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Conserved domains on  [gi|170650661|ref|NP_006199|]
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ectonucleotide pyrophosphatase/phosphodiesterase family member 1 [Homo sapiens]

Protein Classification

DNA/RNA non-specific endonuclease( domain architecture ID 12193410)

DNA/RNA non-specific endonuclease catalyzes the cleavage of dsRNA, ssRNA, ssDNA, dsDNA, as well as RNA/DNA hybrids

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 ...
212-538 2.53e-116

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: 359.04  E-value: 2.53e-116
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650661  212 TLLFSLDGFRAEYLHTWGgLLPVISKLKKCGTYTKNMRPVYPTKTFPNHYSIVTGLYPESHGIIDNKMYDPKMNASFSLK 291
Cdd:pfam01663   1 LLVISLDGFRADYLDRFE-LTPNLAALAKEGVSAPNLTPVFPTLTFPNHYTLVTGLYPGSHGIVGNTFYDPKTGEYLVFV 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650661  292 SKEKFNPEWYKGEPIWVTAKYQGLKSGTFFWPGSDVEI---NGIFPDIYKM-YNGSVPFEERILAVL--QWLQLPKD--- 362
Cdd:pfam01663  80 ISDPEDPRWWQGEPIWDTAAKAGVRAAALFWPGSEVDYstyYGTPPRYLKDdYNNSVPFEDRVDTAVlqTWLDLPFAdva 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650661  363 -ERPHFYTLYLEEPDSSGHSYGPVSSEVIKALQRVDGMVGMLMDGLKELNLHRCLNLILISDHGMEQGSCKKYIYLNKYL 441
Cdd:pfam01663 160 aERPDLLLVYLEEPDYAGHRYGPDSPEVEDALRRVDRAIGDLLEALDERGLFEDTNVIVVSDHGMTPVSDDKVIFLNDYL 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650661  442 GDVKNIKVI-YGPAARLRP-----SDVPDKYYSFNYEGIARNLSCR--EPNQHFKPYLKHFLPKRLHFakSDRIEPLTFY 513
Cdd:pfam01663 240 REKGLLHLVdGGPVVAIYPkarelGHVPPGEVEEVYAELKEKLLGLriQDGEHLAVYLKEEIPGRLHY--NPRIPDLVLV 317
                         330       340
                  ....*....|....*....|....*.
gi 170650661  514 LDPQWQLALNPSERKYC-GSGFHGSD 538
Cdd:pfam01663 318 ADPGWYITGKDGGDKEAaIHGTHGYD 343
NUC smart00477
DNA/RNA non-specific endonuclease; prokaryotic and eukaryotic double- and single-stranded DNA ...
676-907 8.85e-83

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: 265.38  E-value: 8.85e-83
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650661   676 QHQFMSGYSQDILMPLWTSYTVDRNDSFS-TEDFSNCLYQDFRIPLSPVHKCSFYKNNtKVSYGFLSPPQLNKNSSGIYS 754
Cdd:smart00477   1 RNQYVLGYNRSTRMPNWVAYHITGELLTSgAERKSDCFKPDTRIPEKFQAKLSDYKGS-GYDRGHLAPAADHKFSSEAMA 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650661   755 EALLTTNIVPMYQSF-QVIWRYFHDTLLRKYAEERNGVNVVSGPVFDFDYDGRCDSLEnlrQKRRVIRNQEILIPTHFFI 833
Cdd:smart00477  80 DTFYLSNIVPQYPDFnRGAWAYLEDYLRKLTASERNGVYVVSGPLFLPNYDGKGDKLE---VKYQVIGSKNVAIPTHFFK 156
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 170650661   834 VLTSCKDTSqtplhceNLDTLAFILPHRTDNSESCvhgkhdsswveelLMLHRARITDVEHITGLSFYQQRKEP 907
Cdd:smart00477 157 VITAEKADS-------YLEVAAFILPNDPINDESP-------------LTNFRVPVDEIERLTGLDFFRNLDPA 210
SO smart00201
Somatomedin B -like domains; Somatomedin-B is a peptide, proteolytically excised from ...
145-188 9.31e-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: 65.86  E-value: 9.31e-14
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 170650661   145 HIWTCnKFRCGEKRLTRSLCACSDDCKDKGDCCINYSSVCQGEK 188
Cdd:smart00201   1 AIGSC-KGRCGESFNEGNACRCDALCLSYGDCCTDYESVCKKEV 43
SO smart00201
Somatomedin B -like domains; Somatomedin-B is a peptide, proteolytically excised from ...
104-144 5.31e-12

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: 61.24  E-value: 5.31e-12
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|...
gi 170650661   104 EVKSCKGRCFERTFGN--CRCDAACVELGNCCLDYQETCIEPE 144
Cdd:smart00201   1 AIGSCKGRCGESFNEGnaCRCDALCLSYGDCCTDYESVCKKEV 43
 
Name Accession Description Interval E-value
Phosphodiest pfam01663
Type I phosphodiesterase / nucleotide pyrophosphatase; This family consists of ...
212-538 2.53e-116

