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Conserved domains on  [gi|564324723|ref|XP_006227754|]
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ectonucleotide pyrophosphatase/phosphodiesterase family member 1 isoform X1 [Rattus norvegicus]

Protein Classification

DNA/RNA non-specific endonuclease( domain architecture ID 12193405)

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 ...
 194-520 1.81e-113

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: 350.95  E-value: 1.81e-113
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564324723  194 TLLFSLDGFRAEYLHTWGgLLPVISKLKNCGTYTKNMRPVYPTKTFPNHYSIVTGLYPESHGIIDNKMYDPKMNASFSLK 273
Cdd:pfam01663   1 LLVISLDGFRADYLDRFE-LTPNLAALAKEGVSAPNLTPVFPTLTFPNHYTLVTGLYPGSHGIVGNTFYDPKTGEYLVFV 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564324723  274 SKEKFNPLWYKGQPIWVTANHQEVRSGTYFWPGSDVEID---GILPDIYK-VYNGSVPFEERILAVL--EWLQLPS---- 343
Cdd:pfam01663  80 ISDPEDPRWWQGEPIWDTAAKAGVRAAALFWPGSEVDYStyyGTPPRYLKdDYNNSVPFEDRVDTAVlqTWLDLPFadva 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564324723  344 YERPHFYTLYLEEPDSSGHSHGPVSSEVIKALQKVDHIVGMLMDGLKDLGLDKCLNLILISDHGMEQGSCKKYVYLNKYL 423
Cdd:pfam01663 160 AERPDLLLVYLEEPDYAGHRYGPDSPEVEDALRRVDRAIGDLLEALDERGLFEDTNVIVVSDHGMTPVSDDKVIFLNDYL 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564324723  424 GDVNNVKVV-YGPAARLRP-----TEVPETYYSFNYEALAKNLSCR--ETNQHFRPYLKHFLPKRLHFakNDRIEPLTFY 495
Cdd:pfam01663 240 REKGLLHLVdGGPVVAIYPkarelGHVPPGEVEEVYAELKEKLLGLriQDGEHLAVYLKEEIPGRLHY--NPRIPDLVLV 317

                         330       340
                  ....*....|....*....|....*.
gi 564324723  496 LDPQWQLALNPSERKYC-GSGFHGSD 520
Cdd:pfam01663 318 ADPGWYITGKDGGDKEAaIHGTHGYD 343
NUC smart00477
DNA/RNA non-specific endonuclease; prokaryotic and eukaryotic double- and single-stranded DNA ...
 656-887 4.00e-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: 247.27  E-value: 4.00e-76
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564324723   656 QQQFLTGYSLDLLMPLWTSYTFLSNDQFS-TDDFSNCLYQDLRIPLSPMHKCSYYKStSKLSYGFLTPPRLNRVSRQIYS 734
Cdd:smart00477   1 RNQYVLGYNRSTRMPNWVAYHITGELLTSgAERKSDCFKPDTRIPEKFQAKLSDYKG-SGYDRGHLAPAADHKFSSEAMA 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564324723   735 EALLTSNIVPMYQSF-QVIWQYLHDTVLRRYAQERNGVNVVSGPVFDFDYDGRYDSSEILKQntrVIRSQENLIPTHFFI 813
Cdd:smart00477  80 DTFYLSNIVPQYPDFnRGAWAYLEDYLRKLTASERNGVYVVSGPLFLPNYDGKGDKLEVKYQ---VIGSKNVAIPTHFFK 156

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 564324723   814 VLTSCKQLSesplkctALESSAFLLPHRPDNIESCthgkqesawveelLALHRARVTDVELITGLSFYQDRQES 887
Cdd:smart00477 157 VITAEKADS-------YLEVAAFILPNDPINDESP-------------LTNFRVPVDEIERLTGLDFFRNLDPA 210
SO smart00201
Somatomedin B -like domains; Somatomedin-B is a peptide, proteolytically excised from ...
 86-126 1.61e-11

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: 59.69  E-value: 1.61e-11
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|...
gi 564324723    86 EVKSCKGRCFERTFSN--CRCDAACVSLGNCCLDFQETCVEPT 126
Cdd:smart00201   1 AIGSCKGRCGESFNEGnaCRCDALCLSYGDCCTDYESVCKKEV 43
Somatomedin_B pfam01033
Somatomedin B domain;
129-169 2.35e-11

Somatomedin B domain;


:

Pssm-ID: 460034  Cd Length: 40  Bit Score: 59.24  E-value: 2.35e-11
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 564324723  129 WTCnKFRCGEKRLSRFVCSCADDCKAHNDCCINYSSVCQEK 169
Cdd:pfam01033   1 ESC-KGRCGESFDRGRLCQCDDDCVKYGDCCPDYESLCLGE 40
 
Name Accession Description Interval E-value
Phosphodiest pfam01663
Type I phosphodiesterase / nucleotide pyrophosphatase; This family consists of ...
 194-520 1.81e-113

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: 350.95  E-value: 1.81e-113
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564324723  194 TLLFSLDGFRAEYLHTWGgLLPVISKLKNCGTYTKNMRPVYPTKTFPNHYSIVTGLYPESHGIIDNKMYDPKMNASFSLK 273
Cdd:pfam01663   1 LLVISLDGFRADYLDRFE-LTPNLAALAKEGVSAPNLTPVFPTLTFPNHYTLVTGLYPGSHGIVGNTFYDPKTGEYLVFV 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564324723  274 SKEKFNPLWYKGQPIWVTANHQEVRSGTYFWPGSDVEID---GILPDIYK-VYNGSVPFEERILAVL--EWLQLPS---- 343
Cdd:pfam01663  80 ISDPEDPRWWQGEPIWDTAAKAGVRAAALFWPGSEVDYStyyGTPPRYLKdDYNNSVPFEDRVDTAVlqTWLDLPFadva 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564324723  344 YERPHFYTLYLEEPDSSGHSHGPVSSEVIKALQKVDHIVGMLMDGLKDLGLDKCLNLILISDHGMEQGSCKKYVYLNKYL 423
Cdd:pfam01663 160 AERPDLLLVYLEEPDYAGHRYGPDSPEVEDALRRVDRAIGDLLEALDERGLFEDTNVIVVSDHGMTPVSDDKVIFLNDYL 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564324723  424 GDVNNVKVV-YGPAARLRP-----TEVPETYYSFNYEALAKNLSCR--ETNQHFRPYLKHFLPKRLHFakNDRIEPLTFY 495
Cdd:pfam01663 240 REKGLLHLVdGGPVVAIYPkarelGHVPPGEVEEVYAELKEKLLGLriQDGEHLAVYLKEEIPGRLHY--NPRIPDLVLV 317

