                  ...
gi 1907110803 589 GFD 591
Cdd:pfam01663 341 GYD 343
NUC super family cl00089
DNA/RNA non-specific endonuclease; prokaryotic and eukaryotic double- and single-stranded DNA ...
753-851 3.76e-29

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: 115.54  E-value: 3.76e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907110803  753 HTDFESGYSEIFLMPLWTSYTISKQAEVSSiPEHLTNCVRPDVRVSPGFSQNCLAYKNDKqMSYGFLFPPYL-SSSPEAK 831
Cdd:smart00477   1 RNQYVLGYNRSTRMPNWVAYHITGELLTSG-AERKSDCFKPDTRIPEKFQAKLSDYKGSG-YDRGHLAPAADhKFSSEAM 78
                           90       100
                   ....*....|....*....|.
gi 1907110803  832 YDAFLVTNMVPMYPAFKR-MW 851
Cdd:smart00477  79 ADTFYLSNIVPQYPDFNRgAW 99
SO smart00201
Somatomedin B -like domains; Somatomedin-B is a peptide, proteolytically excised from ...
118-159 6.07e-15

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: 69.32  E-value: 6.07e-15
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|..
gi 1907110803  118 GSCKGRCFELQEVGPPdCRCDNLCKSYSSCCHDFDELCLKTA 159
Cdd:smart00201   3 GSCKGRCGESFNEGNA-CRCDALCLSYGDCCTDYESVCKKEV 43
SO smart00201
Somatomedin B -like domains; Somatomedin-B is a peptide, proteolytically excised from ...
160-203 7.24e-15

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: 69.32  E-value: 7.24e-15
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 1907110803  160 RGWECtKDRCGEVRNEENACHCSEDCLSRGDCCTNYQVVCKGES 203
Cdd:smart00201   1 AIGSC-KGRCGESFNEGNACRCDALCLSYGDCCTDYESVCKKEV 43
AslA super family cl34556
Arylsulfatase A or related enzyme, AlkP superfamily [Inorganic ion transport and metabolism];
391-474 1.77e-03

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


The actual alignment was detected with superfamily member COG3119:

Pssm-ID: 442353 [Multi-domain]  Cd Length: 393  Bit Score: 41.79  E-value: 1.77e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907110803 391 SPLTPAKRPKRKVAPKRRQERPVAPPKKRRRKLHR--MDHYTAEtrqdkmtnpLREIDKTVGQLMDGLKQLKLHRcvN-- 466
Cdd:COG3119   162 APYQAPEEYLDKYDGKDIPLPPNLAPRDLTEEELRraRAAYAAM---------IEEVDDQVGRLLDALEELGLAD--Nti 230

                  ....*...
gi 1907110803 467 VIFVGDHG 474
Cdd:COG3119   231 VVFTSDNG 238
 
Name Accession Description Interval E-value
Phosphodiest pfam01663
Type I phosphodiesterase / nucleotide pyrophosphatase; This family consists of ...
227-591 7.80e-101

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: 318.21  E-value: 7.80e-101
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907110803 227 LIIFSVDGFRASYMKKGsKVMPNIEKLRSCGTHAPYMRPVYPTKTFPNLYTLATGLYPESHGIVGNSMYDPVFDATFHLR 306
Cdd:pfam01663   1 LLVISLDGFRADYLDRF-ELTPNLAALAKEGVSAPNLTPVFPTLTFPNHYTLVTGLYPGSHGIVGNTFYDPKTGEYLVFV 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907110803 307 GREKFNHRWWGGQPLWITATKQGVRAGTFFW----------------------SVSIPHERRILTIL--QWLSLPD---- 358
Cdd:pfam01663  80 ISDPEDPRWWQGEPIWDTAAKAGVRAAALFWpgsevdystyygtpprylkddyNNSVPFEDRVDTAVlqTWLDLPFadva 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907110803 359 NERPSVYAFYSEQPDFSGHKYGPFGPEessygspltpakrpkrkvapkrrqerpvappkkrrrklhrmdhytaetrqdkM 438
Cdd:pfam01663 160 AERPDLLLVYLEEPDYAGHRYGPDSPE----------------------------------------------------V 187
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907110803 439 TNPLREIDKTVGQLMDGLKQLKLHRCVNVIFVGDHGMEDVTCDRTEFLSNYLTNVDDITLV-PGTLGRIRPKI------- 510
Cdd:pfam01663 188 EDALRRVDRAIGDLLEALDERGLFEDTNVIVVSDHGMTPVSDDKVIFLNDYLREKGLLHLVdGGPVVAIYPKArelghvp 267
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907110803 511 PNNLKYDPKAIIANLTC--KKPDQHFKPYMKQHLPKRLHYanNRRIEDLHLLVERRWHVARKpldvyKKPSGKCFFQGDH 588
Cdd:pfam01663 268 PGEVEEVYAELKEKLLGlrIQDGEHLAVYLKEEIPGRLHY--NPRIPDLVLVADPGWYITGK-----DGGDKEAAIHGTH 340