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: 359.04  E-value: 2.53e-116
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650661  212 TLLFSLDGFRAEYLHTWGgLLPVISKLKKCGTYTKNMRPVYPTKTFPNHYSIVTGLYPESHGIIDNKMYDPKMNASFSLK 291
Cdd:pfam01663   1 LLVISLDGFRADYLDRFE-LTPNLAALAKEGVSAPNLTPVFPTLTFPNHYTLVTGLYPGSHGIVGNTFYDPKTGEYLVFV 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650661  292 SKEKFNPEWYKGEPIWVTAKYQGLKSGTFFWPGSDVEI---NGIFPDIYKM-YNGSVPFEERILAVL--QWLQLPKD--- 362
Cdd:pfam01663  80 ISDPEDPRWWQGEPIWDTAAKAGVRAAALFWPGSEVDYstyYGTPPRYLKDdYNNSVPFEDRVDTAVlqTWLDLPFAdva 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650661  363 -ERPHFYTLYLEEPDSSGHSYGPVSSEVIKALQRVDGMVGMLMDGLKELNLHRCLNLILISDHGMEQGSCKKYIYLNKYL 441
Cdd:pfam01663 160 aERPDLLLVYLEEPDYAGHRYGPDSPEVEDALRRVDRAIGDLLEALDERGLFEDTNVIVVSDHGMTPVSDDKVIFLNDYL 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650661  442 GDVKNIKVI-YGPAARLRP-----SDVPDKYYSFNYEGIARNLSCR--EPNQHFKPYLKHFLPKRLHFakSDRIEPLTFY 513
Cdd:pfam01663 240 REKGLLHLVdGGPVVAIYPkarelGHVPPGEVEEVYAELKEKLLGLriQDGEHLAVYLKEEIPGRLHY--NPRIPDLVLV 317
                         330       340
                  ....*....|....*....|....*.
gi 170650661  514 LDPQWQLALNPSERKYC-GSGFHGSD 538
Cdd:pfam01663 318 ADPGWYITGKDGGDKEAaIHGTHGYD 343
Enpp cd16018
Ectonucleotide pyrophosphatase/phosphodiesterase, also called autotaxin; Ecto-nucleotide ...
210-578 7.03e-113

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: 347.26  E-value: 7.03e-113
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650661 210 PPTLLFSLDGFRAEYLhTWGGLLPVISKLKKCGTYTKNMRPVYPTKTFPNHYSIVTGLYPESHGIIDNKMYDPKMNASFS 289
Cdd:cd16018    1 PPLIVISIDGFRWDYL-DRAGLTPNLKRLAEEGVRAKYVKPVFPTLTFPNHYSIVTGLYPESHGIVGNYFYDPKTNEEFS 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650661 290 lKSKEKFNPEWYKGEPIWVTAKYQGLKSGTFFWPGSDVEINGIFPD------IYKMYNGSVPFEERILAVLQWLQLpkdE 363
Cdd:cd16018   80 -DSDWVWDPWWIGGEPIWVTAEKAGLKTASYFWPGSEVAIIGYNPTpiplggYWQPYNDSFPFEERVDTILEWLDL---E 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650661 364 RPHFYTLYLEEPDSSGHSYGPVSSEVIKALQRVDGMVGMLMDGLKELNLHRCLNLILISDHGMeqgsckkyiylnkylgd 443
Cdd:cd16018  156 RPDLILLYFEEPDSAGHKYGPDSPEVNEALKRVDRRLGYLIEALKERGLLDDTNIIVVSDHGM----------------- 218
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650661 444 vknikviygpaarlrpSDVpdkyysfnyegiarnlscrepnqhfkpylkhflpkrlhfaksdriepltfyldpqwqlaln 523
Cdd:cd16018  219 ----------------TDV------------------------------------------------------------- 221
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 170650661 524 pserkycgsGFHGSDNVFSNMQALFVGYGPGFKHGIEADTFENIEVYNLMCDLLN 578
Cdd:cd16018  222 ---------GTHGYDNELPDMRAIFIARGPAFKKGKKLGPFRNVDIYPLMCNLLG 267
NUC smart00477
DNA/RNA non-specific endonuclease; prokaryotic and eukaryotic double- and single-stranded DNA ...
676-907 8.85e-83

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: 265.38  E-value: 8.85e-83
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650661   676 QHQFMSGYSQDILMPLWTSYTVDRNDSFS-TEDFSNCLYQDFRIPLSPVHKCSFYKNNtKVSYGFLSPPQLNKNSSGIYS 754
Cdd:smart00477   1 RNQYVLGYNRSTRMPNWVAYHITGELLTSgAERKSDCFKPDTRIPEKFQAKLSDYKGS-GYDRGHLAPAADHKFSSEAMA 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650661   755 EALLTTNIVPMYQSF-QVIWRYFHDTLLRKYAEERNGVNVVSGPVFDFDYDGRCDSLEnlrQKRRVIRNQEILIPTHFFI 833
Cdd:smart00477  80 DTFYLSNIVPQYPDFnRGAWAYLEDYLRKLTASERNGVYVVSGPLFLPNYDGKGDKLE---VKYQVIGSKNVAIPTHFFK 156
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 170650661   834 VLTSCKDTSqtplhceNLDTLAFILPHRTDNSESCvhgkhdsswveelLMLHRARITDVEHITGLSFYQQRKEP 907
Cdd:smart00477 157 VITAEKADS-------YLEVAAFILPNDPINDESP-------------LTNFRVPVDEIERLTGLDFFRNLDPA 210
AtaC COG1524
c-di-AMP phosphodiesterase AtaC or nucleotide pyrophosphatase, AlkP superfamily [Signal ...
204-579 1.42e-68