                         330       340
                  ....*....|....*....|....*.
gi 564324723  496 LDPQWQLALNPSERKYC-GSGFHGSD 520
Cdd:pfam01663 318 ADPGWYITGKDGGDKEAaIHGTHGYD 343
Enpp cd16018
Ectonucleotide pyrophosphatase/phosphodiesterase, also called autotaxin; Ecto-nucleotide ...
 192-560 1.06e-109

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: 338.41  E-value: 1.06e-109
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564324723 192 PPTLLFSLDGFRAEYLhTWGGLLPVISKLKNCGTYTKNMRPVYPTKTFPNHYSIVTGLYPESHGIIDNKMYDPKMNASFS 271
Cdd:cd16018    1 PPLIVISIDGFRWDYL-DRAGLTPNLKRLAEEGVRAKYVKPVFPTLTFPNHYSIVTGLYPESHGIVGNYFYDPKTNEEFS 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564324723 272 lKSKEKFNPLWYKGQPIWVTANHQEVRSGTYFWPGSDVEIDGILPD------IYKVYNGSVPFEERILAVLEWLQLpsyE 345
Cdd:cd16018   80 -DSDWVWDPWWIGGEPIWVTAEKAGLKTASYFWPGSEVAIIGYNPTpiplggYWQPYNDSFPFEERVDTILEWLDL---E 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564324723 346 RPHFYTLYLEEPDSSGHSHGPVSSEVIKALQKVDHIVGMLMDGLKDLGLDKCLNLILISDHGMeqgsckkyvylnkylgd 425
Cdd:cd16018  156 RPDLILLYFEEPDSAGHKYGPDSPEVNEALKRVDRRLGYLIEALKERGLLDDTNIIVVSDHGM----------------- 218

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564324723 426 vnnvkvvygpaarlrpTEVpetyysfnyealaknlscretnqhfrpylkhflpkrlhfakndriepltfyldpqwqlaln 505
Cdd:cd16018  219 ----------------TDV------------------------------------------------------------- 221

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 564324723 506 pserkycgsGFHGSDNLFSNMQALFIGYGPAFKHGAEVDSFENIEVYNLMCDLLG 560
Cdd:cd16018  222 ---------GTHGYDNELPDMRAIFIARGPAFKKGKKLGPFRNVDIYPLMCNLLG 267
NUC smart00477
DNA/RNA non-specific endonuclease; prokaryotic and eukaryotic double- and single-stranded DNA ...
 656-887 4.00e-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: 247.27  E-value: 4.00e-76
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564324723   656 QQQFLTGYSLDLLMPLWTSYTFLSNDQFS-TDDFSNCLYQDLRIPLSPMHKCSYYKStSKLSYGFLTPPRLNRVSRQIYS 734
Cdd:smart00477   1 RNQYVLGYNRSTRMPNWVAYHITGELLTSgAERKSDCFKPDTRIPEKFQAKLSDYKG-SGYDRGHLAPAADHKFSSEAMA 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564324723   735 EALLTSNIVPMYQSF-QVIWQYLHDTVLRRYAQERNGVNVVSGPVFDFDYDGRYDSSEILKQntrVIRSQENLIPTHFFI 813
Cdd:smart00477  80 DTFYLSNIVPQYPDFnRGAWAYLEDYLRKLTASERNGVYVVSGPLFLPNYDGKGDKLEVKYQ---VIGSKNVAIPTHFFK 156

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 564324723   814 VLTSCKQLSesplkctALESSAFLLPHRPDNIESCthgkqesawveelLALHRARVTDVELITGLSFYQDRQES 887
Cdd:smart00477 157 VITAEKADS-------YLEVAAFILPNDPINDESP-------------LTNFRVPVDEIERLTGLDFFRNLDPA 210
AtaC COG1524
c-di-AMP phosphodiesterase AtaC or nucleotide pyrophosphatase, AlkP superfamily [Signal ...
 192-561 1.58e-65

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


Pssm-ID: 441133 [Multi-domain]  Cd Length: 370  Bit Score: 224.24  E-value: 1.58e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564324723 192 PPTLLFSLDGFRAEYLHTwgGLLPVISKLKNCGTYTKNMRPVYPTKTFPNHYSIVTGLYPESHGIIDNKMYDP---KMNA 268
Cdd:COG1524   24 KKVVLILVDGLRADLLER--AHAPNLAALAARGVYARPLTSVFPSTTAPAHTTLLTGLYPGEHGIVGNGWYDPelgRVVN 101

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564324723 269 SFSLKSKEKFNPLWYKGQPIWVTANHQEVRSGTYFWPGSDVE--IDGILPdiyKVYNGSVPF----EERILAVLEWLQLP 342
Cdd:COG1524  102 SLSWVEDGFGSNSLLPVPTIFERARAAGLTTAAVFWPSFEGSglIDAARP---YPYDGRKPLlgnpAADRWIAAAALELL 178