                  ...
gi 1907110803 589 GFD 591
Cdd:pfam01663 341 GYD 343
Enpp cd16018
Ectonucleotide pyrophosphatase/phosphodiesterase, also called autotaxin; Ecto-nucleotide ...
225-631 7.05e-90

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: 286.02  E-value: 7.05e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907110803 225 PPLIIFSVDGFRASYMKKGsKVMPNIEKLRSCGTHAPYMRPVYPTKTFPNLYTLATGLYPESHGIVGNSMYDPVFDATFH 304
Cdd:cd16018     1 PPLIVISIDGFRWDYLDRA-GLTPNLKRLAEEGVRAKYVKPVFPTLTFPNHYSIVTGLYPESHGIVGNYFYDPKTNEEFS 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907110803 305 lRGREKFNHRWWGGQPLWITATKQGVRAGTFFWSVS------------------------IPHERRILTILQWLslpDNE 360
Cdd:cd16018    80 -DSDWVWDPWWIGGEPIWVTAEKAGLKTASYFWPGSevaiigynptpiplggywqpyndsFPFEERVDTILEWL---DLE 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907110803 361 RPSVYAFYSEQPDFSGHKYGPFGPEessygspltpakrpkrkvapkrrqerpvappkkrrrklhrmdhytaetrqdkMTN 440
Cdd:cd16018   156 RPDLILLYFEEPDSAGHKYGPDSPE----------------------------------------------------VNE 183
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907110803 441 PLREIDKTVGQLMDGLKQLKLHRCVNVIFVGDHGMEDVtcdrteflsnyltnvdditlvpgtlgrirpkipnnlkydpka 520
Cdd:cd16018   184 ALKRVDRRLGYLIEALKERGLLDDTNIIVVSDHGMTDV------------------------------------------ 221
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907110803 521 iianltckkpdqhfkpymkqhlpkrlhyannrriedlhllverrwhvarkpldvykkpsgkcffqGDHGFDNKVNSMQTV 600
Cdd:cd16018   222 -----------------------------------------------------------------GTHGYDNELPDMRAI 236
                         410       420       430
                  ....*....|....*....|....*....|.
gi 1907110803 601 FVGYGPTFKYRTKVPPFENIELYNVMCDLLG 631
Cdd:cd16018   237 FIARGPAFKKGKKLGPFRNVDIYPLMCNLLG 267
AtaC COG1524
c-di-AMP phosphodiesterase AtaC or nucleotide pyrophosphatase, AlkP superfamily [Signal ...
224-633 9.63e-55