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


Pssm-ID: 441133 [Multi-domain]  Cd Length: 370  Bit Score: 232.72  E-value: 1.42e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650661 204 PAGFETPPTLLFSLDGFRAEYLHTwgGLLPVISKLKKCGTYTKNMRPVYPTKTFPNHYSIVTGLYPESHGIIDNKMYDP- 282
Cdd:COG1524   18 AAAPPAKKVVLILVDGLRADLLER--AHAPNLAALAARGVYARPLTSVFPSTTAPAHTTLLTGLYPGEHGIVGNGWYDPe 95
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650661 283 --KMNASFSLKSKEKFNPEWYKGEPIWVTAKYQGLKSGTFFWPGSDVE--INGIFPdiyKMYNGSVPF----EERILAVL 354
Cdd:COG1524   96 lgRVVNSLSWVEDGFGSNSLLPVPTIFERARAAGLTTAAVFWPSFEGSglIDAARP---YPYDGRKPLlgnpAADRWIAA 172
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650661 355 QWLQLPKDERPHFYTLYLEEPDSSGHSYGPVSSEVIKALQRVDGMVGMLMDGLKELNLHRCLNLILISDHGMeqGSCKKY 434
Cdd:COG1524  173 AALELLREGRPDLLLVYLPDLDYAGHRYGPDSPEYRAALREVDAALGRLLDALKARGLYEGTLVIVTADHGM--VDVPPD 250
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650661 435 IYLNKyLGDVKNIKVIYGPAARL--RPSDVPDKYYSFnyegiarnlscrepNQHFKPYLKHFLpKRLHFAkSDRIEPLTF 512
Cdd:COG1524  251 IDLNR-LRLAGLLAVRAGESAHLylKDGADAEVRALL--------------GLPARVLTREEL-AAGHFG-PHRIGDLVL 313
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 170650661 513 YLDPQWqlalnPSERKYCGSgfHGSDNvFSNMQALFVGYGPGFKHGieadtFENIEVYNLMCDLLNL 579
Cdd:COG1524  314 VAKPGW-----ALDAPLKGS--HGGLP-DEEMRVPLLASGPGFRPG-----VRNVDVAPTIARLLGL 367
NUC cd00091
DNA/RNA non-specific endonuclease; prokaryotic and eukaryotic double- and single-stranded DNA ...
657-917 6.73e-65

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: 218.01  E-value: 6.73e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650661 657 LPYGRPRVLQKEntiCLLSQHQFMSGYSQDILMPLWTSYTVDRND-SFSTEDFSNCLYQDFRIPLSPVHKCSFYKNNTKV 735
Cdd:cd00091    1 LQYGRPGVLADT---EVLSYTHYVLSYNRATRLPLWVAEHIDKEDlGKNVDRKYDQFKQDPRIPPLFSATNSDYKGSGSL 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650661 736 SYGFLSPPQLNKNSSGIYSEALLTTNIVPMYQ-SFQVIWRYFHDTLLRKYAEERNGVNVVSGPVFDFDYDGRCDSLENlr 814
Cdd:cd00091   78 DRGHLAPAADPVWSQDAQDATFYLTNMAPQVQgFNQGNWAYLEDYLRDLAASEGKDVYVVTGPLFLPDLDGDGGSYLS-- 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650661 815 qkRRVIRNQEILIPTHFFIVLTSCKDTSqtplhceNLDTLAFILPHRTDNSESCVHgkhdsSWVEELLMLHRARitdVEH 894
Cdd:cd00091  156 --TQVINNGKVAVPTHFWKVIIDEKAPG-------NLSVGAFVLPNNNPHDTLEFI-----LCVEKTFQVPVAS---VEK 218
                        250       260
                 ....*....|....*....|...
gi 170650661 895 ITGLSFYQQRKEPVSDILKLKTH 917
Cdd:cd00091  219 ATGLSFFCNVPDSVSAVLELKKK 241
NUC1 COG1864
DNA/RNA endonuclease G, NUC1 [Nucleotide transport and metabolism];
657-917 6.06e-17

