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Conserved domains on  [gi|1958791576|ref|XP_038935904|]
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ectonucleotide pyrophosphatase/phosphodiesterase family member 2 isoform X1 [Rattus norvegicus]

Protein Classification

Enpp and NUC domain-containing protein( domain architecture ID 12193410)

protein containing domains SO, Enpp, and NUC

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 ...
 226-538 2.28e-107

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: 336.32  E-value: 2.28e-107
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958791576 226 LIIFSVDGFRASYMKKGsKVMPNIEKLRSCGTHAPYMRPVYPTKTFPNLYTLATGLYPESHGIVGNSMYDPVFDASFHLR 305
Cdd:pfam01663   1 LLVISLDGFRADYLDRF-ELTPNLAALAKEGVSAPNLTPVFPTLTFPNHYTLVTGLYPGSHGIVGNTFYDPKTGEYLVFV 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958791576 306 GREKFNHRWWGGQPLWITATKQGVRAGTFFW----------------------SVSIPHERRILTIL--QWLSLPD---- 357
Cdd:pfam01663  80 ISDPEDPRWWQGEPIWDTAAKAGVRAAALFWpgsevdystyygtpprylkddyNNSVPFEDRVDTAVlqTWLDLPFadva 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958791576 358 NERPSVYAFYSEQPDFSGHKYGPFGPEMTNPLREIDKTVGQLMDGLKQLRLHRCVNVIFVGDHGMEDVTCDRTEFLSNYL 437
Cdd:pfam01663 160 AERPDLLLVYLEEPDYAGHRYGPDSPEVEDALRRVDRAIGDLLEALDERGLFEDTNVIVVSDHGMTPVSDDKVIFLNDYL 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958791576 438 TNVDDITLV-PGTLGRIRAKSIN-------NSKYDPKTIIANLTC--KKPDQHFKPYMKQHLPKRLHYanNRRIEDIHLL 507
Cdd:pfam01663 240 REKGLLHLVdGGPVVAIYPKARElghvppgEVEEVYAELKEKLLGlrIQDGEHLAVYLKEEIPGRLHY--NPRIPDLVLV 317

                         330       340       350
                  ....*....|....*....|....*....|.
gi 1958791576 508 VDRRWHVARKpldvyKKPSGKCFFQGDHGFD 538
Cdd:pfam01663 318 ADPGWYITGK-----DGGDKEAAIHGTHGYD 343
NUC smart00477
DNA/RNA non-specific endonuclease; prokaryotic and eukaryotic double- and single-stranded DNA ...
 700-930 2.60e-76

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: 248.43  E-value: 2.60e-76
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958791576  700 HTDFESGYSEIFLMPLWTSYTISKQAEVSSiPEHLTNCVRPDVRVSPGFSQNCLAYKNDKqMSYGFLFPPYL-SSSPEAK 778
Cdd:smart00477   1 RNQYVLGYNRSTRMPNWVAYHITGELLTSG-AERKSDCFKPDTRIPEKFQAKLSDYKGSG-YDRGHLAPAADhKFSSEAM 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958791576  779 YDAFLVTNMVPMYPAFKRV-WAYFQRVLVKKYASERNGVNVISGPIFDYNYDGLRDTEdEIKQYVEGS-SIPVPTHYYSI 856
Cdd:smart00477  79 ADTFYLSNIVPQYPDFNRGaWAYLEDYLRKLTASERNGVYVVSGPLFLPNYDGKGDKL-EVKYQVIGSkNVAIPTHFFKV 157

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958791576  857 ITSCLDftqpadkcDGPLSVSSFILPHRPDNDESCnssedeskwveelMKMHTARVRDIEHLTGLDFYRKTSRS 930
Cdd:smart00477 158 ITAEKA--------DSYLEVAAFILPNDPINDESP-------------LTNFRVPVDEIERLTGLDFFRNLDPA 210
SO smart00201
Somatomedin B -like domains; Somatomedin-B is a peptide, proteolytically excised from ...
 117-158 2.46e-14

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: 67.78  E-value: 2.46e-14
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|..
gi 1958791576  117 GSCKGRCFELQEVGPPdCRCDNLCKSYSSCCHDFDELCLKTA 158
Cdd:smart00201   3 GSCKGRCGESFNEGNA-CRCDALCLSYGDCCTDYESVCKKEV 43
SO smart00201
Somatomedin B -like domains; Somatomedin-B is a peptide, proteolytically excised from ...
 159-202 2.99e-14

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: 67.40  E-value: 2.99e-14
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 1958791576  159 RGWECtKDRCGEVRNEENACHCSEDCLSRGDCCTNYQVVCKGES 202
Cdd:smart00201   1 AIGSC-KGRCGESFNEGNACRCDALCLSYGDCCTDYESVCKKEV 43
 
Name Accession Description Interval E-value
Phosphodiest pfam01663
Type I phosphodiesterase / nucleotide pyrophosphatase; This family consists of ...
 226-538 2.28e-107