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


Pssm-ID: 441133 [Multi-domain]  Cd Length: 370  Bit Score: 194.20  E-value: 9.63e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907110803 224 RPPLIIFSVDGFRASYMKKGSkvMPNIEKLRSCGTHAPYMRPVYPTKTFPNLYTLATGLYPESHGIVGNSMYDPVFDAT- 302
Cdd:COG1524    23 AKKVVLILVDGLRADLLERAH--APNLAALAARGVYARPLTSVFPSTTAPAHTTLLTGLYPGEHGIVGNGWYDPELGRVv 100
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907110803 303 FHLRGREKFNH--RWWGGQPLWITATKQGVRAGTFFWSVS---------IPH------------ERRILTILQWLSLPDN 359
Cdd:COG1524   101 NSLSWVEDGFGsnSLLPVPTIFERARAAGLTTAAVFWPSFegsglidaaRPYpydgrkpllgnpAADRWIAAAALELLRE 180
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907110803 360 ERPSVYAFYSEQPDFSGHKYGPFGPEessygspltpakrpkrkvapkrrqerpvappkkrrrklhrmdhYTAEtrqdkmt 439
Cdd:COG1524   181 GRPDLLLVYLPDLDYAGHRYGPDSPE-------------------------------------------YRAA------- 210
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907110803 440 npLREIDKTVGQLMDGLKQLKLHRCVNVIFVGDHGMEDVTcdrTEFLSNYLTNVDDITLVPGTLGRIRPKIPnnlkyDPK 519
Cdd:COG1524   211 --LREVDAALGRLLDALKARGLYEGTLVIVTADHGMVDVP---PDIDLNRLRLAGLLAVRAGESAHLYLKDG-----ADA 280
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907110803 520 AIIANLtckkpDQHFKPYMKQHLpKRLHYANNrRIEDLHLLVERRWHVARKPLdvykkpsgkcffqGDHGFDNKvNSMQT 599
Cdd:COG1524   281 EVRALL-----GLPARVLTREEL-AAGHFGPH-RIGDLVLVAKPGWALDAPLK-------------GSHGGLPD-EEMRV 339
                         410       420       430
                  ....*....|....*....|....*....|....
gi 1907110803 600 VFVGYGPTFKyrtkvPPFENIELYNVMCDLLGLK 633
Cdd:COG1524   340 PLLASGPGFR-----PGVRNVDVAPTIARLLGLP 368
NUC smart00477
DNA/RNA non-specific endonuclease; prokaryotic and eukaryotic double- and single-stranded DNA ...
753-851 3.76e-29

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: 115.54  E-value: 3.76e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907110803  753 HTDFESGYSEIFLMPLWTSYTISKQAEVSSiPEHLTNCVRPDVRVSPGFSQNCLAYKNDKqMSYGFLFPPYL-SSSPEAK 831
Cdd:smart00477   1 RNQYVLGYNRSTRMPNWVAYHITGELLTSG-AERKSDCFKPDTRIPEKFQAKLSDYKGSG-YDRGHLAPAADhKFSSEAM 78
                           90       100
                   ....*....|....*....|.
gi 1907110803  832 YDAFLVTNMVPMYPAFKR-MW 851
Cdd:smart00477  79 ADTFYLSNIVPQYPDFNRgAW 99
NUC cd00091
DNA/RNA non-specific endonuclease; prokaryotic and eukaryotic double- and single-stranded DNA ...
735-851 1.34e-28

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: 115.16  E-value: 1.34e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907110803 735 LLYGRPAVLYRTsyDILYHTDFESGYSEIFLMPLWTSYTISKQAEvSSIPEHLTNCVRPDVRVSPGFSQNCLAYKNDKQM 814
Cdd:cd00091     1 LQYGRPGVLADT--EVLSYTHYVLSYNRATRLPLWVAEHIDKEDL-GKNVDRKYDQFKQDPRIPPLFSATNSDYKGSGSL 77
                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1907110803 815 SYGFLFPPYLSS-SPEAKYDAFLVTNMVPMYPAF-KRMW 851
Cdd:cd00091    78 DRGHLAPAADPVwSQDAQDATFYLTNMAPQVQGFnQGNW 116
SO smart00201
Somatomedin B -like domains; Somatomedin-B is a peptide, proteolytically excised from ...
118-159 6.07e-15

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: 69.32  E-value: 6.07e-15
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|..
gi 1907110803  118 GSCKGRCFELQEVGPPdCRCDNLCKSYSSCCHDFDELCLKTA 159
Cdd:smart00201   3 GSCKGRCGESFNEGNA-CRCDALCLSYGDCCTDYESVCKKEV 43
SO smart00201
Somatomedin B -like domains; Somatomedin-B is a peptide, proteolytically excised from ...
160-203 7.24e-15