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


Pssm-ID: 441469  Cd Length: 238  Bit Score: 81.10  E-value: 6.06e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650661 657 LPYGRP---RVLQKENTIclLSQHQFMSGYSQDILMPLWTSYTVDRNDSFSTEDFSNCLYQDFRIPLS-PVHKcSFYKNN 732
Cdd:COG1864   10 LLLGLPslaRALSTNNYL--LCYTGYSLSYNESRRTPNWVAYNLDGSWLGKSLKRSDDFRPDPRLPSGyRATL-ADYTGS 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650661 733 tkvsyGF----LSP---PQLNKNSsgiYSEALLTTNIVPMYQSF-QVIWRYFHDtLLRKYAEERNGVNVVSGPVFDfdyd 804
Cdd:COG1864   87 -----GYdrghLAPsadRTFSKEA---NSETFLMTNISPQAPDFnQGIWARLEN-YVRDLARKGGEVYVVTGPVFD---- 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650661 805 grcdslenlRQKRRVIRNQEILIPTHFF-IVLTSCKDTSqtplhceNLDTLAFILPHRTDNSEScvhgkhdsswveelLM 883
Cdd:COG1864  154 ---------DGDLKTIGSGGVAVPTAFWkVVVDPDKNTG-------TLRAIAFLLPNTALSSGP--------------LR 203
                        250       260       270
                 ....*....|....*....|....*....|....
gi 170650661 884 LHRARITDVEHITGLSFYQQRKEPVSDILKLKTH 917
Cdd:COG1864  204 TYQVSVDEIEKLTGLDFFPNLPDDLEAALEAKVD 237
SO smart00201
Somatomedin B -like domains; Somatomedin-B is a peptide, proteolytically excised from ...
145-188 9.31e-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: 65.86  E-value: 9.31e-14
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 170650661   145 HIWTCnKFRCGEKRLTRSLCACSDDCKDKGDCCINYSSVCQGEK 188
Cdd:smart00201   1 AIGSC-KGRCGESFNEGNACRCDALCLSYGDCCTDYESVCKKEV 43
SO smart00201
Somatomedin B -like domains; Somatomedin-B is a peptide, proteolytically excised from ...
104-144 5.31e-12

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: 61.24  E-value: 5.31e-12
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|...
gi 170650661   104 EVKSCKGRCFERTFGN--CRCDAACVELGNCCLDYQETCIEPE 144
Cdd:smart00201   1 AIGSCKGRCGESFNEGnaCRCDALCLSYGDCCTDYESVCKKEV 43
Endonuclease_NS pfam01223
DNA/RNA non-specific endonuclease;
673-900 5.62e-12

DNA/RNA non-specific endonuclease;


Pssm-ID: 460120  Cd Length: 220  Bit Score: 66.31  E-value: 5.62e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650661  673 LLSQHQFMSGYSQDILMPLWTSYTVD-----RNDSFSTEDFsnclYQDFRIPLSPVHKC-SFYKNNtKVSYGFLSPPQLN 746
Cdd:pfam01223  18 VLFYKYYSLCYDRRTRRALWVAHHLTgaslaGSKGRRRPGF----KQDPRIPGAYFRTLyTDYTGS-GFDRGHLAPAADF 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650661  747 KNSSGIYSEALLTTNIVPMYQSF-QVIWRYFHDtLLRKYAEERNG-VNVVSGPVFDFDYDGrcdslenlrqkrrvirNQE 824
Cdd:pfam01223  93 KFSAGANAATFNFTNIAPQWAGFnQGNWAYLEN-YVRDLAARHNNsVYVYTGPLYVPNLLD----------------KNK 155
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 170650661  825 ILIPTHFFIVLtsckdTSQTPLHCENLDTLAFILPHrtdnsESCVHGKHDSSWVEEllmlhrarITDVEHITGLSF 900
Cdd:pfam01223 156 VAVPTHFWKVI-----LSEDGDGGGGLNAPAFVLPN-----KYILDDGPLRTFQVP--------VDELERLTGLDF 213
Somatomedin_B pfam01033
Somatomedin B domain;
147-187 1.56e-11

Somatomedin B domain;


Pssm-ID: 460034  Cd Length: 40  Bit Score: 59.62  E-value: 1.56e-11
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 170650661  147 WTCnKFRCGEKRLTRSLCACSDDCKDKGDCCINYSSVCQGE 187
Cdd:pfam01033   1 ESC-KGRCGESFDRGRLCQCDDDCVKYGDCCPDYESLCLGE 40
Somatomedin_B pfam01033
Somatomedin B domain;
107-143 1.59e-09

Somatomedin B domain;


Pssm-ID: 460034  Cd Length: 40  Bit Score: 53.85  E-value: 1.59e-09
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 170650661  107 SCKGRCFERTFGN--CRCDAACVELGNCCLDYQETCIEP 143
Cdd:pfam01033   2 SCKGRCGESFDRGrlCQCDDDCVKYGDCCPDYESLCLGE 40
PTZ00259 PTZ00259
endonuclease G; Provisional
679-902 3.72e-06

endonuclease G; Provisional


Pssm-ID: 240335 [Multi-domain]  Cd Length: 434  Bit Score: 50.25  E-value: 3.72e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650661 679 FMSGYSQDILMPLWTSYTVDRNDSFSTE-----DFSNC-LYQDFRIPLspvhkcsfYKNNTKVSY-------GFLSPPQL 745
Cdd:PTZ00259 117 YVSSLNYERRIPNWVAEYIPYRGISVEAgekkaNRADCvFYADPTVPE--------AFRAENKDYtgsgysrGHLAAAGF 188
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650661 746 NKNSSGIYSEA-LLTTNIVPmyQSF---QVIWrYFHDTLLRKYAEER-NGVNVVSGPVF---DFDYDGRCDSLENLRQKR 817
Cdd:PTZ00259 189 HKASQTAMDDTfLLSANIVP--QDLtnnAGDW-LRLENLTRKLAREYeVGVYVVSGPLFvprYMREKLRKWRLAEPSEIH 265
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650661 818 R----------------VIRNQEILIPTHFFIVLTSCKDTSQTPLhcenldTLAFILPhrtdNSESCvhgkhdsswVEEL 881
Cdd:PTZ00259 266 KpdspadktpkkvvtyeVIGDNNVAVPTHLFKVILAEKNDGPPHE------VAAFLMP----NEPIS---------KEKP 326
                        250       260
                 ....*....|....*....|.
gi 170650661 882 LMLHRARITDVEHITGLSFYQ 902
Cdd:PTZ00259 327 LTAYQVPLEEIEKLTGLQFFP 347
 