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: 336.32  E-value: 2.28e-107
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958791576 226 LIIFSVDGFRASYMKKGsKVMPNIEKLRSCGTHAPYMRPVYPTKTFPNLYTLATGLYPESHGIVGNSMYDPVFDASFHLR 305
Cdd:pfam01663   1 LLVISLDGFRADYLDRF-ELTPNLAALAKEGVSAPNLTPVFPTLTFPNHYTLVTGLYPGSHGIVGNTFYDPKTGEYLVFV 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958791576 306 GREKFNHRWWGGQPLWITATKQGVRAGTFFW----------------------SVSIPHERRILTIL--QWLSLPD---- 357
Cdd:pfam01663  80 ISDPEDPRWWQGEPIWDTAAKAGVRAAALFWpgsevdystyygtpprylkddyNNSVPFEDRVDTAVlqTWLDLPFadva 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958791576 358 NERPSVYAFYSEQPDFSGHKYGPFGPEMTNPLREIDKTVGQLMDGLKQLRLHRCVNVIFVGDHGMEDVTCDRTEFLSNYL 437
Cdd:pfam01663 160 AERPDLLLVYLEEPDYAGHRYGPDSPEVEDALRRVDRAIGDLLEALDERGLFEDTNVIVVSDHGMTPVSDDKVIFLNDYL 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958791576 438 TNVDDITLV-PGTLGRIRAKSIN-------NSKYDPKTIIANLTC--KKPDQHFKPYMKQHLPKRLHYanNRRIEDIHLL 507
Cdd:pfam01663 240 REKGLLHLVdGGPVVAIYPKARElghvppgEVEEVYAELKEKLLGlrIQDGEHLAVYLKEEIPGRLHY--NPRIPDLVLV 317

                         330       340       350
                  ....*....|....*....|....*....|.
gi 1958791576 508 VDRRWHVARKpldvyKKPSGKCFFQGDHGFD 538
Cdd:pfam01663 318 ADPGWYITGK-----DGGDKEAAIHGTHGYD 343
Enpp cd16018
Ectonucleotide pyrophosphatase/phosphodiesterase, also called autotaxin; Ecto-nucleotide ...
 224-578 2.01e-97

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: 306.82  E-value: 2.01e-97
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958791576 224 PPLIIFSVDGFRASYMKKGsKVMPNIEKLRSCGTHAPYMRPVYPTKTFPNLYTLATGLYPESHGIVGNSMYDPVFDASFH 303
Cdd:cd16018     1 PPLIVISIDGFRWDYLDRA-GLTPNLKRLAEEGVRAKYVKPVFPTLTFPNHYSIVTGLYPESHGIVGNYFYDPKTNEEFS 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958791576 304 lRGREKFNHRWWGGQPLWITATKQGVRAGTFFWSVS------------------------IPHERRILTILQWLslpDNE 359
Cdd:cd16018    80 -DSDWVWDPWWIGGEPIWVTAEKAGLKTASYFWPGSevaiigynptpiplggywqpyndsFPFEERVDTILEWL---DLE 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958791576 360 RPSVYAFYSEQPDFSGHKYGPFGPEMTNPLREIDKTVGQLMDGLKQLRLHRCVNVIFVGDHGMEDVtcdrteflsnyltn 439
Cdd:cd16018   156 RPDLILLYFEEPDSAGHKYGPDSPEVNEALKRVDRRLGYLIEALKERGLLDDTNIIVVSDHGMTDV-------------- 221

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958791576 440 vdditlvpgtlgriraksinnskydpktiianltckkpdqhfkpymkqhlpkrlhyannrriedihllvdrrwhvarkpl 519
Cdd:cd16018       --------------------------------------------------------------------------------

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1958791576 520 dvykkpsgkcffqGDHGFDNKVNSMQTVFVGYGPTFKYRTKVPPFENIELYNVMCDLLG 578
Cdd:cd16018   222 -------------GTHGYDNELPDMRAIFIARGPAFKKGKKLGPFRNVDIYPLMCNLLG 267
NUC smart00477
DNA/RNA non-specific endonuclease; prokaryotic and eukaryotic double- and single-stranded DNA ...
 700-930 2.60e-76

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: 248.43  E-value: 2.60e-76
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958791576  700 HTDFESGYSEIFLMPLWTSYTISKQAEVSSiPEHLTNCVRPDVRVSPGFSQNCLAYKNDKqMSYGFLFPPYL-SSSPEAK 778
Cdd:smart00477   1 RNQYVLGYNRSTRMPNWVAYHITGELLTSG-AERKSDCFKPDTRIPEKFQAKLSDYKGSG-YDRGHLAPAADhKFSSEAM 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958791576  779 YDAFLVTNMVPMYPAFKRV-WAYFQRVLVKKYASERNGVNVISGPIFDYNYDGLRDTEdEIKQYVEGS-SIPVPTHYYSI 856
Cdd:smart00477  79 ADTFYLSNIVPQYPDFNRGaWAYLEDYLRKLTASERNGVYVVSGPLFLPNYDGKGDKL-EVKYQVIGSkNVAIPTHFFKV 157

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958791576  857 ITSCLDftqpadkcDGPLSVSSFILPHRPDNDESCnssedeskwveelMKMHTARVRDIEHLTGLDFYRKTSRS 930
Cdd:smart00477 158 ITAEKA--------DSYLEVAAFILPNDPINDESP-------------LTNFRVPVDEIERLTGLDFFRNLDPA 210
NUC cd00091
DNA/RNA non-specific endonuclease; prokaryotic and eukaryotic double- and single-stranded DNA ...
 682-940 8.29e-71