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: 69.32  E-value: 7.24e-15
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 1907110803  160 RGWECtKDRCGEVRNEENACHCSEDCLSRGDCCTNYQVVCKGES 203
Cdd:smart00201   1 AIGSC-KGRCGESFNEGNACRCDALCLSYGDCCTDYESVCKKEV 43
Somatomedin_B pfam01033
Somatomedin B domain;
162-202 8.84e-13

Somatomedin B domain;


Pssm-ID: 460034  Cd Length: 40  Bit Score: 63.09  E-value: 8.84e-13
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 1907110803 162 WECtKDRCGEVRNEENACHCSEDCLSRGDCCTNYQVVCKGE 202
Cdd:pfam01033   1 ESC-KGRCGESFDRGRLCQCDDDCVKYGDCCPDYESLCLGE 40
Somatomedin_B pfam01033
Somatomedin B domain;
118-158 6.24e-12

Somatomedin B domain;


Pssm-ID: 460034  Cd Length: 40  Bit Score: 60.78  E-value: 6.24e-12
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 1907110803 118 GSCKGRCFELQEVGPPdCRCDNLCKSYSSCCHDFDELCLKT 158
Cdd:pfam01033   1 ESCKGRCGESFDRGRL-CQCDDDCVKYGDCCPDYESLCLGE 40
AslA COG3119
Arylsulfatase A or related enzyme, AlkP superfamily [Inorganic ion transport and metabolism];
391-474 1.77e-03

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


Pssm-ID: 442353 [Multi-domain]  Cd Length: 393  Bit Score: 41.79  E-value: 1.77e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907110803 391 SPLTPAKRPKRKVAPKRRQERPVAPPKKRRRKLHR--MDHYTAEtrqdkmtnpLREIDKTVGQLMDGLKQLKLHRcvN-- 466
Cdd:COG3119   162 APYQAPEEYLDKYDGKDIPLPPNLAPRDLTEEELRraRAAYAAM---------IEEVDDQVGRLLDALEELGLAD--Nti 230

                  ....*...
gi 1907110803 467 VIFVGDHG 474
Cdd:COG3119   231 VVFTSDNG 238
 
Name Accession Description Interval E-value
Phosphodiest pfam01663
Type I phosphodiesterase / nucleotide pyrophosphatase; This family consists of ...
227-591 7.80e-101

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: 318.21  E-value: 7.80e-101
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907110803 227 LIIFSVDGFRASYMKKGsKVMPNIEKLRSCGTHAPYMRPVYPTKTFPNLYTLATGLYPESHGIVGNSMYDPVFDATFHLR 306
Cdd:pfam01663   1 LLVISLDGFRADYLDRF-ELTPNLAALAKEGVSAPNLTPVFPTLTFPNHYTLVTGLYPGSHGIVGNTFYDPKTGEYLVFV 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907110803 307 GREKFNHRWWGGQPLWITATKQGVRAGTFFW----------------------SVSIPHERRILTIL--QWLSLPD---- 358
Cdd:pfam01663  80 ISDPEDPRWWQGEPIWDTAAKAGVRAAALFWpgsevdystyygtpprylkddyNNSVPFEDRVDTAVlqTWLDLPFadva 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907110803 359 NERPSVYAFYSEQPDFSGHKYGPFGPEessygspltpakrpkrkvapkrrqerpvappkkrrrklhrmdhytaetrqdkM 438
Cdd:pfam01663 160 AERPDLLLVYLEEPDYAGHRYGPDSPE----------------------------------------------------V 187
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907110803 439 TNPLREIDKTVGQLMDGLKQLKLHRCVNVIFVGDHGMEDVTCDRTEFLSNYLTNVDDITLV-PGTLGRIRPKI------- 510
Cdd:pfam01663 188 EDALRRVDRAIGDLLEALDERGLFEDTNVIVVSDHGMTPVSDDKVIFLNDYLREKGLLHLVdGGPVVAIYPKArelghvp 267
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907110803 511 PNNLKYDPKAIIANLTC--KKPDQHFKPYMKQHLPKRLHYanNRRIEDLHLLVERRWHVARKpldvyKKPSGKCFFQGDH 588
Cdd:pfam01663 268 PGEVEEVYAELKEKLLGlrIQDGEHLAVYLKEEIPGRLHY--NPRIPDLVLVADPGWYITGK-----DGGDKEAAIHGTH 340

