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Conserved domains on  [gi|1526949|dbj|BAA06333|]
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phosphodiesterase I [Rattus norvegicus]

Protein Classification

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 ...
162-486 4.77e-109

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: 339.01  E-value: 4.77e-109
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1526949    162 VILFSMDGFRAEYLQTWsTLLPNINKLKTCGLHSKYMRAVYPTKTFPNHYTIVTGLYPESHGIIDNNMYDVYLNKNFSLS 241
Cdd:pfam01663   1 LLVISLDGFRADYLDRF-ELTPNLAALAKEGVSAPNLTPVFPTLTFPNHYTLVTGLYPGSHGIVGNTFYDPKTGEYLVFV 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1526949    242 SVEKSNPAWWSGQPIWLTAMYQGLKAASYYWPGSDVAV---NGSFPNIY-RNYSNSVPYESRIATLL--QWLDLPKA--- 312
Cdd:pfam01663  80 ISDPEDPRWWQGEPIWDTAAKAGVRAAALFWPGSEVDYstyYGTPPRYLkDDYNNSVPFEDRVDTAVlqTWLDLPFAdva 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1526949    313 -ERPSFYTIYVEEPDSAGHKSGPVSAGVIKALQLVDDAFGMLMEGLKQRNLHNCVNIIVLADHGMDQTSCDRVEYMTDYF 391
Cdd:pfam01663 160 aERPDLLLVYLEEPDYAGHRYGPDSPEVEDALRRVDRAIGDLLEALDERGLFEDTNVIVVSDHGMTPVSDDKVIFLNDYL 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1526949    392 PEINFY--MYQGPAPRIRTR-----NIPQDFFTFNSEEIVRDLSCR--KSDQHFKPYLTPDLPKRLHYAKnvRIDKVHLM 462
Cdd:pfam01663 240 REKGLLhlVDGGPVVAIYPKarelgHVPPGEVEEVYAELKEKLLGLriQDGEHLAVYLKEEIPGRLHYNP--RIPDLVLV 317
                         330       340
                  ....*....|....*....|....*.
gi 1526949    463 VDRQWLAYRNKG--VPNCEGGTHGYN 486
Cdd:pfam01663 318 ADPGWYITGKDGgdKEAAIHGTHGYD 343
NUC cd00091
DNA/RNA non-specific endonuclease; prokaryotic and eukaryotic double- and single-stranded DNA ...
608-868 3.17e-64

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: 215.70  E-value: 3.17e-64
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1526949  608 LPFGRPRVIQKNkdhCLLYHREYVSGFGKAMKMPMWSSYTVPKPGDTSSlPPTVPDCLRADVRVDPSESQKCSFYLADQN 687
Cdd:cd00091   1 LQYGRPGVLADT---EVLSYTHYVLSYNRATRLPLWVAEHIDKEDLGKN-VDRKYDQFKQDPRIPPLFSATNSDYKGSGS 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1526949  688 IDHGFLYPPA-IKGNNESQYDALITSNLVPMYKEF-KKMWDYFHKVLLIKYAIERNGVNVVSGPIFDYNYDGHFDApDEI 765
Cdd:cd00091  77 LDRGHLAPAAdPVWSQDAQDATFYLTNMAPQVQGFnQGNWAYLEDYLRDLAASEGKDVYVVTGPLFLPDLDGDGGS-YLS 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1526949  766 TNYVAGTDVPVPTHYFVVLTSCKNkthtpdscPGWLDVLPFVVPHRPTKpvescpENKAEDLWVEERFKAHIARVRDvel 845
Cdd:cd00091 156 TQVINNGKVAVPTHFWKVIIDEKA--------PGNLSVGAFVLPNNNPH------DTLEFILCVEKTFQVPVASVEK--- 218
                       250       260
                ....*....|....*....|...
gi 1526949  846 LTGLDFYQEKTQPVSEILQLKTY 868
Cdd:cd00091 219 ATGLSFFCNVPDSVSAVLELKKK 241
SO smart00201
Somatomedin B -like domains; Somatomedin-B is a peptide, proteolytically excised from ...
51-94 1.55e-13

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: 65.47  E-value: 1.55e-13
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 1526949      51 HIGSCRKKCFDSSHRGLEgCRCDSGCTDRGDCCWDFEDTCVKST 94
Cdd:smart00201   1 AIGSCKGRCGESFNEGNA-CRCDALCLSYGDCCTDYESVCKKEV 43
SO smart00201
Somatomedin B -like domains; Somatomedin-B is a peptide, proteolytically excised from ...
95-138 2.87e-13