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564324723 343 SYERPHFYTLYLEEPDSSGHSHGPVSSEVIKALQKVDHIVGMLMDGLKDLGLDKCLNLILISDHGMeqGSCKKYVYLNKy 422
Cdd:COG1524  179 REGRPDLLLVYLPDLDYAGHRYGPDSPEYRAALREVDAALGRLLDALKARGLYEGTLVIVTADHGM--VDVPPDIDLNR- 255

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564324723 423 LGDVNNVKVVYGPAARL--RPTEVPETyysfnYEALAknlscretnQHFRPYLKHFLpKRLHFAKNdRIEPLTFYLDPQW 500
Cdd:COG1524  256 LRLAGLLAVRAGESAHLylKDGADAEV-----RALLG---------LPARVLTREEL-AAGHFGPH-RIGDLVLVAKPGW 319

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 564324723 501 qlalnPSERKYCGSgfHGSDNlFSNMQALFIGYGPAFKHGaevdsFENIEVYNLMCDLLGL 561
Cdd:COG1524  320 -----ALDAPLKGS--HGGLP-DEEMRVPLLASGPGFRPG-----VRNVDVAPTIARLLGL 367
NUC cd00091
DNA/RNA non-specific endonuclease; prokaryotic and eukaryotic double- and single-stranded DNA ...
 640-897 1.89e-64

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


Pssm-ID: 238043  Cd Length: 241  Bit Score: 216.85  E-value: 1.89e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564324723 640 GRPRNLQKQhrvCLLHQQQFLTGYSLDLLMPLWTSYTFLSNDQ-FSTDDFSNCLYQDLRIPLSPMHKCSYYKSTSKLSYG 718
Cdd:cd00091    4 GRPGVLADT---EVLSYTHYVLSYNRATRLPLWVAEHIDKEDLgKNVDRKYDQFKQDPRIPPLFSATNSDYKGSGSLDRG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564324723 719 FLTPPRLNRVSRQIYSEALLTSNIVPMYQ-SFQVIWQYLHDTVLRRYAQERNGVNVVSGPVFDFDYDGRYDSseilKQNT 797
Cdd:cd00091   81 HLAPAADPVWSQDAQDATFYLTNMAPQVQgFNQGNWAYLEDYLRDLAASEGKDVYVVTGPLFLPDLDGDGGS----YLST 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564324723 798 RVIRSQENLIPTHFFIVLTSCKQLSEsplkctaLESSAFLLPHRPDNIESCthgkqESAWVEELLALHRARVTDvelITG 877
Cdd:cd00091  157 QVINNGKVAVPTHFWKVIIDEKAPGN-------LSVGAFVLPNNNPHDTLE-----FILCVEKTFQVPVASVEK---ATG 221

                        250       260
                 ....*....|....*....|
gi 564324723 878 LSFYQDRQESVSELLRLKTH 897
Cdd:cd00091  222 LSFFCNVPDSVSAVLELKKK 241
NUC1 COG1864
DNA/RNA endonuclease G, NUC1 [Nucleotide transport and metabolism];
653-897 6.25e-15

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


Pssm-ID: 441469  Cd Length: 238  Bit Score: 75.33  E-value: 6.25e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564324723 653 LLHQQQFLTGYSLDLLMPLWTSY----TFLSNDQFSTDDFsnclYQDLRIPLSPMHKCSYYKStSKLSYGFLTPPRLNRV 728
Cdd:COG1864   27 LLCYTGYSLSYNESRRTPNWVAYnldgSWLGKSLKRSDDF----RPDPRLPSGYRATLADYTG-SGYDRGHLAPSADRTF 101

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564324723 729 SRQIYSEALLTSNIVPMYQSF-QVIWQYLHDTVlRRYAQERNGVNVVSGPVFDFDYDGRYDSSEIlkqntrvirsqenLI 807
Cdd:COG1864  102 SKEANSETFLMTNISPQAPDFnQGIWARLENYV-RDLARKGGEVYVVTGPVFDDGDLKTIGSGGV-------------AV 167

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564324723 808 PTHFF-IVLTSCKQLSEsplkctaLESSAFLLPHRPDNIEscthgkqesawveellALHRARVT--DVELITGLSFYQDR 884
Cdd:COG1864  168 PTAFWkVVVDPDKNTGT-------LRAIAFLLPNTALSSG----------------PLRTYQVSvdEIEKLTGLDFFPNL 224

                        250
                 ....*....|...
gi 564324723 885 QESVSELLRLKTH 897
Cdd:COG1864  225 PDDLEAALEAKVD 237
SO smart00201
Somatomedin B -like domains; Somatomedin-B is a peptide, proteolytically excised from ...
 86-126 1.61e-11

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: 59.69  E-value: 1.61e-11
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|...
gi 564324723    86 EVKSCKGRCFERTFSN--CRCDAACVSLGNCCLDFQETCVEPT 126
Cdd:smart00201   1 AIGSCKGRCGESFNEGnaCRCDALCLSYGDCCTDYESVCKKEV 43
Somatomedin_B pfam01033
Somatomedin B domain;
129-169 2.35e-11

Somatomedin B domain;


Pssm-ID: 460034  Cd Length: 40  Bit Score: 59.24  E-value: 2.35e-11
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 564324723  129 WTCnKFRCGEKRLSRFVCSCADDCKAHNDCCINYSSVCQEK 169
Cdd:pfam01033   1 ESC-KGRCGESFDRGRLCQCDDDCVKYGDCCPDYESLCLGE 40
SO smart00201
Somatomedin B -like domains; Somatomedin-B is a peptide, proteolytically excised from ...
 127-170 8.09e-11

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: 57.77  E-value: 8.09e-11
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 564324723   127 HIWTCnKFRCGEKRLSRFVCSCADDCKAHNDCCINYSSVCQEKK 170
Cdd:smart00201   1 AIGSC-KGRCGESFNEGNACRCDALCLSYGDCCTDYESVCKKEV 43
Somatomedin_B pfam01033
Somatomedin B domain;
89-125 2.81e-10

Somatomedin B domain;