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: 234.57  E-value: 8.29e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958791576 682 LLYGRPAVLYRTsyDILYHTDFESGYSEIFLMPLWTSYTISKQAEvSSIPEHLTNCVRPDVRVSPGFSQNCLAYKNDKQM 761
Cdd:cd00091     1 LQYGRPGVLADT--EVLSYTHYVLSYNRATRLPLWVAEHIDKEDL-GKNVDRKYDQFKQDPRIPPLFSATNSDYKGSGSL 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958791576 762 SYGFLFPPYLSS-SPEAKYDAFLVTNMVPMYPAF-KRVWAYFQRVLVKKYASERNGVNVISGPIFDYNYDGLRDTeDEIK 839
Cdd:cd00091    78 DRGHLAPAADPVwSQDAQDATFYLTNMAPQVQGFnQGNWAYLEDYLRDLAASEGKDVYVVTGPLFLPDLDGDGGS-YLST 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958791576 840 QYVEGSSIPVPTHYYSIITSCLDftqpadkcDGPLSVSSFILPHRPDNDESCNSSedeskWVEELMKMHtarVRDIEHLT 919
Cdd:cd00091   157 QVINNGKVAVPTHFWKVIIDEKA--------PGNLSVGAFVLPNNNPHDTLEFIL-----CVEKTFQVP---VASVEKAT 220

                         250       260
                  ....*....|....*....|.
gi 1958791576 920 GLDFYRKTSRSYSEILTLKTY 940
Cdd:cd00091   221 GLSFFCNVPDSVSAVLELKKK 241
AtaC COG1524
c-di-AMP phosphodiesterase AtaC or nucleotide pyrophosphatase, AlkP superfamily [Signal ...
 223-580 8.45e-62

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


Pssm-ID: 441133 [Multi-domain]  Cd Length: 370  Bit Score: 214.61  E-value: 8.45e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958791576 223 RPPLIIFSVDGFRASYMKKGSkvMPNIEKLRSCGTHAPYMRPVYPTKTFPNLYTLATGLYPESHGIVGNSMYDPVFDA-S 301
Cdd:COG1524    23 AKKVVLILVDGLRADLLERAH--APNLAALAARGVYARPLTSVFPSTTAPAHTTLLTGLYPGEHGIVGNGWYDPELGRvV 100

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958791576 302 FHLRGREKFNH--RWWGGQPLWITATKQGVRAGTFFWSVS---------IPH------------ERRILTILQWLSLPDN 358
Cdd:COG1524   101 NSLSWVEDGFGsnSLLPVPTIFERARAAGLTTAAVFWPSFegsglidaaRPYpydgrkpllgnpAADRWIAAAALELLRE 180

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958791576 359 ERPSVYAFYSEQPDFSGHKYGPFGPEMTNPLREIDKTVGQLMDGLKQLRLHRCVNVIFVGDHGMEDVTcdrTEFLSNYLT 438
Cdd:COG1524   181 GRPDLLLVYLPDLDYAGHRYGPDSPEYRAALREVDAALGRLLDALKARGLYEGTLVIVTADHGMVDVP---PDIDLNRLR 257

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958791576 439 NVDDITLVPGTLGRIRAKSINNSKydpktIIANLtckkpDQHFKPYMKQHLpKRLHYANNrRIEDIHLLVDRRWHVARKP 518
Cdd:COG1524   258 LAGLLAVRAGESAHLYLKDGADAE-----VRALL-----GLPARVLTREEL-AAGHFGPH-RIGDLVLVAKPGWALDAPL 325

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958791576 519 LdvykkpsgkcffqGDHGFDNKvNSMQTVFVGYGPTFKyrtkvPPFENIELYNVMCDLLGLK 580
Cdd:COG1524   326 K-------------GSHGGLPD-EEMRVPLLASGPGFR-----PGVRNVDVAPTIARLLGLP 368
NUC1 COG1864
DNA/RNA endonuclease G, NUC1 [Nucleotide transport and metabolism];
679-923 7.66e-20

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


Pssm-ID: 441469  Cd Length: 238  Bit Score: 89.58  E-value: 7.66e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958791576 679 ERHLLYGRPAVLYRTSYD--ILYHTDFESGYSEIFLMPLWTSYTISKQAEVSSIPEhlTNCVRPDVRVSPGFSqnclA-- 754
Cdd:COG1864     7 PDFLLLGLPSLARALSTNnyLLCYTGYSLSYNESRRTPNWVAYNLDGSWLGKSLKR--SDDFRPDPRLPSGYR----Atl 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958791576 755 --YKN---DKqmsyGFLFPPY-LSSSPEAKYDAFLVTNMVPMYPAFKR-VWAYFQRVlVKKYASERNGVNVISGPIFDyn 827
Cdd:COG1864    81 adYTGsgyDR----GHLAPSAdRTFSKEANSETFLMTNISPQAPDFNQgIWARLENY-VRDLARKGGEVYVVTGPVFD-- 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958791576 828 ydglrdtEDEIKQYVEGSsIPVPTHYYSIItscLDftqpADKCDGPLSVSSFILPHRPDNDEScnssedeskwveelmkM 907
Cdd:COG1864   154 -------DGDLKTIGSGG-VAVPTAFWKVV---VD----PDKNTGTLRAIAFLLPNTALSSGP----------------L 202

                         250
                  ....*....|....*...
gi 1958791576 908 HTARV--RDIEHLTGLDF 923
Cdd:COG1864   203 RTYQVsvDEIEKLTGLDF 220
SO smart00201
Somatomedin B -like domains; Somatomedin-B is a peptide, proteolytically excised from ...
 117-158 2.46e-14