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: 64.70  E-value: 2.87e-13
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 1526949      95 QIWTCNsFRCGETRLETALCSCADDCLQRKDCCTDYKAVCQGEV 138
Cdd:smart00201   1 AIGSCK-GRCGESFNEGNACRCDALCLSYGDCCTDYESVCKKEV 43
 
Name Accession Description Interval E-value
Phosphodiest pfam01663
Type I phosphodiesterase / nucleotide pyrophosphatase; This family consists of ...
162-486 4.77e-109

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: 339.01  E-value: 4.77e-109
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1526949    162 VILFSMDGFRAEYLQTWsTLLPNINKLKTCGLHSKYMRAVYPTKTFPNHYTIVTGLYPESHGIIDNNMYDVYLNKNFSLS 241
Cdd:pfam01663   1 LLVISLDGFRADYLDRF-ELTPNLAALAKEGVSAPNLTPVFPTLTFPNHYTLVTGLYPGSHGIVGNTFYDPKTGEYLVFV 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1526949    242 SVEKSNPAWWSGQPIWLTAMYQGLKAASYYWPGSDVAV---NGSFPNIY-RNYSNSVPYESRIATLL--QWLDLPKA--- 312
Cdd:pfam01663  80 ISDPEDPRWWQGEPIWDTAAKAGVRAAALFWPGSEVDYstyYGTPPRYLkDDYNNSVPFEDRVDTAVlqTWLDLPFAdva 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1526949    313 -ERPSFYTIYVEEPDSAGHKSGPVSAGVIKALQLVDDAFGMLMEGLKQRNLHNCVNIIVLADHGMDQTSCDRVEYMTDYF 391
Cdd:pfam01663 160 aERPDLLLVYLEEPDYAGHRYGPDSPEVEDALRRVDRAIGDLLEALDERGLFEDTNVIVVSDHGMTPVSDDKVIFLNDYL 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1526949    392 PEINFY--MYQGPAPRIRTR-----NIPQDFFTFNSEEIVRDLSCR--KSDQHFKPYLTPDLPKRLHYAKnvRIDKVHLM 462
Cdd:pfam01663 240 REKGLLhlVDGGPVVAIYPKarelgHVPPGEVEEVYAELKEKLLGLriQDGEHLAVYLKEEIPGRLHYNP--RIPDLVLV 317
                         330       340
                  ....*....|....*....|....*.
gi 1526949    463 VDRQWLAYRNKG--VPNCEGGTHGYN 486
Cdd:pfam01663 318 ADPGWYITGKDGgdKEAAIHGTHGYD 343
Enpp cd16018
Ectonucleotide pyrophosphatase/phosphodiesterase, also called autotaxin; Ecto-nucleotide ...
160-526 1.22e-108

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: 334.94  E-value: 1.22e-108
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1526949  160 PPVILFSMDGFRAEYLQTWStLLPNINKLKTCGLHSKYMRAVYPTKTFPNHYTIVTGLYPESHGIIDNNMYDVYLNKNFS 239
Cdd:cd16018   1 PPLIVISIDGFRWDYLDRAG-LTPNLKRLAEEGVRAKYVKPVFPTLTFPNHYSIVTGLYPESHGIVGNYFYDPKTNEEFS 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1526949  240 lSSVEKSNPAWWSGQPIWLTAMYQGLKAASYYWPGSDVAVNGSFP------NIYRNYSNSVPYESRIATLLQWLDLpkaE 313
Cdd:cd16018  80 -DSDWVWDPWWIGGEPIWVTAEKAGLKTASYFWPGSEVAIIGYNPtpiplgGYWQPYNDSFPFEERVDTILEWLDL---E 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1526949  314 RPSFYTIYVEEPDSAGHKSGPVSAGVIKALQLVDDAFGMLMEGLKQRNLHNCVNIIVLADHGMDQTscdrveymtdyfpe 393
Cdd:cd16018 156 RPDLILLYFEEPDSAGHKYGPDSPEVNEALKRVDRRLGYLIEALKERGLLDDTNIIVVSDHGMTDV-------------- 221
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1526949  394 infymyqgpaprirtrnipqdfftfnseeivrdlscrksdqhfkpyltpdlpkrlhyaknvridkvhlmvdrqwlayrnk 473
Cdd:cd16018     --------------------------------------------------------------------------------
                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|...
gi 1526949  474 gvpncegGTHGYNNEFKSMEAIFLAHGPSFKEKTVIEPFENIEVYNLLCDLLH 526
Cdd:cd16018 222 -------GTHGYDNELPDMRAIFIARGPAFKKGKKLGPFRNVDIYPLMCNLLG 267
AtaC COG1524
c-di-AMP phosphodiesterase AtaC or nucleotide pyrophosphatase, AlkP superfamily [Signal ...
158-528 7.57e-68