Pssm-ID: 460034  Cd Length: 40  Bit Score: 56.16  E-value: 2.81e-10
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 564324723   89 SCKGRCFERTFSN--CRCDAACVSLGNCCLDFQETCVEP 125
Cdd:pfam01033   2 SCKGRCGESFDRGrlCQCDDDCVKYGDCCPDYESLCLGE 40
Endonuclease_NS pfam01223
DNA/RNA non-specific endonuclease;
659-880 5.02e-09

DNA/RNA non-specific endonuclease;


Pssm-ID: 460120  Cd Length: 220  Bit Score: 57.45  E-value: 5.02e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564324723  659 FLTGYSL----DLLMPLWTSY-----TFLSNDQFSTDDFsnclYQDLRIPLSPMHKCSYYKSTSKLSYGFLTPPRLNRVS 729
Cdd:pfam01223  20 FYKYYSLcydrRTRRALWVAHhltgaSLAGSKGRRRPGF----KQDPRIPGAYFRTLYTDYTGSGFDRGHLAPAADFKFS 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564324723  730 RQIYSEALLTSNIVPMYQSF-QVIWQYLHDTVLRRYAQERNGVNVVSGPVfdfdydgrYDSSEILKQNTRVirsqenliP 808
Cdd:pfam01223  96 AGANAATFNFTNIAPQWAGFnQGNWAYLENYVRDLAARHNNSVYVYTGPL--------YVPNLLDKNKVAV--------P 159

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 564324723  809 THFFIVLtsckqLSESPLKCTALESSAFLLPHrpdniESCTHGKQESAWVEEllalhrarVTDVELITGLSF 880
Cdd:pfam01223 160 THFWKVI-----LSEDGDGGGGLNAPAFVLPN-----KYILDDGPLRTFQVP--------VDELERLTGLDF 213
PTZ00259 PTZ00259
endonuclease G; Provisional
 598-883 1.61e-07

endonuclease G; Provisional


Pssm-ID: 240335 [Multi-domain]  Cd Length: 434  Bit Score: 54.87  E-value: 1.61e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564324723 598 IKSVSSDLGCTCDPSIVPIMDFEKQFNLTTDAEDVYSMTVPNGRPrnlQKQHrvcLLHQQQFLTGYSLDLLMPLWT---- 673
Cdd:PTZ00259  62 VKSVVSGNALKKVTELPPPYPSEQASTARADTLPFCKEYPSFGLP---STEN---LRLYEGYVSSLNYERRIPNWVaeyi 135

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564324723 674 SYTFLSNDQFSTD-DFSNC-LYQDLRIPLSPMHKCSYYKStSKLSYGFLTPPRLNRVSRQIYSEA-LLTSNIVPmyQSF- 749
Cdd:PTZ00259 136 PYRGISVEAGEKKaNRADCvFYADPTVPEAFRAENKDYTG-SGYSRGHLAAAGFHKASQTAMDDTfLLSANIVP--QDLt 212

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564324723 750 --QVIWQYLhDTVLRRYAQER-NGVNVVSGPVFDFDYDGRYDSSEILKQNTR-------------------VIRSQENLI 807
Cdd:PTZ00259 213 nnAGDWLRL-ENLTRKLAREYeVGVYVVSGPLFVPRYMREKLRKWRLAEPSEihkpdspadktpkkvvtyeVIGDNNVAV 291

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 564324723 808 PTHFFIVLtsckqLSESPLKCTAlESSAFLLPHRPdnIEScthgkqesawvEELLALHRARVTDVELITGLSFYQD 883
Cdd:PTZ00259 292 PTHLFKVI-----LAEKNDGPPH-EVAAFLMPNEP--ISK-----------EKPLTAYQVPLEEIEKLTGLQFFPK 348
 
Name Accession Description Interval E-value
Phosphodiest pfam01663
Type I phosphodiesterase / nucleotide pyrophosphatase; This family consists of ...
 194-520 1.81e-113

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: 350.95  E-value: 1.81e-113
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564324723  194 TLLFSLDGFRAEYLHTWGgLLPVISKLKNCGTYTKNMRPVYPTKTFPNHYSIVTGLYPESHGIIDNKMYDPKMNASFSLK 273
Cdd:pfam01663   1 LLVISLDGFRADYLDRFE-LTPNLAALAKEGVSAPNLTPVFPTLTFPNHYTLVTGLYPGSHGIVGNTFYDPKTGEYLVFV 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564324723  274 SKEKFNPLWYKGQPIWVTANHQEVRSGTYFWPGSDVEID---GILPDIYK-VYNGSVPFEERILAVL--EWLQLPS---- 343
Cdd:pfam01663  80 ISDPEDPRWWQGEPIWDTAAKAGVRAAALFWPGSEVDYStyyGTPPRYLKdDYNNSVPFEDRVDTAVlqTWLDLPFadva 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564324723  344 YERPHFYTLYLEEPDSSGHSHGPVSSEVIKALQKVDHIVGMLMDGLKDLGLDKCLNLILISDHGMEQGSCKKYVYLNKYL 423
Cdd:pfam01663 160 AERPDLLLVYLEEPDYAGHRYGPDSPEVEDALRRVDRAIGDLLEALDERGLFEDTNVIVVSDHGMTPVSDDKVIFLNDYL 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564324723  424 GDVNNVKVV-YGPAARLRP-----TEVPETYYSFNYEALAKNLSCR--ETNQHFRPYLKHFLPKRLHFakNDRIEPLTFY 495
Cdd:pfam01663 240 REKGLLHLVdGGPVVAIYPkarelGHVPPGEVEEVYAELKEKLLGLriQDGEHLAVYLKEEIPGRLHY--NPRIPDLVLV 317