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: 67.78  E-value: 2.46e-14
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|..
gi 1958791576  117 GSCKGRCFELQEVGPPdCRCDNLCKSYSSCCHDFDELCLKTA 158
Cdd:smart00201   3 GSCKGRCGESFNEGNA-CRCDALCLSYGDCCTDYESVCKKEV 43
SO smart00201
Somatomedin B -like domains; Somatomedin-B is a peptide, proteolytically excised from ...
 159-202 2.99e-14

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: 67.40  E-value: 2.99e-14
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 1958791576  159 RGWECtKDRCGEVRNEENACHCSEDCLSRGDCCTNYQVVCKGES 202
Cdd:smart00201   1 AIGSC-KGRCGESFNEGNACRCDALCLSYGDCCTDYESVCKKEV 43
Endonuclease_NS pfam01223
DNA/RNA non-specific endonuclease;
683-923 9.01e-13

DNA/RNA non-specific endonuclease;


Pssm-ID: 460120  Cd Length: 220  Bit Score: 68.62  E-value: 9.01e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958791576 683 LYGRPAVLYRTSYDILYhtdfeSGYSEIflmPLWTSYTISKQAEVSSIPEHltncvRPDVRVSPGFSQNCLAYKNDKQMS 762
Cdd:pfam01223  12 GSGSDVVLFYKYYSLCY-----DRRTRR---ALWVAHHLTGASLAGSKGRR-----RPGFKQDPRIPGAYFRTLYTDYTG 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958791576 763 YGF----LFPPY-LSSSPEAKYDAFLVTNMVPMYPAFKR-VWAYFQRvLVKKYASERNG-VNVISGPIFDYNYDglrdte 835
Cdd:pfam01223  79 SGFdrghLAPAAdFKFSAGANAATFNFTNIAPQWAGFNQgNWAYLEN-YVRDLAARHNNsVYVYTGPLYVPNLL------ 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958791576 836 deikqyvEGSSIPVPTHYYSIITScldftqPADKCDGPLSVSSFILPHrpdndESCNSSEDESKWVEElmkmhtarVRDI 915
Cdd:pfam01223 152 -------DKNKVAVPTHFWKVILS------EDGDGGGGLNAPAFVLPN-----KYILDDGPLRTFQVP--------VDEL 205


                  ....*...
gi 1958791576 916 EHLTGLDF 923
Cdd:pfam01223 206 ERLTGLDF 213
Somatomedin_B pfam01033
Somatomedin B domain;
161-201 3.65e-12

Somatomedin B domain;


Pssm-ID: 460034  Cd Length: 40  Bit Score: 61.55  E-value: 3.65e-12
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 1958791576 161 WECtKDRCGEVRNEENACHCSEDCLSRGDCCTNYQVVCKGE 201
Cdd:pfam01033   1 ESC-KGRCGESFDRGRLCQCDDDCVKYGDCCPDYESLCLGE 40
Somatomedin_B pfam01033
Somatomedin B domain;
117-157 2.46e-11

Somatomedin B domain;


Pssm-ID: 460034  Cd Length: 40  Bit Score: 59.24  E-value: 2.46e-11
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 1958791576 117 GSCKGRCFELQEVGPPdCRCDNLCKSYSSCCHDFDELCLKT 157
Cdd:pfam01033   1 ESCKGRCGESFDRGRL-CQCDDDCVKYGDCCPDYESLCLGE 40
PTZ00259 PTZ00259
endonuclease G; Provisional
 741-926 6.97e-05

endonuclease G; Provisional


Pssm-ID: 240335 [Multi-domain]  Cd Length: 434  Bit Score: 46.39  E-value: 6.97e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958791576 741 DVRVSPGFSQNCLAYKnDKQMSYGFLFPP-YLSSSPEAKYDAFLVT-NMVPMYPAFKRV-W---AYFQRVLVKKYAserN 814
Cdd:PTZ00259  159 DPTVPEAFRAENKDYT-GSGYSRGHLAAAgFHKASQTAMDDTFLLSaNIVPQDLTNNAGdWlrlENLTRKLAREYE---V 234

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958791576 815 GVNVISGPIFDYNYdglRDTEDEIKQYVEGSSIP-------------------------VPTHYYSIITscldftqpADK 869
Cdd:PTZ00259  235 GVYVVSGPLFVPRY---MREKLRKWRLAEPSEIHkpdspadktpkkvvtyevigdnnvaVPTHLFKVIL--------AEK 303

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1958791576 870 CDG-PLSVSSFILPHRPdndescnssedESKwvEELMKMHTARVRDIEHLTGLDFYRK 926
Cdd:PTZ00259  304 NDGpPHEVAAFLMPNEP-----------ISK--EKPLTAYQVPLEEIEKLTGLQFFPK 348
 
Name Accession Description Interval E-value
Phosphodiest pfam01663
Type I phosphodiesterase / nucleotide pyrophosphatase; This family consists of ...
 226-538 2.28e-107