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


Pssm-ID: 441133 [Multi-domain]  Cd Length: 370  Bit Score: 230.41  E-value: 7.57e-68
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1526949  158 DQPPVILFSMDGFRAEYLQTWSTllPNINKLKTCGLHSKYMRAVYPTKTFPNHYTIVTGLYPESHGIIDNNMYD-VYLNK 236
Cdd:COG1524  22 PAKKVVLILVDGLRADLLERAHA--PNLAALAARGVYARPLTSVFPSTTAPAHTTLLTGLYPGEHGIVGNGWYDpELGRV 99
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1526949  237 NFSLSSVEKSN--PAWWSGQPIWLTAMYQGLKAASYYWPGSDVA--VNGSFPNIYRNYSNSVP-YESRIATLLQWLDLPK 311
Cdd:COG1524 100 VNSLSWVEDGFgsNSLLPVPTIFERARAAGLTTAAVFWPSFEGSglIDAARPYPYDGRKPLLGnPAADRWIAAAALELLR 179
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1526949  312 AERPSFYTIYVEEPDSAGHKSGPVSAGVIKALQLVDDAFGMLMEGLKQRNLHNCVNIIVLADHGMdqTSCDRVEYMTDYF 391
Cdd:COG1524 180 EGRPDLLLVYLPDLDYAGHRYGPDSPEYRAALREVDAALGRLLDALKARGLYEGTLVIVTADHGM--VDVPPDIDLNRLR 257
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1526949  392 PEINFYMYQGPAPRIRTRNipqdfftfNSEEIVRDLscrkSDQHFKPYlTPDLPKRLHYAKNvRIDKVHLMVDRQWLAYR 471
Cdd:COG1524 258 LAGLLAVRAGESAHLYLKD--------GADAEVRAL----LGLPARVL-TREELAAGHFGPH-RIGDLVLVAKPGWALDA 323
                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 1526949  472 NKgvpnceGGTHGYNNEfKSMEAIFLAHGPSFKEKtviepFENIEVYNLLCDLLHIQ 528
Cdd:COG1524 324 PL------KGSHGGLPD-EEMRVPLLASGPGFRPG-----VRNVDVAPTIARLLGLP 368
NUC cd00091
DNA/RNA non-specific endonuclease; prokaryotic and eukaryotic double- and single-stranded DNA ...
608-868 3.17e-64

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: 215.70  E-value: 3.17e-64
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1526949  608 LPFGRPRVIQKNkdhCLLYHREYVSGFGKAMKMPMWSSYTVPKPGDTSSlPPTVPDCLRADVRVDPSESQKCSFYLADQN 687
Cdd:cd00091   1 LQYGRPGVLADT---EVLSYTHYVLSYNRATRLPLWVAEHIDKEDLGKN-VDRKYDQFKQDPRIPPLFSATNSDYKGSGS 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1526949  688 IDHGFLYPPA-IKGNNESQYDALITSNLVPMYKEF-KKMWDYFHKVLLIKYAIERNGVNVVSGPIFDYNYDGHFDApDEI 765
Cdd:cd00091  77 LDRGHLAPAAdPVWSQDAQDATFYLTNMAPQVQGFnQGNWAYLEDYLRDLAASEGKDVYVVTGPLFLPDLDGDGGS-YLS 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1526949  766 TNYVAGTDVPVPTHYFVVLTSCKNkthtpdscPGWLDVLPFVVPHRPTKpvescpENKAEDLWVEERFKAHIARVRDvel 845
Cdd:cd00091 156 TQVINNGKVAVPTHFWKVIIDEKA--------PGNLSVGAFVLPNNNPH------DTLEFILCVEKTFQVPVASVEK--- 218
                       250       260
                ....*....|....*....|...
gi 1526949  846 LTGLDFYQEKTQPVSEILQLKTY 868
Cdd:cd00091 219 ATGLSFFCNVPDSVSAVLELKKK 241
NUC smart00477
DNA/RNA non-specific endonuclease; prokaryotic and eukaryotic double- and single-stranded DNA ...
627-858 4.65e-63