Name Accession Description Interval E-value
Phosphodiest pfam01663
Type I phosphodiesterase / nucleotide pyrophosphatase; This family consists of ...
212-538 2.53e-116

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: 359.04  E-value: 2.53e-116
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650661  212 TLLFSLDGFRAEYLHTWGgLLPVISKLKKCGTYTKNMRPVYPTKTFPNHYSIVTGLYPESHGIIDNKMYDPKMNASFSLK 291
Cdd:pfam01663   1 LLVISLDGFRADYLDRFE-LTPNLAALAKEGVSAPNLTPVFPTLTFPNHYTLVTGLYPGSHGIVGNTFYDPKTGEYLVFV 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650661  292 SKEKFNPEWYKGEPIWVTAKYQGLKSGTFFWPGSDVEI---NGIFPDIYKM-YNGSVPFEERILAVL--QWLQLPKD--- 362
Cdd:pfam01663  80 ISDPEDPRWWQGEPIWDTAAKAGVRAAALFWPGSEVDYstyYGTPPRYLKDdYNNSVPFEDRVDTAVlqTWLDLPFAdva 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650661  363 -ERPHFYTLYLEEPDSSGHSYGPVSSEVIKALQRVDGMVGMLMDGLKELNLHRCLNLILISDHGMEQGSCKKYIYLNKYL 441
Cdd:pfam01663 160 aERPDLLLVYLEEPDYAGHRYGPDSPEVEDALRRVDRAIGDLLEALDERGLFEDTNVIVVSDHGMTPVSDDKVIFLNDYL 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650661  442 GDVKNIKVI-YGPAARLRP-----SDVPDKYYSFNYEGIARNLSCR--EPNQHFKPYLKHFLPKRLHFakSDRIEPLTFY 513
Cdd:pfam01663 240 REKGLLHLVdGGPVVAIYPkarelGHVPPGEVEEVYAELKEKLLGLriQDGEHLAVYLKEEIPGRLHY--NPRIPDLVLV 317
                         330       340
                  ....*....|....*....|....*.
gi 170650661  514 LDPQWQLALNPSERKYC-GSGFHGSD 538
Cdd:pfam01663 318 ADPGWYITGKDGGDKEAaIHGTHGYD 343
Enpp cd16018
Ectonucleotide pyrophosphatase/phosphodiesterase, also called autotaxin; Ecto-nucleotide ...
210-578 7.03e-113

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: 347.26  E-value: 7.03e-113
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650661 210 PPTLLFSLDGFRAEYLhTWGGLLPVISKLKKCGTYTKNMRPVYPTKTFPNHYSIVTGLYPESHGIIDNKMYDPKMNASFS 289
Cdd:cd16018    1 PPLIVISIDGFRWDYL-DRAGLTPNLKRLAEEGVRAKYVKPVFPTLTFPNHYSIVTGLYPESHGIVGNYFYDPKTNEEFS 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650661 290 lKSKEKFNPEWYKGEPIWVTAKYQGLKSGTFFWPGSDVEINGIFPD------IYKMYNGSVPFEERILAVLQWLQLpkdE 363
Cdd:cd16018   80 -DSDWVWDPWWIGGEPIWVTAEKAGLKTASYFWPGSEVAIIGYNPTpiplggYWQPYNDSFPFEERVDTILEWLDL---E 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650661 364 RPHFYTLYLEEPDSSGHSYGPVSSEVIKALQRVDGMVGMLMDGLKELNLHRCLNLILISDHGMeqgsckkyiylnkylgd 443
Cdd:cd16018  156 RPDLILLYFEEPDSAGHKYGPDSPEVNEALKRVDRRLGYLIEALKERGLLDDTNIIVVSDHGM----------------- 218
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650661 444 vknikviygpaarlrpSDVpdkyysfnyegiarnlscrepnqhfkpylkhflpkrlhfaksdriepltfyldpqwqlaln 523
Cdd:cd16018  219 ----------------TDV------------------------------------------------------------- 221
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 170650661 524 pserkycgsGFHGSDNVFSNMQALFVGYGPGFKHGIEADTFENIEVYNLMCDLLN 578
Cdd:cd16018  222 ---------GTHGYDNELPDMRAIFIARGPAFKKGKKLGPFRNVDIYPLMCNLLG 267
NUC smart00477
DNA/RNA non-specific endonuclease; prokaryotic and eukaryotic double- and single-stranded DNA ...
676-907 8.85e-83