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: 336.32  E-value: 2.28e-107
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958791576 226 LIIFSVDGFRASYMKKGsKVMPNIEKLRSCGTHAPYMRPVYPTKTFPNLYTLATGLYPESHGIVGNSMYDPVFDASFHLR 305
Cdd:pfam01663   1 LLVISLDGFRADYLDRF-ELTPNLAALAKEGVSAPNLTPVFPTLTFPNHYTLVTGLYPGSHGIVGNTFYDPKTGEYLVFV 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958791576 306 GREKFNHRWWGGQPLWITATKQGVRAGTFFW----------------------SVSIPHERRILTIL--QWLSLPD---- 357
Cdd:pfam01663  80 ISDPEDPRWWQGEPIWDTAAKAGVRAAALFWpgsevdystyygtpprylkddyNNSVPFEDRVDTAVlqTWLDLPFadva 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958791576 358 NERPSVYAFYSEQPDFSGHKYGPFGPEMTNPLREIDKTVGQLMDGLKQLRLHRCVNVIFVGDHGMEDVTCDRTEFLSNYL 437
Cdd:pfam01663 160 AERPDLLLVYLEEPDYAGHRYGPDSPEVEDALRRVDRAIGDLLEALDERGLFEDTNVIVVSDHGMTPVSDDKVIFLNDYL 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958791576 438 TNVDDITLV-PGTLGRIRAKSIN-------NSKYDPKTIIANLTC--KKPDQHFKPYMKQHLPKRLHYanNRRIEDIHLL 507
Cdd:pfam01663 240 REKGLLHLVdGGPVVAIYPKARElghvppgEVEEVYAELKEKLLGlrIQDGEHLAVYLKEEIPGRLHY--NPRIPDLVLV 317

                         330       340       350
                  ....*....|....*....|....*....|.
gi 1958791576 508 VDRRWHVARKpldvyKKPSGKCFFQGDHGFD 538
Cdd:pfam01663 318 ADPGWYITGK-----DGGDKEAAIHGTHGYD 343
Enpp cd16018
Ectonucleotide pyrophosphatase/phosphodiesterase, also called autotaxin; Ecto-nucleotide ...
 224-578 2.01e-97

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: 306.82  E-value: 2.01e-97
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958791576 224 PPLIIFSVDGFRASYMKKGsKVMPNIEKLRSCGTHAPYMRPVYPTKTFPNLYTLATGLYPESHGIVGNSMYDPVFDASFH 303
Cdd:cd16018     1 PPLIVISIDGFRWDYLDRA-GLTPNLKRLAEEGVRAKYVKPVFPTLTFPNHYSIVTGLYPESHGIVGNYFYDPKTNEEFS 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958791576 304 lRGREKFNHRWWGGQPLWITATKQGVRAGTFFWSVS------------------------IPHERRILTILQWLslpDNE 359
Cdd:cd16018    80 -DSDWVWDPWWIGGEPIWVTAEKAGLKTASYFWPGSevaiigynptpiplggywqpyndsFPFEERVDTILEWL---DLE 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958791576 360 RPSVYAFYSEQPDFSGHKYGPFGPEMTNPLREIDKTVGQLMDGLKQLRLHRCVNVIFVGDHGMEDVtcdrteflsnyltn 439
Cdd:cd16018   156 RPDLILLYFEEPDSAGHKYGPDSPEVNEALKRVDRRLGYLIEALKERGLLDDTNIIVVSDHGMTDV-------------- 221

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958791576 440 vdditlvpgtlgriraksinnskydpktiianltckkpdqhfkpymkqhlpkrlhyannrriedihllvdrrwhvarkpl 519
Cdd:cd16018       --------------------------------------------------------------------------------

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1958791576 520 dvykkpsgkcffqGDHGFDNKVNSMQTVFVGYGPTFKYRTKVPPFENIELYNVMCDLLG 578
Cdd:cd16018   222 -------------GTHGYDNELPDMRAIFIARGPAFKKGKKLGPFRNVDIYPLMCNLLG 267
NUC smart00477
DNA/RNA non-specific endonuclease; prokaryotic and eukaryotic double- and single-stranded DNA ...
 700-930 2.60e-76

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: 248.43  E-value: 2.60e-76
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958791576  700 HTDFESGYSEIFLMPLWTSYTISKQAEVSSiPEHLTNCVRPDVRVSPGFSQNCLAYKNDKqMSYGFLFPPYL-SSSPEAK 778
Cdd:smart00477   1 RNQYVLGYNRSTRMPNWVAYHITGELLTSG-AERKSDCFKPDTRIPEKFQAKLSDYKGSG-YDRGHLAPAADhKFSSEAM 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958791576  779 YDAFLVTNMVPMYPAFKRV-WAYFQRVLVKKYASERNGVNVISGPIFDYNYDGLRDTEdEIKQYVEGS-SIPVPTHYYSI 856
Cdd:smart00477  79 ADTFYLSNIVPQYPDFNRGaWAYLEDYLRKLTASERNGVYVVSGPLFLPNYDGKGDKL-EVKYQVIGSkNVAIPTHFFKV 157

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958791576  857 ITSCLDftqpadkcDGPLSVSSFILPHRPDNDESCnssedeskwveelMKMHTARVRDIEHLTGLDFYRKTSRS 930
Cdd:smart00477 158 ITAEKA--------DSYLEVAAFILPNDPINDESP-------------LTNFRVPVDEIERLTGLDFFRNLDPA 210
NUC cd00091
DNA/RNA non-specific endonuclease; prokaryotic and eukaryotic double- and single-stranded DNA ...
 682-940 8.29e-71