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: 211.45  E-value: 4.65e-63
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1526949     627 HREYVSGFGKAMKMPMWSSYTVPKPGDTSSlPPTVPDCLRADVRVDPSESQKCSFYLADqNIDHGFLYPPA-IKGNNESQ 705
Cdd:smart00477   1 RNQYVLGYNRSTRMPNWVAYHITGELLTSG-AERKSDCFKPDTRIPEKFQAKLSDYKGS-GYDRGHLAPAAdHKFSSEAM 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1526949     706 YDALITSNLVPMYKEFK-KMWDYFHKVLLIKYAIERNGVNVVSGPIFDYNYDGHFDAPdEITNYVAG-TDVPVPTHYFVV 783
Cdd:smart00477  79 ADTFYLSNIVPQYPDFNrGAWAYLEDYLRKLTASERNGVYVVSGPLFLPNYDGKGDKL-EVKYQVIGsKNVAIPTHFFKV 157
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1526949     784 LTSCKNkthtpdscPGWLDVLPFVVPHRPTKpVESCpenkaedlwveerFKAHIARVRDVELLTGLDFYQEKTQP 858
Cdd:smart00477 158 ITAEKA--------DSYLEVAAFILPNDPIN-DESP-------------LTNFRVPVDEIERLTGLDFFRNLDPA 210
SO smart00201
Somatomedin B -like domains; Somatomedin-B is a peptide, proteolytically excised from ...
51-94 1.55e-13

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: 65.47  E-value: 1.55e-13
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 1526949      51 HIGSCRKKCFDSSHRGLEgCRCDSGCTDRGDCCWDFEDTCVKST 94
Cdd:smart00201   1 AIGSCKGRCGESFNEGNA-CRCDALCLSYGDCCTDYESVCKKEV 43
SO smart00201
Somatomedin B -like domains; Somatomedin-B is a peptide, proteolytically excised from ...
95-138 2.87e-13

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: 64.70  E-value: 2.87e-13
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 1526949      95 QIWTCNsFRCGETRLETALCSCADDCLQRKDCCTDYKAVCQGEV 138
Cdd:smart00201   1 AIGSCK-GRCGESFNEGNACRCDALCLSYGDCCTDYESVCKKEV 43
Somatomedin_B pfam01033
Somatomedin B domain;
97-137 1.23e-11

Somatomedin B domain;


Pssm-ID: 460034  Cd Length: 40  Bit Score: 60.01  E-value: 1.23e-11
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 1526949     97 WTCNsFRCGETRLETALCSCADDCLQRKDCCTDYKAVCQGE 137
Cdd:pfam01033   1 ESCK-GRCGESFDRGRLCQCDDDCVKYGDCCPDYESLCLGE 40
NUC1 COG1864
DNA/RNA endonuclease G, NUC1 [Nucleotide transport and metabolism];
607-851 1.28e-10

DNA/RNA endonuclease G, NUC1 [Nucleotide transport and metabolism];


Pssm-ID: 441469  Cd Length: 238  Bit Score: 62.62  E-value: 1.28e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1526949  607 NLPFGRPRVIQK-NKDHCLLYHREYVSGFGKAMKMPMWSSYTVpkpgDTSSLPPTVP--DCLRADVRVDPSESQKCSFYl 683
Cdd:COG1864   9 FLLLGLPSLARAlSTNNYLLCYTGYSLSYNESRRTPNWVAYNL----DGSWLGKSLKrsDDFRPDPRLPSGYRATLADY- 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1526949  684 ADQNIDHGFLYPPA-IKGNNESQYDALITSNLVPMYKEF-KKMWDYFHKVLLiKYAIERNGVNVVSGPIFDynydghfda 761
Cdd:COG1864  84 TGSGYDRGHLAPSAdRTFSKEANSETFLMTNISPQAPDFnQGIWARLENYVR-DLARKGGEVYVVTGPVFD--------- 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1526949  762 PDEITNYVAGtDVPVPTHYF-VVLTscknkthtPDSCPGWLDVLPFVVPHRPTKpvescpenkaedlwvEERFKAHIARV 840
Cdd:COG1864 154 DGDLKTIGSG-GVAVPTAFWkVVVD--------PDKNTGTLRAIAFLLPNTALS---------------SGPLRTYQVSV 209
                       250
                ....*....|.
gi 1526949  841 RDVELLTGLDF 851
Cdd:COG1864 210 DEIEKLTGLDF 220
Somatomedin_B pfam01033
Somatomedin B domain;
53-93 2.56e-10

Somatomedin B domain;


Pssm-ID: 460034  Cd Length: 40  Bit Score: 56.16  E-value: 2.56e-10
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 1526949     53 GSCRKKCFDSSHRGLeGCRCDSGCTDRGDCCWDFEDTCVKS 93
Cdd:pfam01033   1 ESCKGRCGESFDRGR-LCQCDDDCVKYGDCCPDYESLCLGE 40
 