                  ...
gi 1907110803 589 GFD 591
Cdd:pfam01663 341 GYD 343
Enpp cd16018
Ectonucleotide pyrophosphatase/phosphodiesterase, also called autotaxin; Ecto-nucleotide ...
225-631 7.05e-90

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: 286.02  E-value: 7.05e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907110803 225 PPLIIFSVDGFRASYMKKGsKVMPNIEKLRSCGTHAPYMRPVYPTKTFPNLYTLATGLYPESHGIVGNSMYDPVFDATFH 304
Cdd:cd16018     1 PPLIVISIDGFRWDYLDRA-GLTPNLKRLAEEGVRAKYVKPVFPTLTFPNHYSIVTGLYPESHGIVGNYFYDPKTNEEFS 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907110803 305 lRGREKFNHRWWGGQPLWITATKQGVRAGTFFWSVS------------------------IPHERRILTILQWLslpDNE 360
Cdd:cd16018    80 -DSDWVWDPWWIGGEPIWVTAEKAGLKTASYFWPGSevaiigynptpiplggywqpyndsFPFEERVDTILEWL---DLE 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907110803 361 RPSVYAFYSEQPDFSGHKYGPFGPEessygspltpakrpkrkvapkrrqerpvappkkrrrklhrmdhytaetrqdkMTN 440
Cdd:cd16018   156 RPDLILLYFEEPDSAGHKYGPDSPE----------------------------------------------------VNE 183
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907110803 441 PLREIDKTVGQLMDGLKQLKLHRCVNVIFVGDHGMEDVtcdrteflsnyltnvdditlvpgtlgrirpkipnnlkydpka 520
Cdd:cd16018   184 ALKRVDRRLGYLIEALKERGLLDDTNIIVVSDHGMTDV------------------------------------------ 221
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907110803 521 iianltckkpdqhfkpymkqhlpkrlhyannrriedlhllverrwhvarkpldvykkpsgkcffqGDHGFDNKVNSMQTV 600
Cdd:cd16018   222 -----------------------------------------------------------------GTHGYDNELPDMRAI 236
                         410       420       430
                  ....*....|....*....|....*....|.
gi 1907110803 601 FVGYGPTFKYRTKVPPFENIELYNVMCDLLG 631
Cdd:cd16018   237 FIARGPAFKKGKKLGPFRNVDIYPLMCNLLG 267
AtaC COG1524
c-di-AMP phosphodiesterase AtaC or nucleotide pyrophosphatase, AlkP superfamily [Signal ...
224-633 9.63e-55