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: 234.57  E-value: 8.29e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958791576 682 LLYGRPAVLYRTsyDILYHTDFESGYSEIFLMPLWTSYTISKQAEvSSIPEHLTNCVRPDVRVSPGFSQNCLAYKNDKQM 761
Cdd:cd00091     1 LQYGRPGVLADT--EVLSYTHYVLSYNRATRLPLWVAEHIDKEDL-GKNVDRKYDQFKQDPRIPPLFSATNSDYKGSGSL 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958791576 762 SYGFLFPPYLSS-SPEAKYDAFLVTNMVPMYPAF-KRVWAYFQRVLVKKYASERNGVNVISGPIFDYNYDGLRDTeDEIK 839
Cdd:cd00091    78 DRGHLAPAADPVwSQDAQDATFYLTNMAPQVQGFnQGNWAYLEDYLRDLAASEGKDVYVVTGPLFLPDLDGDGGS-YLST 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958791576 840 QYVEGSSIPVPTHYYSIITSCLDftqpadkcDGPLSVSSFILPHRPDNDESCNSSedeskWVEELMKMHtarVRDIEHLT 919
Cdd:cd00091   157 QVINNGKVAVPTHFWKVIIDEKA--------PGNLSVGAFVLPNNNPHDTLEFIL-----CVEKTFQVP---VASVEKAT 220

                         250       260
                  ....*....|....*....|.
gi 1958791576 920 GLDFYRKTSRSYSEILTLKTY 940
Cdd:cd00091   221 GLSFFCNVPDSVSAVLELKKK 241
AtaC COG1524
c-di-AMP phosphodiesterase AtaC or nucleotide pyrophosphatase, AlkP superfamily [Signal ...
 223-580 8.45e-62

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


Pssm-ID: 441133 [Multi-domain]  Cd Length: 370  Bit Score: 214.61  E-value: 8.45e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958791576 223 RPPLIIFSVDGFRASYMKKGSkvMPNIEKLRSCGTHAPYMRPVYPTKTFPNLYTLATGLYPESHGIVGNSMYDPVFDA-S 301
Cdd:COG1524    23 AKKVVLILVDGLRADLLERAH--APNLAALAARGVYARPLTSVFPSTTAPAHTTLLTGLYPGEHGIVGNGWYDPELGRvV 100

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958791576 302 FHLRGREKFNH--RWWGGQPLWITATKQGVRAGTFFWSVS---------IPH------------ERRILTILQWLSLPDN 358
Cdd:COG1524   101 NSLSWVEDGFGsnSLLPVPTIFERARAAGLTTAAVFWPSFegsglidaaRPYpydgrkpllgnpAADRWIAAAALELLRE 180

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958791576 359 ERPSVYAFYSEQPDFSGHKYGPFGPEMTNPLREIDKTVGQLMDGLKQLRLHRCVNVIFVGDHGMEDVTcdrTEFLSNYLT 438
Cdd:COG1524   181 GRPDLLLVYLPDLDYAGHRYGPDSPEYRAALREVDAALGRLLDALKARGLYEGTLVIVTADHGMVDVP---PDIDLNRLR 257

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958791576 439 NVDDITLVPGTLGRIRAKSINNSKydpktIIANLtckkpDQHFKPYMKQHLpKRLHYANNrRIEDIHLLVDRRWHVARKP 518
Cdd:COG1524   258 LAGLLAVRAGESAHLYLKDGADAE-----VRALL-----GLPARVLTREEL-AAGHFGPH-RIGDLVLVAKPGWALDAPL 325

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958791576 519 LdvykkpsgkcffqGDHGFDNKvNSMQTVFVGYGPTFKyrtkvPPFENIELYNVMCDLLGLK 580
Cdd:COG1524   326 K-------------GSHGGLPD-EEMRVPLLASGPGFR-----PGVRNVDVAPTIARLLGLP 368
ALP_like cd00016
alkaline phosphatases and sulfatases; This family includes alkaline phosphatases and ...
 224-447 4.85e-48

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: 171.06  E-value: 4.85e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958791576 224 PPLIIFSVDGFRASYMKKGSKVM---PNIEKLRSCGTHApYMRPVYP-TKTFPNLYTLATGLYPESHGIVGNSMYDPvfd 299
Cdd:cd00016     1 KHVVLIVLDGLGADDLGKAGNPApttPNLKRLASEGATF-NFRSVSPpTSSAPNHAALLTGAYPTLHGYTGNGSADP--- 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958791576 300 asfhlRGREKFNHRWWGGQPLWITATKQGVRAGTFFwsvsipherrILTILQWLSlpdNERPSVYAFYSEQPDFSGHKYG 379
Cdd:cd00016    77 -----ELPSRAAGKDEDGPTIPELLKQAGYRTGVIG----------LLKAIDETS---KEKPFVLFLHFDGPDGPGHAYG 138

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958791576 380 PFGPEMTNPLREIDKTVGQLMDGLKQLRLHRCVNVIFVGDHGMEDVTCDRTEFLSNYLTNVDDITLVP 447
Cdd:cd00016   139 PNTPEYYDAVEEIDERIGKVLDALKKAGDADDTVIIVTADHGGIDKGHGGDPKADGKADKSHTGMRVP 206
Endonuclease_NS smart00892
DNA/RNA non-specific endonuclease; A family of bacterial and eukaryotic endonucleases share ...
 700-929 9.63e-45