Name Accession Description Interval E-value
Phosphodiest pfam01663
Type I phosphodiesterase / nucleotide pyrophosphatase; This family consists of ...
162-486 4.77e-109

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: 339.01  E-value: 4.77e-109
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1526949    162 VILFSMDGFRAEYLQTWsTLLPNINKLKTCGLHSKYMRAVYPTKTFPNHYTIVTGLYPESHGIIDNNMYDVYLNKNFSLS 241
Cdd:pfam01663   1 LLVISLDGFRADYLDRF-ELTPNLAALAKEGVSAPNLTPVFPTLTFPNHYTLVTGLYPGSHGIVGNTFYDPKTGEYLVFV 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1526949    242 SVEKSNPAWWSGQPIWLTAMYQGLKAASYYWPGSDVAV---NGSFPNIY-RNYSNSVPYESRIATLL--QWLDLPKA--- 312
Cdd:pfam01663  80 ISDPEDPRWWQGEPIWDTAAKAGVRAAALFWPGSEVDYstyYGTPPRYLkDDYNNSVPFEDRVDTAVlqTWLDLPFAdva 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1526949    313 -ERPSFYTIYVEEPDSAGHKSGPVSAGVIKALQLVDDAFGMLMEGLKQRNLHNCVNIIVLADHGMDQTSCDRVEYMTDYF 391
Cdd:pfam01663 160 aERPDLLLVYLEEPDYAGHRYGPDSPEVEDALRRVDRAIGDLLEALDERGLFEDTNVIVVSDHGMTPVSDDKVIFLNDYL 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1526949    392 PEINFY--MYQGPAPRIRTR-----NIPQDFFTFNSEEIVRDLSCR--KSDQHFKPYLTPDLPKRLHYAKnvRIDKVHLM 462
Cdd:pfam01663 240 REKGLLhlVDGGPVVAIYPKarelgHVPPGEVEEVYAELKEKLLGLriQDGEHLAVYLKEEIPGRLHYNP--RIPDLVLV 317
                         330       340
                  ....*....|....*....|....*.
gi 1526949    463 VDRQWLAYRNKG--VPNCEGGTHGYN 486
Cdd:pfam01663 318 ADPGWYITGKDGgdKEAAIHGTHGYD 343
Enpp cd16018
Ectonucleotide pyrophosphatase/phosphodiesterase, also called autotaxin; Ecto-nucleotide ...
160-526 1.22e-108

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: 334.94  E-value: 1.22e-108
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1526949  160 PPVILFSMDGFRAEYLQTWStLLPNINKLKTCGLHSKYMRAVYPTKTFPNHYTIVTGLYPESHGIIDNNMYDVYLNKNFS 239
Cdd:cd16018   1 PPLIVISIDGFRWDYLDRAG-LTPNLKRLAEEGVRAKYVKPVFPTLTFPNHYSIVTGLYPESHGIVGNYFYDPKTNEEFS 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1526949  240 lSSVEKSNPAWWSGQPIWLTAMYQGLKAASYYWPGSDVAVNGSFP------NIYRNYSNSVPYESRIATLLQWLDLpkaE 313
Cdd:cd16018  80 -DSDWVWDPWWIGGEPIWVTAEKAGLKTASYFWPGSEVAIIGYNPtpiplgGYWQPYNDSFPFEERVDTILEWLDL---E 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1526949  314 RPSFYTIYVEEPDSAGHKSGPVSAGVIKALQLVDDAFGMLMEGLKQRNLHNCVNIIVLADHGMDQTscdrveymtdyfpe 393
Cdd:cd16018 156 RPDLILLYFEEPDSAGHKYGPDSPEVNEALKRVDRRLGYLIEALKERGLLDDTNIIVVSDHGMTDV-------------- 221
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1526949  394 infymyqgpaprirtrnipqdfftfnseeivrdlscrksdqhfkpyltpdlpkrlhyaknvridkvhlmvdrqwlayrnk 473
Cdd:cd16018     --------------------------------------------------------------------------------
                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|...
gi 1526949  474 gvpncegGTHGYNNEFKSMEAIFLAHGPSFKEKTVIEPFENIEVYNLLCDLLH 526
Cdd:cd16018 222 -------GTHGYDNELPDMRAIFIARGPAFKKGKKLGPFRNVDIYPLMCNLLG 267
AtaC COG1524
c-di-AMP phosphodiesterase AtaC or nucleotide pyrophosphatase, AlkP superfamily [Signal ...
158-528 7.57e-68