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


Pssm-ID: 441133 [Multi-domain]  Cd Length: 370  Bit Score: 194.20  E-value: 9.63e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907110803 224 RPPLIIFSVDGFRASYMKKGSkvMPNIEKLRSCGTHAPYMRPVYPTKTFPNLYTLATGLYPESHGIVGNSMYDPVFDAT- 302
Cdd:COG1524    23 AKKVVLILVDGLRADLLERAH--APNLAALAARGVYARPLTSVFPSTTAPAHTTLLTGLYPGEHGIVGNGWYDPELGRVv 100
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907110803 303 FHLRGREKFNH--RWWGGQPLWITATKQGVRAGTFFWSVS---------IPH------------ERRILTILQWLSLPDN 359
Cdd:COG1524   101 NSLSWVEDGFGsnSLLPVPTIFERARAAGLTTAAVFWPSFegsglidaaRPYpydgrkpllgnpAADRWIAAAALELLRE 180
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907110803 360 ERPSVYAFYSEQPDFSGHKYGPFGPEessygspltpakrpkrkvapkrrqerpvappkkrrrklhrmdhYTAEtrqdkmt 439
Cdd:COG1524   181 GRPDLLLVYLPDLDYAGHRYGPDSPE-------------------------------------------YRAA------- 210
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907110803 440 npLREIDKTVGQLMDGLKQLKLHRCVNVIFVGDHGMEDVTcdrTEFLSNYLTNVDDITLVPGTLGRIRPKIPnnlkyDPK 519
Cdd:COG1524   211 --LREVDAALGRLLDALKARGLYEGTLVIVTADHGMVDVP---PDIDLNRLRLAGLLAVRAGESAHLYLKDG-----ADA 280
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907110803 520 AIIANLtckkpDQHFKPYMKQHLpKRLHYANNrRIEDLHLLVERRWHVARKPLdvykkpsgkcffqGDHGFDNKvNSMQT 599
Cdd:COG1524   281 EVRALL-----GLPARVLTREEL-AAGHFGPH-RIGDLVLVAKPGWALDAPLK-------------GSHGGLPD-EEMRV 339
                         410       420       430
                  ....*....|....*....|....*....|....
gi 1907110803 600 VFVGYGPTFKyrtkvPPFENIELYNVMCDLLGLK 633
Cdd:COG1524   340 PLLASGPGFR-----PGVRNVDVAPTIARLLGLP 368
ALP_like cd00016
alkaline phosphatases and sulfatases; This family includes alkaline phosphatases and ...
225-500 5.54e-39

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: 144.87  E-value: 5.54e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907110803 225 PPLIIFSVDGFRASYMKKGSKVM---PNIEKLRSCGTHApYMRPVYP-TKTFPNLYTLATGLYPESHGIVGNSMYDPvfd 300
Cdd:cd00016     1 KHVVLIVLDGLGADDLGKAGNPApttPNLKRLASEGATF-NFRSVSPpTSSAPNHAALLTGAYPTLHGYTGNGSADP--- 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907110803 301 atfhlRGREKFNHRWWGGQPLWITATKQGVRAGTFFwsvsipherrILTILQWLSlpdNERPSVYAFYSEQPDFSGHKYG 380
Cdd:cd00016    77 -----ELPSRAAGKDEDGPTIPELLKQAGYRTGVIG----------LLKAIDETS---KEKPFVLFLHFDGPDGPGHAYG 138
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907110803 381 PFGPEessygspltpakrpkrkvapkrrqerpvappkkrrrklhrmdhytaetrqdkMTNPLREIDKTVGQLMDGLKQLK 460
Cdd:cd00016   139 PNTPE----------------------------------------------------YYDAVEEIDERIGKVLDALKKAG 166
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 1907110803 461 LHRCVNVIFVGDHGMEDVTCDRTEFLSNYLTNVDDITLVP 500
Cdd:cd00016   167 DADDTVIIVTADHGGIDKGHGGDPKADGKADKSHTGMRVP 206
NUC smart00477
DNA/RNA non-specific endonuclease; prokaryotic and eukaryotic double- and single-stranded DNA ...
753-851 3.76e-29

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: 115.54  E-value: 3.76e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907110803  753 HTDFESGYSEIFLMPLWTSYTISKQAEVSSiPEHLTNCVRPDVRVSPGFSQNCLAYKNDKqMSYGFLFPPYL-SSSPEAK 831
Cdd:smart00477   1 RNQYVLGYNRSTRMPNWVAYHITGELLTSG-AERKSDCFKPDTRIPEKFQAKLSDYKGSG-YDRGHLAPAADhKFSSEAM 78
                           90       100
                   ....*....|....*....|.
gi 1907110803  832 YDAFLVTNMVPMYPAFKR-MW 851
Cdd:smart00477  79 ADTFYLSNIVPQYPDFNRgAW 99
NUC cd00091
DNA/RNA non-specific endonuclease; prokaryotic and eukaryotic double- and single-stranded DNA ...
735-851 1.34e-28