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: 160.27  E-value: 9.63e-45
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958791576  700 HTDFESGYSEIFLMPLWTSYTISKQAEVSSIPEHLTNCVRPDVRVSPGFSQNCLAYKNDKQMSYGFLFPPYLS-SSPEAK 778
Cdd:smart00892   1 YKHYALCYDERRRLPLWVAYHLTGSTRQGKNTGRKRPWFKPDGWHLPAIFQAVNSDYTGSGYDRGHLAPAADHgVSQEAM 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958791576  779 YDAFLVTNMVPMYPAFKR-VWAYFQRVLVKKYASERNGVNVISGPIFDYNYDGLRdtedeikqyvegssIPVPTHYYSII 857
Cdd:smart00892  81 AATFYLTNIVPQTAGFNQgNWNRLENYVRKLLAKNKDTVYVVTGPIYLPTLPDNN--------------VAVPSHFWKVI 146

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958791576  858 TSCldftqpaDKCDGPLSVSSFILPHRPDNDescnssedeskwvEELMKMHTARVRDIEHLTGLDFYRKTSR 929
Cdd:smart00892 147 LSE-------DGSNGGLAAIAFNLPNAPINE-------------DYPLCEFQVPVDNIERLTGLDFFCGLPD 198
NUC1 COG1864
DNA/RNA endonuclease G, NUC1 [Nucleotide transport and metabolism];
679-923 7.66e-20

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


Pssm-ID: 441469  Cd Length: 238  Bit Score: 89.58  E-value: 7.66e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958791576 679 ERHLLYGRPAVLYRTSYD--ILYHTDFESGYSEIFLMPLWTSYTISKQAEVSSIPEhlTNCVRPDVRVSPGFSqnclA-- 754
Cdd:COG1864     7 PDFLLLGLPSLARALSTNnyLLCYTGYSLSYNESRRTPNWVAYNLDGSWLGKSLKR--SDDFRPDPRLPSGYR----Atl 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958791576 755 --YKN---DKqmsyGFLFPPY-LSSSPEAKYDAFLVTNMVPMYPAFKR-VWAYFQRVlVKKYASERNGVNVISGPIFDyn 827
Cdd:COG1864    81 adYTGsgyDR----GHLAPSAdRTFSKEANSETFLMTNISPQAPDFNQgIWARLENY-VRDLARKGGEVYVVTGPVFD-- 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958791576 828 ydglrdtEDEIKQYVEGSsIPVPTHYYSIItscLDftqpADKCDGPLSVSSFILPHRPDNDEScnssedeskwveelmkM 907
Cdd:COG1864   154 -------DGDLKTIGSGG-VAVPTAFWKVV---VD----PDKNTGTLRAIAFLLPNTALSSGP----------------L 202

                         250
                  ....*....|....*...
gi 1958791576 908 HTARV--RDIEHLTGLDF 923
Cdd:COG1864   203 RTYQVsvDEIEKLTGLDF 220
SO smart00201
Somatomedin B -like domains; Somatomedin-B is a peptide, proteolytically excised from ...
 117-158 2.46e-14

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: 67.78  E-value: 2.46e-14
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|..
gi 1958791576  117 GSCKGRCFELQEVGPPdCRCDNLCKSYSSCCHDFDELCLKTA 158
Cdd:smart00201   3 GSCKGRCGESFNEGNA-CRCDALCLSYGDCCTDYESVCKKEV 43
SO smart00201
Somatomedin B -like domains; Somatomedin-B is a peptide, proteolytically excised from ...
 159-202 2.99e-14

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: 67.40  E-value: 2.99e-14
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 1958791576  159 RGWECtKDRCGEVRNEENACHCSEDCLSRGDCCTNYQVVCKGES 202
Cdd:smart00201   1 AIGSC-KGRCGESFNEGNACRCDALCLSYGDCCTDYESVCKKEV 43
Endonuclease_NS pfam01223
DNA/RNA non-specific endonuclease;
683-923 9.01e-13

DNA/RNA non-specific endonuclease;


Pssm-ID: 460120  Cd Length: 220  Bit Score: 68.62  E-value: 9.01e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958791576 683 LYGRPAVLYRTSYDILYhtdfeSGYSEIflmPLWTSYTISKQAEVSSIPEHltncvRPDVRVSPGFSQNCLAYKNDKQMS 762
Cdd:pfam01223  12 GSGSDVVLFYKYYSLCY-----DRRTRR---ALWVAHHLTGASLAGSKGRR-----RPGFKQDPRIPGAYFRTLYTDYTG 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958791576 763 YGF----LFPPY-LSSSPEAKYDAFLVTNMVPMYPAFKR-VWAYFQRvLVKKYASERNG-VNVISGPIFDYNYDglrdte 835
Cdd:pfam01223  79 SGFdrghLAPAAdFKFSAGANAATFNFTNIAPQWAGFNQgNWAYLEN-YVRDLAARHNNsVYVYTGPLYVPNLL------ 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958791576 836 deikqyvEGSSIPVPTHYYSIITScldftqPADKCDGPLSVSSFILPHrpdndESCNSSEDESKWVEElmkmhtarVRDI 915
Cdd:pfam01223 152 -------DKNKVAVPTHFWKVILS------EDGDGGGGLNAPAFVLPN-----KYILDDGPLRTFQVP--------VDEL 205


                  ....*...
gi 1958791576 916 EHLTGLDF 923
Cdd:pfam01223 206 ERLTGLDF 213
Somatomedin_B pfam01033
Somatomedin B domain;
161-201 3.65e-12

Somatomedin B domain;