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


Pssm-ID: 441133 [Multi-domain]  Cd Length: 370  Bit Score: 230.41  E-value: 7.57e-68
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1526949  158 DQPPVILFSMDGFRAEYLQTWSTllPNINKLKTCGLHSKYMRAVYPTKTFPNHYTIVTGLYPESHGIIDNNMYD-VYLNK 236
Cdd:COG1524  22 PAKKVVLILVDGLRADLLERAHA--PNLAALAARGVYARPLTSVFPSTTAPAHTTLLTGLYPGEHGIVGNGWYDpELGRV 99
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1526949  237 NFSLSSVEKSN--PAWWSGQPIWLTAMYQGLKAASYYWPGSDVA--VNGSFPNIYRNYSNSVP-YESRIATLLQWLDLPK 311
Cdd:COG1524 100 VNSLSWVEDGFgsNSLLPVPTIFERARAAGLTTAAVFWPSFEGSglIDAARPYPYDGRKPLLGnPAADRWIAAAALELLR 179
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1526949  312 AERPSFYTIYVEEPDSAGHKSGPVSAGVIKALQLVDDAFGMLMEGLKQRNLHNCVNIIVLADHGMdqTSCDRVEYMTDYF 391
Cdd:COG1524 180 EGRPDLLLVYLPDLDYAGHRYGPDSPEYRAALREVDAALGRLLDALKARGLYEGTLVIVTADHGM--VDVPPDIDLNRLR 257
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1526949  392 PEINFYMYQGPAPRIRTRNipqdfftfNSEEIVRDLscrkSDQHFKPYlTPDLPKRLHYAKNvRIDKVHLMVDRQWLAYR 471
Cdd:COG1524 258 LAGLLAVRAGESAHLYLKD--------GADAEVRAL----LGLPARVL-TREELAAGHFGPH-RIGDLVLVAKPGWALDA 323
                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 1526949  472 NKgvpnceGGTHGYNNEfKSMEAIFLAHGPSFKEKtviepFENIEVYNLLCDLLHIQ 528
Cdd:COG1524 324 PL------KGSHGGLPD-EEMRVPLLASGPGFRPG-----VRNVDVAPTIARLLGLP 368
NUC cd00091
DNA/RNA non-specific endonuclease; prokaryotic and eukaryotic double- and single-stranded DNA ...
608-868 3.17e-64

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: 215.70  E-value: 3.17e-64
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1526949  608 LPFGRPRVIQKNkdhCLLYHREYVSGFGKAMKMPMWSSYTVPKPGDTSSlPPTVPDCLRADVRVDPSESQKCSFYLADQN 687
Cdd:cd00091   1 LQYGRPGVLADT---EVLSYTHYVLSYNRATRLPLWVAEHIDKEDLGKN-VDRKYDQFKQDPRIPPLFSATNSDYKGSGS 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1526949  688 IDHGFLYPPA-IKGNNESQYDALITSNLVPMYKEF-KKMWDYFHKVLLIKYAIERNGVNVVSGPIFDYNYDGHFDApDEI 765
Cdd:cd00091  77 LDRGHLAPAAdPVWSQDAQDATFYLTNMAPQVQGFnQGNWAYLEDYLRDLAASEGKDVYVVTGPLFLPDLDGDGGS-YLS 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1526949  766 TNYVAGTDVPVPTHYFVVLTSCKNkthtpdscPGWLDVLPFVVPHRPTKpvescpENKAEDLWVEERFKAHIARVRDvel 845
Cdd:cd00091 156 TQVINNGKVAVPTHFWKVIIDEKA--------PGNLSVGAFVLPNNNPH------DTLEFILCVEKTFQVPVASVEK--- 218
                       250       260
                ....*....|....*....|...
gi 1526949  846 LTGLDFYQEKTQPVSEILQLKTY 868
Cdd:cd00091 219 ATGLSFFCNVPDSVSAVLELKKK 241
NUC smart00477
DNA/RNA non-specific endonuclease; prokaryotic and eukaryotic double- and single-stranded DNA ...
627-858 4.65e-63