                         330       340
                  ....*....|....*....|....*.
gi 564324723  496 LDPQWQLALNPSERKYC-GSGFHGSD 520
Cdd:pfam01663 318 ADPGWYITGKDGGDKEAaIHGTHGYD 343
Enpp cd16018
Ectonucleotide pyrophosphatase/phosphodiesterase, also called autotaxin; Ecto-nucleotide ...
 192-560 1.06e-109

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: 338.41  E-value: 1.06e-109
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564324723 192 PPTLLFSLDGFRAEYLhTWGGLLPVISKLKNCGTYTKNMRPVYPTKTFPNHYSIVTGLYPESHGIIDNKMYDPKMNASFS 271
Cdd:cd16018    1 PPLIVISIDGFRWDYL-DRAGLTPNLKRLAEEGVRAKYVKPVFPTLTFPNHYSIVTGLYPESHGIVGNYFYDPKTNEEFS 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564324723 272 lKSKEKFNPLWYKGQPIWVTANHQEVRSGTYFWPGSDVEIDGILPD------IYKVYNGSVPFEERILAVLEWLQLpsyE 345
Cdd:cd16018   80 -DSDWVWDPWWIGGEPIWVTAEKAGLKTASYFWPGSEVAIIGYNPTpiplggYWQPYNDSFPFEERVDTILEWLDL---E 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564324723 346 RPHFYTLYLEEPDSSGHSHGPVSSEVIKALQKVDHIVGMLMDGLKDLGLDKCLNLILISDHGMeqgsckkyvylnkylgd 425
Cdd:cd16018  156 RPDLILLYFEEPDSAGHKYGPDSPEVNEALKRVDRRLGYLIEALKERGLLDDTNIIVVSDHGM----------------- 218

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564324723 426 vnnvkvvygpaarlrpTEVpetyysfnyealaknlscretnqhfrpylkhflpkrlhfakndriepltfyldpqwqlaln 505
Cdd:cd16018  219 ----------------TDV------------------------------------------------------------- 221

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 564324723 506 pserkycgsGFHGSDNLFSNMQALFIGYGPAFKHGAEVDSFENIEVYNLMCDLLG 560
Cdd:cd16018  222 ---------GTHGYDNELPDMRAIFIARGPAFKKGKKLGPFRNVDIYPLMCNLLG 267
NUC smart00477
DNA/RNA non-specific endonuclease; prokaryotic and eukaryotic double- and single-stranded DNA ...
 656-887 4.00e-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: 247.27  E-value: 4.00e-76
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564324723   656 QQQFLTGYSLDLLMPLWTSYTFLSNDQFS-TDDFSNCLYQDLRIPLSPMHKCSYYKStSKLSYGFLTPPRLNRVSRQIYS 734
Cdd:smart00477   1 RNQYVLGYNRSTRMPNWVAYHITGELLTSgAERKSDCFKPDTRIPEKFQAKLSDYKG-SGYDRGHLAPAADHKFSSEAMA 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564324723   735 EALLTSNIVPMYQSF-QVIWQYLHDTVLRRYAQERNGVNVVSGPVFDFDYDGRYDSSEILKQntrVIRSQENLIPTHFFI 813
Cdd:smart00477  80 DTFYLSNIVPQYPDFnRGAWAYLEDYLRKLTASERNGVYVVSGPLFLPNYDGKGDKLEVKYQ---VIGSKNVAIPTHFFK 156

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 564324723   814 VLTSCKQLSesplkctALESSAFLLPHRPDNIESCthgkqesawveelLALHRARVTDVELITGLSFYQDRQES 887
Cdd:smart00477 157 VITAEKADS-------YLEVAAFILPNDPINDESP-------------LTNFRVPVDEIERLTGLDFFRNLDPA 210
AtaC COG1524
c-di-AMP phosphodiesterase AtaC or nucleotide pyrophosphatase, AlkP superfamily [Signal ...
 192-561 1.58e-65

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


Pssm-ID: 441133 [Multi-domain]  Cd Length: 370  Bit Score: 224.24  E-value: 1.58e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564324723 192 PPTLLFSLDGFRAEYLHTwgGLLPVISKLKNCGTYTKNMRPVYPTKTFPNHYSIVTGLYPESHGIIDNKMYDP---KMNA 268
Cdd:COG1524   24 KKVVLILVDGLRADLLER--AHAPNLAALAARGVYARPLTSVFPSTTAPAHTTLLTGLYPGEHGIVGNGWYDPelgRVVN 101

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564324723 269 SFSLKSKEKFNPLWYKGQPIWVTANHQEVRSGTYFWPGSDVE--IDGILPdiyKVYNGSVPF----EERILAVLEWLQLP 342
Cdd:COG1524  102 SLSWVEDGFGSNSLLPVPTIFERARAAGLTTAAVFWPSFEGSglIDAARP---YPYDGRKPLlgnpAADRWIAAAALELL 178

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564324723 343 SYERPHFYTLYLEEPDSSGHSHGPVSSEVIKALQKVDHIVGMLMDGLKDLGLDKCLNLILISDHGMeqGSCKKYVYLNKy 422
Cdd:COG1524  179 REGRPDLLLVYLPDLDYAGHRYGPDSPEYRAALREVDAALGRLLDALKARGLYEGTLVIVTADHGM--VDVPPDIDLNR- 255

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564324723 423 LGDVNNVKVVYGPAARL--RPTEVPETyysfnYEALAknlscretnQHFRPYLKHFLpKRLHFAKNdRIEPLTFYLDPQW 500
Cdd:COG1524  256 LRLAGLLAVRAGESAHLylKDGADAEV-----RALLG---------LPARVLTREEL-AAGHFGPH-RIGDLVLVAKPGW 319

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 564324723 501 qlalnPSERKYCGSgfHGSDNlFSNMQALFIGYGPAFKHGaevdsFENIEVYNLMCDLLGL 561
Cdd:COG1524  320 -----ALDAPLKGS--HGGLP-DEEMRVPLLASGPGFRPG-----VRNVDVAPTIARLLGL 367
NUC cd00091
DNA/RNA non-specific endonuclease; prokaryotic and eukaryotic double- and single-stranded DNA ...
 640-897 1.89e-64

