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Conserved domains on  [gi|26353972|dbj|BAC40616|]
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unnamed protein product [Mus musculus]

Protein Classification

Enpp and NUC domain-containing protein( domain architecture ID 12193405)

protein containing domains SO, Somatomedin_B, Enpp, and NUC

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Phosphodiest pfam01663
Type I phosphodiesterase / nucleotide pyrophosphatase; This family consists of ...
 194-520 2.01e-112

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: 348.26  E-value: 2.01e-112
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26353972   194 TLLFSLDGFRAEYLHTWGgLLPVISKLKNCGTYTKNMRPMYPTKTFPNHYSIVTGLYPESHGIIDNKMYDPKMNASFSLK 273
Cdd:pfam01663   1 LLVISLDGFRADYLDRFE-LTPNLAALAKEGVSAPNLTPVFPTLTFPNHYTLVTGLYPGSHGIVGNTFYDPKTGEYLVFV 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26353972   274 SKEKFNPLWYKGQPIWVTANHQEVKSGTYFWPGSDVEID---GILPDIYK-VYNGSVPFEERILAVL--EWLQLPS---- 343
Cdd:pfam01663  80 ISDPEDPRWWQGEPIWDTAAKAGVRAAALFWPGSEVDYStyyGTPPRYLKdDYNNSVPFEDRVDTAVlqTWLDLPFadva 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26353972   344 HERPHFYTLYLEEPDSSGHSHGPVSSEVIKALQKVDRLVGMLMDGLKDLGLDKCLNLILISDHGMEQGSCKKYVYLNKYL 423
Cdd:pfam01663 160 AERPDLLLVYLEEPDYAGHRYGPDSPEVEDALRRVDRAIGDLLEALDERGLFEDTNVIVVSDHGMTPVSDDKVIFLNDYL 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26353972   424 GDVNNVKVV-YGPAARLRP-----TDVPETYYSFNYEALAKNLSCR--EPNQHFRPYLKPFLPKRLHFakSDRIEPLTFY 495
Cdd:pfam01663 240 REKGLLHLVdGGPVVAIYPkarelGHVPPGEVEEVYAELKEKLLGLriQDGEHLAVYLKEEIPGRLHY--NPRIPDLVLV 317

                         330       340
                  ....*....|....*....|....*.
gi 26353972   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 3.84e-80

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: 258.06  E-value: 3.84e-80
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26353972    656 QQQFLTGYSLDLLMPLWASYTFLRNDQFSR-DDFSNCLYQDLRIPLSPVHKCSYYKsNSKLSYGFLTPPRLNRVSNHIYS 734
Cdd:smart00477   1 RNQYVLGYNRSTRMPNWVAYHITGELLTSGaERKSDCFKPDTRIPEKFQAKLSDYK-GSGYDRGHLAPAADHKFSSEAMA 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26353972    735 EALLTSNIVPMYQSF-QVIWHYLHDTLLQRYAHERNGINVVSGPVFDFDYDGRYDSLEILKQnsrVIRSQEILIPTHFFI 813
Cdd:smart00477  80 DTFYLSNIVPQYPDFnRGAWAYLEDYLRKLTASERNGVYVVSGPLFLPNYDGKGDKLEVKYQ---VIGSKNVAIPTHFFK 156

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 26353972    814 VLTSCKQLsetplecSALESSAYILPHRPDNIESCthgkresswveelLTLHRARVTDVELITGLSFYQDRQES 887
Cdd:smart00477 157 VITAEKAD-------SYLEVAAFILPNDPINDESP-------------LTNFRVPVDEIERLTGLDFFRNLDPA 210
Somatomedin_B pfam01033
Somatomedin B domain;
129-169 1.38e-11

Somatomedin B domain;


:

Pssm-ID: 460034  Cd Length: 40  Bit Score: 59.62  E-value: 1.38e-11
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 26353972   129 WTCnKFRCGEKRLSRFVCSCADDCKTHNDCCINYSSVCQDK 169
Cdd:pfam01033   1 ESC-KGRCGESFDRGRLCQCDDDCVKYGDCCPDYESLCLGE 40
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 26353972     86 EVKSCKGRCFERTFSN--CRCDAACVSLGNCCLDFQETCVEPT 126
Cdd:smart00201   1 AIGSCKGRCGESFNEGnaCRCDALCLSYGDCCTDYESVCKKEV 43
 
Name Accession Description Interval E-value
Phosphodiest pfam01663
Type I phosphodiesterase / nucleotide pyrophosphatase; This family consists of ...
 194-520 2.01e-112