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: 265.38  E-value: 8.85e-83
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650661   676 QHQFMSGYSQDILMPLWTSYTVDRNDSFS-TEDFSNCLYQDFRIPLSPVHKCSFYKNNtKVSYGFLSPPQLNKNSSGIYS 754
Cdd:smart00477   1 RNQYVLGYNRSTRMPNWVAYHITGELLTSgAERKSDCFKPDTRIPEKFQAKLSDYKGS-GYDRGHLAPAADHKFSSEAMA 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650661   755 EALLTTNIVPMYQSF-QVIWRYFHDTLLRKYAEERNGVNVVSGPVFDFDYDGRCDSLEnlrQKRRVIRNQEILIPTHFFI 833
Cdd:smart00477  80 DTFYLSNIVPQYPDFnRGAWAYLEDYLRKLTASERNGVYVVSGPLFLPNYDGKGDKLE---VKYQVIGSKNVAIPTHFFK 156
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 170650661   834 VLTSCKDTSqtplhceNLDTLAFILPHRTDNSESCvhgkhdsswveelLMLHRARITDVEHITGLSFYQQRKEP 907
Cdd:smart00477 157 VITAEKADS-------YLEVAAFILPNDPINDESP-------------LTNFRVPVDEIERLTGLDFFRNLDPA 210
AtaC COG1524
c-di-AMP phosphodiesterase AtaC or nucleotide pyrophosphatase, AlkP superfamily [Signal ...
204-579 1.42e-68

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


Pssm-ID: 441133 [Multi-domain]  Cd Length: 370  Bit Score: 232.72  E-value: 1.42e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650661 204 PAGFETPPTLLFSLDGFRAEYLHTwgGLLPVISKLKKCGTYTKNMRPVYPTKTFPNHYSIVTGLYPESHGIIDNKMYDP- 282
Cdd:COG1524   18 AAAPPAKKVVLILVDGLRADLLER--AHAPNLAALAARGVYARPLTSVFPSTTAPAHTTLLTGLYPGEHGIVGNGWYDPe 95
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650661 283 --KMNASFSLKSKEKFNPEWYKGEPIWVTAKYQGLKSGTFFWPGSDVE--INGIFPdiyKMYNGSVPF----EERILAVL 354
Cdd:COG1524   96 lgRVVNSLSWVEDGFGSNSLLPVPTIFERARAAGLTTAAVFWPSFEGSglIDAARP---YPYDGRKPLlgnpAADRWIAA 172
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650661 355 QWLQLPKDERPHFYTLYLEEPDSSGHSYGPVSSEVIKALQRVDGMVGMLMDGLKELNLHRCLNLILISDHGMeqGSCKKY 434
Cdd:COG1524  173 AALELLREGRPDLLLVYLPDLDYAGHRYGPDSPEYRAALREVDAALGRLLDALKARGLYEGTLVIVTADHGM--VDVPPD 250
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650661 435 IYLNKyLGDVKNIKVIYGPAARL--RPSDVPDKYYSFnyegiarnlscrepNQHFKPYLKHFLpKRLHFAkSDRIEPLTF 512
Cdd:COG1524  251 IDLNR-LRLAGLLAVRAGESAHLylKDGADAEVRALL--------------GLPARVLTREEL-AAGHFG-PHRIGDLVL 313
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 170650661 513 YLDPQWqlalnPSERKYCGSgfHGSDNvFSNMQALFVGYGPGFKHGieadtFENIEVYNLMCDLLNL 579
Cdd:COG1524  314 VAKPGW-----ALDAPLKGS--HGGLP-DEEMRVPLLASGPGFRPG-----VRNVDVAPTIARLLGL 367
NUC cd00091
DNA/RNA non-specific endonuclease; prokaryotic and eukaryotic double- and single-stranded DNA ...
657-917 6.73e-65

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: 218.01  E-value: 6.73e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650661 657 LPYGRPRVLQKEntiCLLSQHQFMSGYSQDILMPLWTSYTVDRND-SFSTEDFSNCLYQDFRIPLSPVHKCSFYKNNTKV 735
Cdd:cd00091    1 LQYGRPGVLADT---EVLSYTHYVLSYNRATRLPLWVAEHIDKEDlGKNVDRKYDQFKQDPRIPPLFSATNSDYKGSGSL 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650661 736 SYGFLSPPQLNKNSSGIYSEALLTTNIVPMYQ-SFQVIWRYFHDTLLRKYAEERNGVNVVSGPVFDFDYDGRCDSLENlr 814
Cdd:cd00091   78 DRGHLAPAADPVWSQDAQDATFYLTNMAPQVQgFNQGNWAYLEDYLRDLAASEGKDVYVVTGPLFLPDLDGDGGSYLS-- 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650661 815 qkRRVIRNQEILIPTHFFIVLTSCKDTSqtplhceNLDTLAFILPHRTDNSESCVHgkhdsSWVEELLMLHRARitdVEH 894
Cdd:cd00091  156 --TQVINNGKVAVPTHFWKVIIDEKAPG-------NLSVGAFVLPNNNPHDTLEFI-----LCVEKTFQVPVAS---VEK 218
                        250       260
                 ....*....|....*....|...
gi 170650661 895 ITGLSFYQQRKEPVSDILKLKTH 917
Cdd:cd00091  219 ATGLSFFCNVPDSVSAVLELKKK 241
Endonuclease_NS smart00892
DNA/RNA non-specific endonuclease; A family of bacterial and eukaryotic endonucleases share ...
677-901 4.18e-27