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


Pssm-ID: 238043  Cd Length: 241  Bit Score: 216.85  E-value: 1.89e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564324723 640 GRPRNLQKQhrvCLLHQQQFLTGYSLDLLMPLWTSYTFLSNDQ-FSTDDFSNCLYQDLRIPLSPMHKCSYYKSTSKLSYG 718
Cdd:cd00091    4 GRPGVLADT---EVLSYTHYVLSYNRATRLPLWVAEHIDKEDLgKNVDRKYDQFKQDPRIPPLFSATNSDYKGSGSLDRG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564324723 719 FLTPPRLNRVSRQIYSEALLTSNIVPMYQ-SFQVIWQYLHDTVLRRYAQERNGVNVVSGPVFDFDYDGRYDSseilKQNT 797
Cdd:cd00091   81 HLAPAADPVWSQDAQDATFYLTNMAPQVQgFNQGNWAYLEDYLRDLAASEGKDVYVVTGPLFLPDLDGDGGS----YLST 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564324723 798 RVIRSQENLIPTHFFIVLTSCKQLSEsplkctaLESSAFLLPHRPDNIESCthgkqESAWVEELLALHRARVTDvelITG 877
Cdd:cd00091  157 QVINNGKVAVPTHFWKVIIDEKAPGN-------LSVGAFVLPNNNPHDTLE-----FILCVEKTFQVPVASVEK---ATG 221

                        250       260
                 ....*....|....*....|
gi 564324723 878 LSFYQDRQESVSELLRLKTH 897
Cdd:cd00091  222 LSFFCNVPDSVSAVLELKKK 241
Endonuclease_NS smart00892
DNA/RNA non-specific endonuclease; A family of bacterial and eukaryotic endonucleases share ...
 658-883 4.45e-28

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


Pssm-ID: 214889 [Multi-domain]  Cd Length: 198  Bit Score: 112.12  E-value: 4.45e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564324723   658 QFLTGYSLDLLMPLWTSYTFL--SNDQFSTDDFSNCLYQD-LRIPLSPMHKCSYYKStSKLSYGFLTPPRLNRVSRQIYS 734
Cdd:smart00892   3 HYALCYDERRRLPLWVAYHLTgsTRQGKNTGRKRPWFKPDgWHLPAIFQAVNSDYTG-SGYDRGHLAPAADHGVSQEAMA 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564324723   735 EALLTSNIVPMYQSF-QVIWQYLHDTVLRRYAQERNGVNVVSGPVFDFDYDGRydsseilkqntRVirsqenLIPTHFFI 813
Cdd:smart00892  82 ATFYLTNIVPQTAGFnQGNWNRLENYVRKLLAKNKDTVYVVTGPIYLPTLPDN-----------NV------AVPSHFWK 144

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564324723   814 VLTSCKQLSEsplkctALESSAFLLPHRPDNiescthgkqesawVEELLALHRARVTDVELITGLSFYQD 883
Cdd:smart00892 145 VILSEDGSNG------GLAAIAFNLPNAPIN-------------EDYPLCEFQVPVDNIERLTGLDFFCG 195
ALP_like cd00016
alkaline phosphatases and sulfatases; This family includes alkaline phosphatases and ...
 192-447 5.07e-27

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


Pssm-ID: 293732 [Multi-domain]  Cd Length: 237  Bit Score: 110.59  E-value: 5.07e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564324723 192 PPTLLFSLDGFRAEYLHTWGG---LLPVISKLKNCGTYTkNMRPVYP-TKTFPNHYSIVTGLYPESHGIIDNKMYDPKMN 267
Cdd:cd00016    1 KHVVLIVLDGLGADDLGKAGNpapTTPNLKRLASEGATF-NFRSVSPpTSSAPNHAALLTGAYPTLHGYTGNGSADPELP 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564324723 268 asfslkskEKFNPLWYKGQPIWVTANHQEVRSGTYFwpgsdveidgilpdiykvyngsvpfeerILAVLEWLQLpsyERP 347
Cdd:cd00016   80 --------SRAAGKDEDGPTIPELLKQAGYRTGVIG----------------------------LLKAIDETSK---EKP 120

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564324723 348 HFYTLYLEEPDSSGHSHGPVSSEVIKALQKVDHIVGMLMDGLKDLGLDKCLNLILISDHGMEQGSC----KKYVYLNKYL 423
Cdd:cd00016  121 FVLFLHFDGPDGPGHAYGPNTPEYYDAVEEIDERIGKVLDALKKAGDADDTVIIVTADHGGIDKGHggdpKADGKADKSH 200

                        250       260
                 ....*....|....*....|....
gi 564324723 424 GDVNNVKVVYGPAARLRPTEVPET 447
Cdd:cd00016  201 TGMRVPFIAYGPGVKKGGVKHELI 224
NUC1 COG1864
DNA/RNA endonuclease G, NUC1 [Nucleotide transport and metabolism];
653-897 6.25e-15

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


Pssm-ID: 441469  Cd Length: 238  Bit Score: 75.33  E-value: 6.25e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564324723 653 LLHQQQFLTGYSLDLLMPLWTSY----TFLSNDQFSTDDFsnclYQDLRIPLSPMHKCSYYKStSKLSYGFLTPPRLNRV 728
Cdd:COG1864   27 LLCYTGYSLSYNESRRTPNWVAYnldgSWLGKSLKRSDDF----RPDPRLPSGYRATLADYTG-SGYDRGHLAPSADRTF 101

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564324723 729 SRQIYSEALLTSNIVPMYQSF-QVIWQYLHDTVlRRYAQERNGVNVVSGPVFDFDYDGRYDSSEIlkqntrvirsqenLI 807
Cdd:COG1864  102 SKEANSETFLMTNISPQAPDFnQGIWARLENYV-RDLARKGGEVYVVTGPVFDDGDLKTIGSGGV-------------AV 167