Pssm-ID: 460034  Cd Length: 40  Bit Score: 61.55  E-value: 3.65e-12
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 1958791576 161 WECtKDRCGEVRNEENACHCSEDCLSRGDCCTNYQVVCKGE 201
Cdd:pfam01033   1 ESC-KGRCGESFDRGRLCQCDDDCVKYGDCCPDYESLCLGE 40
Somatomedin_B pfam01033
Somatomedin B domain;
117-157 2.46e-11

Somatomedin B domain;


Pssm-ID: 460034  Cd Length: 40  Bit Score: 59.24  E-value: 2.46e-11
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 1958791576 117 GSCKGRCFELQEVGPPdCRCDNLCKSYSSCCHDFDELCLKT 157
Cdd:pfam01033   1 ESCKGRCGESFDRGRL-CQCDDDCVKYGDCCPDYESLCLGE 40
GPI_EPT_3 cd16023
GPI ethanolamine phosphate transferase 3, PIG-O; Ethanolamine phosphate transferase is ...
 375-424 2.70e-05

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


Pssm-ID: 293747  Cd Length: 289  Bit Score: 47.17  E-value: 2.70e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 1958791576 375 GHKYGPFGPEMTNPLREIDKTVGQLMDglkqlRLHRCVNVIFVGDHGMED 424
Cdd:cd16023   174 GHRYGPNHPEMARKLTQMDQFIRDIIE-----RLDDDTLLLVFGDHGMTE 218
PTZ00259 PTZ00259
endonuclease G; Provisional
 741-926 6.97e-05

endonuclease G; Provisional


Pssm-ID: 240335 [Multi-domain]  Cd Length: 434  Bit Score: 46.39  E-value: 6.97e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958791576 741 DVRVSPGFSQNCLAYKnDKQMSYGFLFPP-YLSSSPEAKYDAFLVT-NMVPMYPAFKRV-W---AYFQRVLVKKYAserN 814
Cdd:PTZ00259  159 DPTVPEAFRAENKDYT-GSGYSRGHLAAAgFHKASQTAMDDTFLLSaNIVPQDLTNNAGdWlrlENLTRKLAREYE---V 234

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958791576 815 GVNVISGPIFDYNYdglRDTEDEIKQYVEGSSIP-------------------------VPTHYYSIITscldftqpADK 869
Cdd:PTZ00259  235 GVYVVSGPLFVPRY---MREKLRKWRLAEPSEIHkpdspadktpkkvvtyevigdnnvaVPTHLFKVIL--------AEK 303

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1958791576 870 CDG-PLSVSSFILPHRPdndescnssedESKwvEELMKMHTARVRDIEHLTGLDFYRK 926
Cdd:PTZ00259  304 NDGpPHEVAAFLMPNEP-----------ISK--EKPLTAYQVPLEEIEKLTGLQFFPK 348
GPI_EPT_2 cd16024
GPI ethanolamine phosphate transferase 2; PIG-G; Ethanolamine phosphate transferase is ...
 375-424 7.56e-04

GPI ethanolamine phosphate transferase 2; PIG-G; 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: 293748 [Multi-domain]  Cd Length: 274  Bit Score: 42.55  E-value: 7.56e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 1958791576 375 GHKYGPFGPEMTNPLREIDKTVGQLMDGLKQLRLHRCVNVIFVGDHGMED 424
Cdd:cd16024   159 GHLEGPKSPLMPPKLKEMDDVIKRIYESLEEQSSNNPTLLVVCGDHGMTD 208
ARSA cd16158
Arylsulfatase A or cerebroside-sulfatase; Arylsulfatase A breaks down sulfatides, namely ...
 364-423 5.01e-03

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


Pssm-ID: 293777 [Multi-domain]  Cd Length: 479  Bit Score: 40.51  E-value: 5.01e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958791576 364 YAF-YSEQPDFSGHKY------GPFGpemtNPLREIDKTVGQLMDGLKQLRLHRCVNVIFVGDHGME 423
Cdd:cd16158   204 YAShHTHYPQFAGQKFagrssrGPFG----DALAELDGSVGELLQTLKENGIDNNTLVFFTSDNGPS 266
AP-SPAP cd16016
SPAP is a subclass of alkaline phosphatase (AP); Alkaline phosphatases are non-specific ...
 223-296 5.35e-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: 5.35e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958791576 223 RPPLIIF-SVDGFRASYM--------KKGSK-------VMPNieklrscgTHAPYMrpvyPTKTFPNLYTLATGLYPESH 286
Cdd:cd16016     1 RPKLVVGiVVDQMRADYLyryrdrfgEGGFKrllnegfVFEN--------AHYNYA----PTDTAPGHATIYTGTTPAIH 68

                          90
                  ....*....|
gi 1958791576 287 GIVGNSMYDP 296
Cdd:cd16016    69 GIIGNDWYDR 78
AP-SPAP cd16016
SPAP is a subclass of alkaline phosphatase (AP); Alkaline phosphatases are non-specific ...
 366-436 9.68e-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: 39.44  E-value: 9.68e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958791576 366 FYSeqPDFSGHKYGPFGPEMTNPLREIDKTVGQLMDGL-KQLRLhrcVNVIFV--GDHGmedvTCDRTEFLSNY 436
Cdd:cd16016   214 FSA--TDYIGHAFGPNSVEMEDTYLRLDRDLARLLDALdKKVGK---GNYLVFltADHG----AADNPEFLKDH 278
 
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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