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: 115.16  E-value: 1.34e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907110803 735 LLYGRPAVLYRTsyDILYHTDFESGYSEIFLMPLWTSYTISKQAEvSSIPEHLTNCVRPDVRVSPGFSQNCLAYKNDKQM 814
Cdd:cd00091     1 LQYGRPGVLADT--EVLSYTHYVLSYNRATRLPLWVAEHIDKEDL-GKNVDRKYDQFKQDPRIPPLFSATNSDYKGSGSL 77
                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1907110803 815 SYGFLFPPYLSS-SPEAKYDAFLVTNMVPMYPAF-KRMW 851
Cdd:cd00091    78 DRGHLAPAADPVwSQDAQDATFYLTNMAPQVQGFnQGNW 116
Endonuclease_NS smart00892
DNA/RNA non-specific endonuclease; A family of bacterial and eukaryotic endonucleases share ...
753-849 4.88e-18

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: 83.23  E-value: 4.88e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907110803  753 HTDFESGYSEIFLMPLWTSYTISKQAEVSSIPEHLTNCVRPDVRVSPGFSQNCLAYKNDKQMSYGFLFPPYLS-SSPEAK 831
Cdd:smart00892   1 YKHYALCYDERRRLPLWVAYHLTGSTRQGKNTGRKRPWFKPDGWHLPAIFQAVNSDYTGSGYDRGHLAPAADHgVSQEAM 80
                           90
                   ....*....|....*...
gi 1907110803  832 YDAFLVTNMVPMYPAFKR 849
Cdd:smart00892  81 AATFYLTNIVPQTAGFNQ 98
SO smart00201
Somatomedin B -like domains; Somatomedin-B is a peptide, proteolytically excised from ...
118-159 6.07e-15

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: 69.32  E-value: 6.07e-15
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|..
gi 1907110803  118 GSCKGRCFELQEVGPPdCRCDNLCKSYSSCCHDFDELCLKTA 159
Cdd:smart00201   3 GSCKGRCGESFNEGNA-CRCDALCLSYGDCCTDYESVCKKEV 43
SO smart00201
Somatomedin B -like domains; Somatomedin-B is a peptide, proteolytically excised from ...
160-203 7.24e-15

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: 69.32  E-value: 7.24e-15
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 1907110803  160 RGWECtKDRCGEVRNEENACHCSEDCLSRGDCCTNYQVVCKGES 203
Cdd:smart00201   1 AIGSC-KGRCGESFNEGNACRCDALCLSYGDCCTDYESVCKKEV 43
Somatomedin_B pfam01033
Somatomedin B domain;
162-202 8.84e-13

Somatomedin B domain;


Pssm-ID: 460034  Cd Length: 40  Bit Score: 63.09  E-value: 8.84e-13
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 1907110803 162 WECtKDRCGEVRNEENACHCSEDCLSRGDCCTNYQVVCKGE 202
Cdd:pfam01033   1 ESC-KGRCGESFDRGRLCQCDDDCVKYGDCCPDYESLCLGE 40
Somatomedin_B pfam01033
Somatomedin B domain;
118-158 6.24e-12

Somatomedin B domain;


Pssm-ID: 460034  Cd Length: 40  Bit Score: 60.78  E-value: 6.24e-12
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 1907110803 118 GSCKGRCFELQEVGPPdCRCDNLCKSYSSCCHDFDELCLKT 158
Cdd:pfam01033   1 ESCKGRCGESFDRGRL-CQCDDDCVKYGDCCPDYESLCLGE 40
sulfatase_like cd16150
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ...
225-481 1.77e-06