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: 109.42  E-value: 4.18e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650661   677 HQFMSGYSQDILMPLWTSYTVDR--NDSFSTEDFSNCLYQD-FRIPLSPVHKCSFYKNNtKVSYGFLSPPQLNKNSSGIY 753
Cdd:smart00892   2 KHYALCYDERRRLPLWVAYHLTGstRQGKNTGRKRPWFKPDgWHLPAIFQAVNSDYTGS-GYDRGHLAPAADHGVSQEAM 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650661   754 SEALLTTNIVPMYQSF-QVIWRYFHDTLLRKYAEERNGVNVVSGPVFDFDYDGRcdslenlrqkrrvirnqEILIPTHFF 832
Cdd:smart00892  81 AATFYLTNIVPQTAGFnQGNWNRLENYVRKLLAKNKDTVYVVTGPIYLPTLPDN-----------------NVAVPSHFW 143
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 170650661   833 IVLTSCKDTSqtplhcENLDTLAFILPHRTDNSescvhgkhDSSWVEellmlHRARITDVEHITGLSFY 901
Cdd:smart00892 144 KVILSEDGSN------GGLAAIAFNLPNAPINE--------DYPLCE-----FQVPVDNIERLTGLDFF 193
ALP_like cd00016
alkaline phosphatases and sulfatases; This family includes alkaline phosphatases and ...
210-456 9.37e-26

alkaline phosphatases and sulfatases; This family includes alkaline phosphatases and sulfatases. Alkaline phosphatases are non-specific phosphomonoesterases that catalyze the hydrolysis reaction via a phosphoseryl intermediate to produce inorganic phosphate and the corresponding alcohol, optimally at high pH. Alkaline phosphatase exists as a dimer, each monomer binding 2 zinc atoms and one magnesium atom, which are essential for enzymatic activity. Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. Both alkaline phosphatase and sulfatase are essential for human metabolism. Deficiency of individual enzyme cause genetic diseases.


Pssm-ID: 293732 [Multi-domain]  Cd Length: 237  Bit Score: 106.74  E-value: 9.37e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650661 210 PPTLLFSLDGFRAEYLHTWGG---LLPVISKLKKCGTYTkNMRPVYP-TKTFPNHYSIVTGLYPESHGIIDNKMYDPKMN 285
Cdd:cd00016    1 KHVVLIVLDGLGADDLGKAGNpapTTPNLKRLASEGATF-NFRSVSPpTSSAPNHAALLTGAYPTLHGYTGNGSADPELP 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650661 286 asfslkskEKFNPEWYKGEPIWVTAKYQGLKSGTFFwpgsdveingifpdiykmyngsvpfeerILAVLQWLQlpkDERP 365
Cdd:cd00016   80 --------SRAAGKDEDGPTIPELLKQAGYRTGVIG----------------------------LLKAIDETS---KEKP 120
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650661 366 HFYTLYLEEPDSSGHSYGPVSSEVIKALQRVDGMVGMLMDGLKELNLHRCLNLILISDHGMEQGSC----KKYIYLNKYL 441
Cdd:cd00016  121 FVLFLHFDGPDGPGHAYGPNTPEYYDAVEEIDERIGKVLDALKKAGDADDTVIIVTADHGGIDKGHggdpKADGKADKSH 200
                        250
                 ....*....|....*
gi 170650661 442 GDVKNIKVIYGPAAR 456
Cdd:cd00016  201 TGMRVPFIAYGPGVK 215
NUC1 COG1864
DNA/RNA endonuclease G, NUC1 [Nucleotide transport and metabolism];
657-917 6.06e-17

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


Pssm-ID: 441469  Cd Length: 238  Bit Score: 81.10  E-value: 6.06e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650661 657 LPYGRP---RVLQKENTIclLSQHQFMSGYSQDILMPLWTSYTVDRNDSFSTEDFSNCLYQDFRIPLS-PVHKcSFYKNN 732
Cdd:COG1864   10 LLLGLPslaRALSTNNYL--LCYTGYSLSYNESRRTPNWVAYNLDGSWLGKSLKRSDDFRPDPRLPSGyRATL-ADYTGS 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650661 733 tkvsyGF----LSP---PQLNKNSsgiYSEALLTTNIVPMYQSF-QVIWRYFHDtLLRKYAEERNGVNVVSGPVFDfdyd 804
Cdd:COG1864   87 -----GYdrghLAPsadRTFSKEA---NSETFLMTNISPQAPDFnQGIWARLEN-YVRDLARKGGEVYVVTGPVFD---- 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650661 805 grcdslenlRQKRRVIRNQEILIPTHFF-IVLTSCKDTSqtplhceNLDTLAFILPHRTDNSEScvhgkhdsswveelLM 883
Cdd:COG1864  154 ---------DGDLKTIGSGGVAVPTAFWkVVVDPDKNTG-------TLRAIAFLLPNTALSSGP--------------LR 203
                        250       260       270
                 ....*....|....*....|....*....|....
gi 170650661 884 LHRARITDVEHITGLSFYQQRKEPVSDILKLKTH 917
Cdd:COG1864  204 TYQVSVDEIEKLTGLDFFPNLPDDLEAALEAKVD 237
SO smart00201
Somatomedin B -like domains; Somatomedin-B is a peptide, proteolytically excised from ...
145-188 9.31e-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: 65.86  E-value: 9.31e-14
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 170650661   145 HIWTCnKFRCGEKRLTRSLCACSDDCKDKGDCCINYSSVCQGEK 188
Cdd:smart00201   1 AIGSC-KGRCGESFNEGNACRCDALCLSYGDCCTDYESVCKKEV 43
SO smart00201
Somatomedin B -like domains; Somatomedin-B is a peptide, proteolytically excised from ...
104-144 5.31e-12