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564324723 808 PTHFF-IVLTSCKQLSEsplkctaLESSAFLLPHRPDNIEscthgkqesawveellALHRARVT--DVELITGLSFYQDR 884
Cdd:COG1864  168 PTAFWkVVVDPDKNTGT-------LRAIAFLLPNTALSSG----------------PLRTYQVSvdEIEKLTGLDFFPNL 224

                        250
                 ....*....|...
gi 564324723 885 QESVSELLRLKTH 897
Cdd:COG1864  225 PDDLEAALEAKVD 237
SO smart00201
Somatomedin B -like domains; Somatomedin-B is a peptide, proteolytically excised from ...
 86-126 1.61e-11

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: 59.69  E-value: 1.61e-11
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|...
gi 564324723    86 EVKSCKGRCFERTFSN--CRCDAACVSLGNCCLDFQETCVEPT 126
Cdd:smart00201   1 AIGSCKGRCGESFNEGnaCRCDALCLSYGDCCTDYESVCKKEV 43
Somatomedin_B pfam01033
Somatomedin B domain;
129-169 2.35e-11

Somatomedin B domain;


Pssm-ID: 460034  Cd Length: 40  Bit Score: 59.24  E-value: 2.35e-11
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 564324723  129 WTCnKFRCGEKRLSRFVCSCADDCKAHNDCCINYSSVCQEK 169
Cdd:pfam01033   1 ESC-KGRCGESFDRGRLCQCDDDCVKYGDCCPDYESLCLGE 40
SO smart00201
Somatomedin B -like domains; Somatomedin-B is a peptide, proteolytically excised from ...
 127-170 8.09e-11

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: 57.77  E-value: 8.09e-11
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 564324723   127 HIWTCnKFRCGEKRLSRFVCSCADDCKAHNDCCINYSSVCQEKK 170
Cdd:smart00201   1 AIGSC-KGRCGESFNEGNACRCDALCLSYGDCCTDYESVCKKEV 43
Somatomedin_B pfam01033
Somatomedin B domain;
89-125 2.81e-10

Somatomedin B domain;


Pssm-ID: 460034  Cd Length: 40  Bit Score: 56.16  E-value: 2.81e-10
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 564324723   89 SCKGRCFERTFSN--CRCDAACVSLGNCCLDFQETCVEP 125
Cdd:pfam01033   2 SCKGRCGESFDRGrlCQCDDDCVKYGDCCPDYESLCLGE 40
Endonuclease_NS pfam01223
DNA/RNA non-specific endonuclease;
659-880 5.02e-09

DNA/RNA non-specific endonuclease;


Pssm-ID: 460120  Cd Length: 220  Bit Score: 57.45  E-value: 5.02e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564324723  659 FLTGYSL----DLLMPLWTSY-----TFLSNDQFSTDDFsnclYQDLRIPLSPMHKCSYYKSTSKLSYGFLTPPRLNRVS 729
Cdd:pfam01223  20 FYKYYSLcydrRTRRALWVAHhltgaSLAGSKGRRRPGF----KQDPRIPGAYFRTLYTDYTGSGFDRGHLAPAADFKFS 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564324723  730 RQIYSEALLTSNIVPMYQSF-QVIWQYLHDTVLRRYAQERNGVNVVSGPVfdfdydgrYDSSEILKQNTRVirsqenliP 808
Cdd:pfam01223  96 AGANAATFNFTNIAPQWAGFnQGNWAYLENYVRDLAARHNNSVYVYTGPL--------YVPNLLDKNKVAV--------P 159

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 564324723  809 THFFIVLtsckqLSESPLKCTALESSAFLLPHrpdniESCTHGKQESAWVEEllalhrarVTDVELITGLSF 880
Cdd:pfam01223 160 THFWKVI-----LSEDGDGGGGLNAPAFVLPN-----KYILDDGPLRTFQVP--------VDELERLTGLDF 213
sulfatase_like cd16148
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ...
 192-411 8.88e-08

uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.


Pssm-ID: 293767 [Multi-domain]  Cd Length: 271  Bit Score: 54.48  E-value: 8.88e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564324723 192 PPTLLFSLDGFRAEYLHTWGGLL---PVISKL-KNCGTYTKNMRPVYPTKtfPNHYSIVTGLYPESHGIIDNKMydpkmn 267
Cdd:cd16148    1 MNVILIVIDSLRADHLGCYGYDRvttPNLDRLaAEGVVFDNHYSGSNPTL--PSRFSLFTGLYPFYHGVWGGPL------ 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564324723 268 asfslkskEKFNPLWY-----KGqpiWVTA---NHQEVRSGTYFWPGSDVEIDGILPDIYKVYNGSVPFEERILAVLEWL 339
Cdd:cd16148   73 --------EPDDPTLAeilrkAG---YYTAavsSNPHLFGGPGFDRGFDTFEDFRGQEGDPGEEGDERAERVTDRALEWL 141

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 564324723 340 QLPSYERPHFYTLYLEEPdssghsHGP------VSsevikalqKVDHIVGMLMDGLKDLGL-DKCLnLILISDHGMEQG 411
Cdd:cd16148  142 DRNADDDPFFLFLHYFDP------HEPylydaeVR--------YVDEQIGRLLDKLKELGLlEDTL-VIVTSDHGEEFG 205
PTZ00259 PTZ00259
endonuclease G; Provisional
 598-883 1.61e-07

endonuclease G; Provisional


Pssm-ID: 240335 [Multi-domain]  Cd Length: 434  Bit Score: 54.87  E-value: 1.61e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564324723 598 IKSVSSDLGCTCDPSIVPIMDFEKQFNLTTDAEDVYSMTVPNGRPrnlQKQHrvcLLHQQQFLTGYSLDLLMPLWT---- 673
Cdd:PTZ00259  62 VKSVVSGNALKKVTELPPPYPSEQASTARADTLPFCKEYPSFGLP---STEN---LRLYEGYVSSLNYERRIPNWVaeyi 135