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: 51.47  E-value: 1.77e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907110803 225 PPLIIFSVDGFRA---SYMKKGSKVMPNIEKLRSCGThapymrpvyptkTFPNLYT-----------LATGLYPESHGiv 290
Cdd:cd16150     1 PNIVIFVADQLRAdslGHLGNPAAVTPNLDALAAEGV------------RFSNAYCqnpvcspsrcsFLTGWYPHVNG-- 66
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907110803 291 GNSM------YDPVFDATFhlrgREKFNHRWWGGqplwitatKQGVRAGTFFW-SVSIPHERRILTILQWLSLPDNERPS 363
Cdd:cd16150    67 HRTLhhllrpDEPNLLKTL----KDAGYHVAWAG--------KNDDLPGEFAAeAYCDSDEACVRTAIDWLRNRRPDKPF 134
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907110803 364 VYAFYSEQPdfsgHKygPFGPEESSYgSPLTPAKRPKRKVAPKRRQERPVAppkKRRRKLHRMDHYTAETrqdkmtnpLR 443
Cdd:cd16150   135 CLYLPLIFP----HP--PYGVEEPWF-SMIDREKLPPRRPPGLRAKGKPSM---LEGIEKQGLDRWSEER--------WR 196
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 1907110803 444 EI-----------DKTVGQLMDGLKQLKLHRCVNVIFVGDHGmeDVTCD 481
Cdd:cd16150   197 ELratylgmvsrlDHQFGRLLEALKETGLYDDTAVFFFSDHG--DYTGD 243
SGSH cd16027
N-sulfoglucosamine sulfohydrolase (SGSH; sulfamidase); N-sulfoglucosamine sulfohydrolase (SGSH) ...
277-475 2.31e-04

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: 44.42  E-value: 2.31e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907110803 277 TLATGLYPESHGIVGN-SMYDPVFDA--TF--HLRgrEK-----FNHRWWGGQPlwitATKQGVRAGTFFWSVSIPHERR 346
Cdd:cd16027    54 ALLTGLYPHQNGAHGLrSRGFPLPDGvkTLpeLLR--EAgyytgLIGKTHYNPD----AVFPFDDEMRGPDDGGRNAWDY 127
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907110803 347 ILTILQWLSLPDNERP--SVYAFyseqpdFSGHKYGPFGPEESSYGSPltpakrpkrkvapkrrQERPVAPpkkrrrklh 424
Cdd:cd16027   128 ASNAADFLNRAKKGQPffLWFGF------HDPHRPYPPGDGEEPGYDP----------------EKVKVPP--------- 176
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1907110803 425 rmdhY---TAETRQD--KMTNPLREIDKTVGQLMDGLKQLKLHRcvN--VIFVGDHGM 475
Cdd:cd16027   177 ----YlpdTPEVREDlaDYYDEIERLDQQVGEILDELEEDGLLD--NtiVIFTSDHGM 228
AslA COG3119
Arylsulfatase A or related enzyme, AlkP superfamily [Inorganic ion transport and metabolism];
391-474 1.77e-03

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


Pssm-ID: 442353 [Multi-domain]  Cd Length: 393  Bit Score: 41.79  E-value: 1.77e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907110803 391 SPLTPAKRPKRKVAPKRRQERPVAPPKKRRRKLHR--MDHYTAEtrqdkmtnpLREIDKTVGQLMDGLKQLKLHRcvN-- 466
Cdd:COG3119   162 APYQAPEEYLDKYDGKDIPLPPNLAPRDLTEEELRraRAAYAAM---------IEEVDDQVGRLLDALEELGLAD--Nti 230

                  ....*...
gi 1907110803 467 VIFVGDHG 474
Cdd:COG3119   231 VVFTSDNG 238
AP-SPAP cd16016
SPAP is a subclass of alkaline phosphatase (AP); Alkaline phosphatases are non-specific ...
224-297 5.09e-03

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: 40.21  E-value: 5.09e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907110803 224 RPPLIIF-SVDGFRASYM--------KKGSK-------VMPNieklrscgTHAPYMrpvyPTKTFPNLYTLATGLYPESH 287
Cdd:cd16016     1 RPKLVVGiVVDQMRADYLyryrdrfgEGGFKrllnegfVFEN--------AHYNYA----PTDTAPGHATIYTGTTPAIH 68
                          90
                  ....*....|
gi 1907110803 288 GIVGNSMYDP 297
Cdd:cd16016    69 GIIGNDWYDR 78
 
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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