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: 61.24  E-value: 5.31e-12
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|...
gi 170650661   104 EVKSCKGRCFERTFGN--CRCDAACVELGNCCLDYQETCIEPE 144
Cdd:smart00201   1 AIGSCKGRCGESFNEGnaCRCDALCLSYGDCCTDYESVCKKEV 43
Endonuclease_NS pfam01223
DNA/RNA non-specific endonuclease;
673-900 5.62e-12

DNA/RNA non-specific endonuclease;


Pssm-ID: 460120  Cd Length: 220  Bit Score: 66.31  E-value: 5.62e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650661  673 LLSQHQFMSGYSQDILMPLWTSYTVD-----RNDSFSTEDFsnclYQDFRIPLSPVHKC-SFYKNNtKVSYGFLSPPQLN 746
Cdd:pfam01223  18 VLFYKYYSLCYDRRTRRALWVAHHLTgaslaGSKGRRRPGF----KQDPRIPGAYFRTLyTDYTGS-GFDRGHLAPAADF 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650661  747 KNSSGIYSEALLTTNIVPMYQSF-QVIWRYFHDtLLRKYAEERNG-VNVVSGPVFDFDYDGrcdslenlrqkrrvirNQE 824
Cdd:pfam01223  93 KFSAGANAATFNFTNIAPQWAGFnQGNWAYLEN-YVRDLAARHNNsVYVYTGPLYVPNLLD----------------KNK 155
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 170650661  825 ILIPTHFFIVLtsckdTSQTPLHCENLDTLAFILPHrtdnsESCVHGKHDSSWVEEllmlhrarITDVEHITGLSF 900
Cdd:pfam01223 156 VAVPTHFWKVI-----LSEDGDGGGGLNAPAFVLPN-----KYILDDGPLRTFQVP--------VDELERLTGLDF 213
Somatomedin_B pfam01033
Somatomedin B domain;
147-187 1.56e-11

Somatomedin B domain;


Pssm-ID: 460034  Cd Length: 40  Bit Score: 59.62  E-value: 1.56e-11
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 170650661  147 WTCnKFRCGEKRLTRSLCACSDDCKDKGDCCINYSSVCQGE 187
Cdd:pfam01033   1 ESC-KGRCGESFDRGRLCQCDDDCVKYGDCCPDYESLCLGE 40
Somatomedin_B pfam01033
Somatomedin B domain;
107-143 1.59e-09

Somatomedin B domain;


Pssm-ID: 460034  Cd Length: 40  Bit Score: 53.85  E-value: 1.59e-09
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 170650661  107 SCKGRCFERTFGN--CRCDAACVELGNCCLDYQETCIEP 143
Cdd:pfam01033   2 SCKGRCGESFDRGrlCQCDDDCVKYGDCCPDYESLCLGE 40
PTZ00259 PTZ00259
endonuclease G; Provisional
679-902 3.72e-06

endonuclease G; Provisional


Pssm-ID: 240335 [Multi-domain]  Cd Length: 434  Bit Score: 50.25  E-value: 3.72e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650661 679 FMSGYSQDILMPLWTSYTVDRNDSFSTE-----DFSNC-LYQDFRIPLspvhkcsfYKNNTKVSY-------GFLSPPQL 745
Cdd:PTZ00259 117 YVSSLNYERRIPNWVAEYIPYRGISVEAgekkaNRADCvFYADPTVPE--------AFRAENKDYtgsgysrGHLAAAGF 188
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650661 746 NKNSSGIYSEA-LLTTNIVPmyQSF---QVIWrYFHDTLLRKYAEER-NGVNVVSGPVF---DFDYDGRCDSLENLRQKR 817
Cdd:PTZ00259 189 HKASQTAMDDTfLLSANIVP--QDLtnnAGDW-LRLENLTRKLAREYeVGVYVVSGPLFvprYMREKLRKWRLAEPSEIH 265
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650661 818 R----------------VIRNQEILIPTHFFIVLTSCKDTSQTPLhcenldTLAFILPhrtdNSESCvhgkhdsswVEEL 881
Cdd:PTZ00259 266 KpdspadktpkkvvtyeVIGDNNVAVPTHLFKVILAEKNDGPPHE------VAAFLMP----NEPIS---------KEKP 326
                        250       260
                 ....*....|....*....|.
gi 170650661 882 LMLHRARITDVEHITGLSFYQ 902
Cdd:PTZ00259 327 LTAYQVPLEEIEKLTGLQFFP 347
AP-SPAP cd16016
SPAP is a subclass of alkaline phosphatase (AP); Alkaline phosphatases are non-specific ...
218-283 1.90e-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: 44.83  E-value: 1.90e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 170650661 218 DGFRAEYLH------TWGGLLpvisKLKKCGTYTKNMR-PVYPTKTFPNHYSIVTGLYPESHGIIDNKMYDPK 283
Cdd:cd16016   11 DQMRADYLYryrdrfGEGGFK----RLLNEGFVFENAHyNYAPTDTAPGHATIYTGTTPAIHGIIGNDWYDRE 79
 
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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