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: 211.45  E-value: 4.65e-63
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1526949     627 HREYVSGFGKAMKMPMWSSYTVPKPGDTSSlPPTVPDCLRADVRVDPSESQKCSFYLADqNIDHGFLYPPA-IKGNNESQ 705
Cdd:smart00477   1 RNQYVLGYNRSTRMPNWVAYHITGELLTSG-AERKSDCFKPDTRIPEKFQAKLSDYKGS-GYDRGHLAPAAdHKFSSEAM 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1526949     706 YDALITSNLVPMYKEFK-KMWDYFHKVLLIKYAIERNGVNVVSGPIFDYNYDGHFDAPdEITNYVAG-TDVPVPTHYFVV 783
Cdd:smart00477  79 ADTFYLSNIVPQYPDFNrGAWAYLEDYLRKLTASERNGVYVVSGPLFLPNYDGKGDKL-EVKYQVIGsKNVAIPTHFFKV 157
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1526949     784 LTSCKNkthtpdscPGWLDVLPFVVPHRPTKpVESCpenkaedlwveerFKAHIARVRDVELLTGLDFYQEKTQP 858
Cdd:smart00477 158 ITAEKA--------DSYLEVAAFILPNDPIN-DESP-------------LTNFRVPVDEIERLTGLDFFRNLDPA 210
Endonuclease_NS smart00892
DNA/RNA non-specific endonuclease; A family of bacterial and eukaryotic endonucleases share ...
630-855 1.11e-28

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: 114.04  E-value: 1.11e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1526949     630 YVSGFGKAMKMPMWSSYTVPKPGDTSSLPPTVPDCLRADVRVDPSESQKCSFYLADQNIDHGFLYPPA-IKGNNESQYDA 708
Cdd:smart00892   4 YALCYDERRRLPLWVAYHLTGSTRQGKNTGRKRPWFKPDGWHLPAIFQAVNSDYTGSGYDRGHLAPAAdHGVSQEAMAAT 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1526949     709 LITSNLVPMYKEF-KKMWDYFHKVLLIKYAIERNGVNVVSGPIFDYNYDghfdapdeitnyvaGTDVPVPTHYFVVLTSc 787
Cdd:smart00892  84 FYLTNIVPQTAGFnQGNWNRLENYVRKLLAKNKDTVYVVTGPIYLPTLP--------------DNNVAVPSHFWKVILS- 148
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1526949     788 knkthtPDSCPGWLDVLPFVVPHRPTKPvescpenkaedlwvEERFKAHIARVRDVELLTGLDFYQEK 855
Cdd:smart00892 149 ------EDGSNGGLAAIAFNLPNAPINE--------------DYPLCEFQVPVDNIERLTGLDFFCGL 196
ALP_like cd00016
alkaline phosphatases and sulfatases; This family includes alkaline phosphatases and ...
160-377 1.18e-27

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: 112.13  E-value: 1.18e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1526949  160 PPVILFSMDGFRAEYLQ---TWSTLLPNINKLKTCGLHSKYMRAVYPTKTFPNHYTIVTGLYPESHGIIDNNMYDVYLNk 236
Cdd:cd00016   1 KHVVLIVLDGLGADDLGkagNPAPTTPNLKRLASEGATFNFRSVSPPTSSAPNHAALLTGAYPTLHGYTGNGSADPELP- 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1526949  237 nfslssvEKSNPAWWSGQPIWltamyQGLKAASYYWpgsdvavngsfpniyrnysnsvpyesRIATLLQWLDLPKAERPS 316
Cdd:cd00016  80 -------SRAAGKDEDGPTIP-----ELLKQAGYRT--------------------------GVIGLLKAIDETSKEKPF 121
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1526949  317 FYTIYVEEPDSAGHKSGPVSAGVIKALQLVDDAFGMLMEGLKQRNLHNCVNIIVLADHGMD 377
Cdd:cd00016 122 VLFLHFDGPDGPGHAYGPNTPEYYDAVEEIDERIGKVLDALKKAGDADDTVIIVTADHGGI 182
SO smart00201
Somatomedin B -like domains; Somatomedin-B is a peptide, proteolytically excised from ...
51-94 1.55e-13

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: 65.47  E-value: 1.55e-13
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 1526949      51 HIGSCRKKCFDSSHRGLEgCRCDSGCTDRGDCCWDFEDTCVKST 94
Cdd:smart00201   1 AIGSCKGRCGESFNEGNA-CRCDALCLSYGDCCTDYESVCKKEV 43
SO smart00201
Somatomedin B -like domains; Somatomedin-B is a peptide, proteolytically excised from ...
95-138 2.87e-13

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: 64.70  E-value: 2.87e-13
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 1526949      95 QIWTCNsFRCGETRLETALCSCADDCLQRKDCCTDYKAVCQGEV 138
Cdd:smart00201   1 AIGSCK-GRCGESFNEGNACRCDALCLSYGDCCTDYESVCKKEV 43
Somatomedin_B pfam01033
Somatomedin B domain;
97-137 1.23e-11

Somatomedin B domain;