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564324723 674 SYTFLSNDQFSTD-DFSNC-LYQDLRIPLSPMHKCSYYKStSKLSYGFLTPPRLNRVSRQIYSEA-LLTSNIVPmyQSF- 749
Cdd:PTZ00259 136 PYRGISVEAGEKKaNRADCvFYADPTVPEAFRAENKDYTG-SGYSRGHLAAAGFHKASQTAMDDTfLLSANIVP--QDLt 212

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564324723 750 --QVIWQYLhDTVLRRYAQER-NGVNVVSGPVFDFDYDGRYDSSEILKQNTR-------------------VIRSQENLI 807
Cdd:PTZ00259 213 nnAGDWLRL-ENLTRKLAREYeVGVYVVSGPLFVPRYMREKLRKWRLAEPSEihkpdspadktpkkvvtyeVIGDNNVAV 291

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 564324723 808 PTHFFIVLtsckqLSESPLKCTAlESSAFLLPHRPdnIEScthgkqesawvEELLALHRARVTDVELITGLSFYQD 883
Cdd:PTZ00259 292 PTHLFKVI-----LAEKNDGPPH-EVAAFLMPNEP--ISK-----------EKPLTAYQVPLEEIEKLTGLQFFPK 348
AP-SPAP cd16016
SPAP is a subclass of alkaline phosphatase (AP); Alkaline phosphatases are non-specific ...
 200-265 6.62e-05

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: 46.37  E-value: 6.62e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 564324723 200 DGFRAEYLH------TWGGLLpvisKLKNCGTYTKNMR-PVYPTKTFPNHYSIVTGLYPESHGIIDNKMYDPK 265
Cdd:cd16016   11 DQMRADYLYryrdrfGEGGFK----RLLNEGFVFENAHyNYAPTDTAPGHATIYTGTTPAIHGIIGNDWYDRE 79
GPI_EPT_2 cd16024
GPI ethanolamine phosphate transferase 2; PIG-G; Ethanolamine phosphate transferase is ...
 361-412 1.19e-03

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: 41.78  E-value: 1.19e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 564324723 361 GHSHGPVSSEVIKALQKVDHIVGMLMDGLKDLGLDKCLNLILISDHGM-EQGS 412
Cdd:cd16024  159 GHLEGPKSPLMPPKLKEMDDVIKRIYESLEEQSSNNPTLLVVCGDHGMtDAGN 211
GPI_EPT_1 cd16020
GPI ethanolamine phosphate transferase 1; PIG-N; Ethanolamine phosphate transferase is ...
 352-412 3.45e-03

GPI ethanolamine phosphate transferase 1; PIG-N; 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: 293744  Cd Length: 294  Bit Score: 40.26  E-value: 3.45e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 564324723 352 LYLEEPDSSGHSHGPVSSEVIKALQKVDHIVGMLMDGLKDLGLDKCLNLILISDHGM-EQGS 412
Cdd:cd16020  162 LHLLGLDTNGHAHKPYSKEYLENIRYVDKGIEKTYPLIEEYFNDGRTAYIFTSDHGMtDWGS 223
iduronate-2-sulfatase cd16030
iduronate-2-sulfatase; Iduronate 2-sulfatase is a sulfatase enzyme that catalyze the ...
 244-407 6.27e-03

iduronate-2-sulfatase; Iduronate 2-sulfatase is a sulfatase enzyme that catalyze the hydrolysis of sulfate ester bonds from a wide variety of substrates, including steroids, carbohydrates and proteins. Iduronate 2-sulfatase is required for the lysosomal degradation of heparan sulfate and dermatan sulfate. Mutations in the iduronate 2-sulfatase gene that result in enzymatic deficiency lead to the sex-linked mucopolysaccharidosis type II, also known as Hunter syndrome.


Pssm-ID: 293754 [Multi-domain]  Cd Length: 435  Bit Score: 39.86  E-value: 6.27e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564324723 244 SIVTGLYPESHGIIDNKMYDPK-----------------------------------MNASFSlkskEKFNPLWYKGQPI 288
Cdd:cd16030   56 SLLTGRRPDTTGVYDNNSYFRKvapdavtlpqyfkengyttagvgkifhpgipdgddDPASWD----EPPNPPGPEKYPP 131

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564324723 289 WVTANHQEVRSGTYF---WPGSDVEiDGILPDIY----------KVYNGSVPF--------------------------E 329
Cdd:cd16030  132 GKLCPGKKGGKGGGGgpaWEAADVP-DEAYPDGKvadeaieqlrKLKDSDKPFflavgfykphlpfvapkkyfdlypleS 210

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564324723 330 ERILAVLEWLQLPSYERPHFYTLYLEE---PDSSGHSHGPVSSEVIKALQK--------VDHIVGMLMDGLKDLGLDKcl 398
Cdd:cd16030  211 IPLPNPFDPIDLPEVAWNDLDDLPKYGdipALNPGDPKGPLPDEQARELRQayyasvsyVDAQVGRVLDALEELGLAD-- 288

                        250
                 ....*....|.
gi 564324723 399 NLI--LISDHG 407
Cdd:cd16030  289 NTIvvLWSDHG 299
AslA COG3119
Arylsulfatase A or related enzyme, AlkP superfamily [Inorganic ion transport and metabolism];
378-411 7.55e-03

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


Pssm-ID: 442353 [Multi-domain]  Cd Length: 393  Bit Score: 39.86  E-value: 7.55e-03
                         10        20        30
                 ....*....|....*....|....*....|....*.
gi 564324723 378 VDHIVGMLMDGLKDLGLDKclNLILI--SDHGMEQG 411
Cdd:COG3119  209 VDDQVGRLLDALEELGLAD--NTIVVftSDNGPSLG 242
 
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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