Pssm-ID: 460034  Cd Length: 40  Bit Score: 60.01  E-value: 1.23e-11
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 1526949     97 WTCNsFRCGETRLETALCSCADDCLQRKDCCTDYKAVCQGE 137
Cdd:pfam01033   1 ESCK-GRCGESFDRGRLCQCDDDCVKYGDCCPDYESLCLGE 40
NUC1 COG1864
DNA/RNA endonuclease G, NUC1 [Nucleotide transport and metabolism];
607-851 1.28e-10

DNA/RNA endonuclease G, NUC1 [Nucleotide transport and metabolism];


Pssm-ID: 441469  Cd Length: 238  Bit Score: 62.62  E-value: 1.28e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1526949  607 NLPFGRPRVIQK-NKDHCLLYHREYVSGFGKAMKMPMWSSYTVpkpgDTSSLPPTVP--DCLRADVRVDPSESQKCSFYl 683
Cdd:COG1864   9 FLLLGLPSLARAlSTNNYLLCYTGYSLSYNESRRTPNWVAYNL----DGSWLGKSLKrsDDFRPDPRLPSGYRATLADY- 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1526949  684 ADQNIDHGFLYPPA-IKGNNESQYDALITSNLVPMYKEF-KKMWDYFHKVLLiKYAIERNGVNVVSGPIFDynydghfda 761
Cdd:COG1864  84 TGSGYDRGHLAPSAdRTFSKEANSETFLMTNISPQAPDFnQGIWARLENYVR-DLARKGGEVYVVTGPVFD--------- 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1526949  762 PDEITNYVAGtDVPVPTHYF-VVLTscknkthtPDSCPGWLDVLPFVVPHRPTKpvescpenkaedlwvEERFKAHIARV 840
Cdd:COG1864 154 DGDLKTIGSG-GVAVPTAFWkVVVD--------PDKNTGTLRAIAFLLPNTALS---------------SGPLRTYQVSV 209
                       250
                ....*....|.
gi 1526949  841 RDVELLTGLDF 851
Cdd:COG1864 210 DEIEKLTGLDF 220
Somatomedin_B pfam01033
Somatomedin B domain;
53-93 2.56e-10

Somatomedin B domain;


Pssm-ID: 460034  Cd Length: 40  Bit Score: 56.16  E-value: 2.56e-10
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 1526949     53 GSCRKKCFDSSHRGLeGCRCDSGCTDRGDCCWDFEDTCVKS 93
Cdd:pfam01033   1 ESCKGRCGESFDRGR-LCQCDDDCVKYGDCCPDYESLCLGE 40
GPI_EPT cd16019
GPI ethanolamine phosphate transferase; Ethanolamine phosphate transferase is involved in ...
161-378 2.42e-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: 43.89  E-value: 2.42e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1526949  161 PVILFSMDGFRAEYLQTWSTLLPNINKLKTCGLHSKYMR-----AVYPTKTFPNHYTIVTGLYPEshgIIDnnmydvyLN 235
Cdd:cd16019   6 KVVLIVIDGLRYDLAVNVNKQSSFFSFLQKLNEQPNNSFlalsfADPPTVTGPRLKALTTGNPPT---FLD-------LI 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1526949  236 KNFSLSSVEKSNpawwsgqpiWLTAMYQGLKAASYYwpgSDVAVNGSFPNIYRNYSNSVPYESR---------IATLLQW 306
Cdd:cd16019  76 SNFASSEIKEDN---------IIRQLKKNGKKILFY---GDDTWLDLFPEIFTYKFTITSFNIRdmhdvdpifYNHINDN 143
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1526949  307 LDLPKAERP-SFYTIYVEEPDSAGHKSGPVSAGVI-KALQLVDDAFgmlmeglkqRNLHNCVN----IIVLADHGMDQ 378
Cdd:cd16019 144 LDENIYYDNwDFIILHFLGLDHLGHKHNTTSSPELeKKLDQMDNLI---------RDIYDRMDndtlLVVVSDHGMNN 212
AP-SPAP cd16016
SPAP is a subclass of alkaline phosphatase (AP); Alkaline phosphatases are non-specific ...
162-236 2.91e-04

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: 44.44  E-value: 2.91e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1526949  162 VILFSMDGFRAEYL-QTWSTLLPN-INKLKTCGLHskYMRAVY---PTKTFPNHYTIVTGLYPESHGIIDNNMYDVYLNK 236
Cdd:cd16016   5 VVGIVVDQMRADYLyRYRDRFGEGgFKRLLNEGFV--FENAHYnyaPTDTAPGHATIYTGTTPAIHGIIGNDWYDRETGR 82
 
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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