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: 348.26  E-value: 2.01e-112
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26353972   194 TLLFSLDGFRAEYLHTWGgLLPVISKLKNCGTYTKNMRPMYPTKTFPNHYSIVTGLYPESHGIIDNKMYDPKMNASFSLK 273
Cdd:pfam01663   1 LLVISLDGFRADYLDRFE-LTPNLAALAKEGVSAPNLTPVFPTLTFPNHYTLVTGLYPGSHGIVGNTFYDPKTGEYLVFV 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26353972   274 SKEKFNPLWYKGQPIWVTANHQEVKSGTYFWPGSDVEID---GILPDIYK-VYNGSVPFEERILAVL--EWLQLPS---- 343
Cdd:pfam01663  80 ISDPEDPRWWQGEPIWDTAAKAGVRAAALFWPGSEVDYStyyGTPPRYLKdDYNNSVPFEDRVDTAVlqTWLDLPFadva 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26353972   344 HERPHFYTLYLEEPDSSGHSHGPVSSEVIKALQKVDRLVGMLMDGLKDLGLDKCLNLILISDHGMEQGSCKKYVYLNKYL 423
Cdd:pfam01663 160 AERPDLLLVYLEEPDYAGHRYGPDSPEVEDALRRVDRAIGDLLEALDERGLFEDTNVIVVSDHGMTPVSDDKVIFLNDYL 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26353972   424 GDVNNVKVV-YGPAARLRP-----TDVPETYYSFNYEALAKNLSCR--EPNQHFRPYLKPFLPKRLHFakSDRIEPLTFY 495
Cdd:pfam01663 240 REKGLLHLVdGGPVVAIYPkarelGHVPPGEVEEVYAELKEKLLGLriQDGEHLAVYLKEEIPGRLHY--NPRIPDLVLV 317

                         330       340
                  ....*....|....*....|....*.
gi 26353972   496 LDPQWQLALNPSERKYC-GSGFHGSD 520
Cdd:pfam01663 318 ADPGWYITGKDGGDKEAaIHGTHGYD 343
Enpp cd16018
Ectonucleotide pyrophosphatase/phosphodiesterase, also called autotaxin; Ecto-nucleotide ...
 192-560 2.71e-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: 337.25  E-value: 2.71e-109
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26353972 192 PPTLLFSLDGFRAEYLhTWGGLLPVISKLKNCGTYTKNMRPMYPTKTFPNHYSIVTGLYPESHGIIDNKMYDPKMNASFS 271
Cdd:cd16018   1 PPLIVISIDGFRWDYL-DRAGLTPNLKRLAEEGVRAKYVKPVFPTLTFPNHYSIVTGLYPESHGIVGNYFYDPKTNEEFS 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26353972 272 lKSKEKFNPLWYKGQPIWVTANHQEVKSGTYFWPGSDVEIDGILPD------IYKVYNGSVPFEERILAVLEWLQLpshE 345
Cdd:cd16018  80 -DSDWVWDPWWIGGEPIWVTAEKAGLKTASYFWPGSEVAIIGYNPTpiplggYWQPYNDSFPFEERVDTILEWLDL---E 155

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26353972 346 RPHFYTLYLEEPDSSGHSHGPVSSEVIKALQKVDRLVGMLMDGLKDLGLDKCLNLILISDHGMeqgsckkyvylnkylgd 425
Cdd:cd16018 156 RPDLILLYFEEPDSAGHKYGPDSPEVNEALKRVDRRLGYLIEALKERGLLDDTNIIVVSDHGM----------------- 218

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26353972 426 vnnvkvvygpaarlrpTDVpetyysfnyealaknlscrepnqhfrpylkpflpkrlhfaksdriepltfyldpqwqlaln 505
Cdd:cd16018 219 ----------------TDV------------------------------------------------------------- 221

                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|....*
gi 26353972 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 3.84e-80

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: 258.06  E-value: 3.84e-80
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26353972    656 QQQFLTGYSLDLLMPLWASYTFLRNDQFSR-DDFSNCLYQDLRIPLSPVHKCSYYKsNSKLSYGFLTPPRLNRVSNHIYS 734
Cdd:smart00477   1 RNQYVLGYNRSTRMPNWVAYHITGELLTSGaERKSDCFKPDTRIPEKFQAKLSDYK-GSGYDRGHLAPAADHKFSSEAMA 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26353972    735 EALLTSNIVPMYQSF-QVIWHYLHDTLLQRYAHERNGINVVSGPVFDFDYDGRYDSLEILKQnsrVIRSQEILIPTHFFI 813
Cdd:smart00477  80 DTFYLSNIVPQYPDFnRGAWAYLEDYLRKLTASERNGVYVVSGPLFLPNYDGKGDKLEVKYQ---VIGSKNVAIPTHFFK 156

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 26353972    814 VLTSCKQLsetplecSALESSAYILPHRPDNIESCthgkresswveelLTLHRARVTDVELITGLSFYQDRQES 887
Cdd:smart00477 157 VITAEKAD-------SYLEVAAFILPNDPINDESP-------------LTNFRVPVDEIERLTGLDFFRNLDPA 210
NUC cd00091
DNA/RNA non-specific endonuclease; prokaryotic and eukaryotic double- and single-stranded DNA ...
 638-897 1.67e-68

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: 227.64  E-value: 1.67e-68
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26353972 638 PYGRPRILLKQhhvCLLQQQQFLTGYSLDLLMPLWASYTFLRNDQFSR-DDFSNCLYQDLRIPLSPVHKCSYYKSNSKLS 716
Cdd:cd00091   2 QYGRPGVLADT---EVLSYTHYVLSYNRATRLPLWVAEHIDKEDLGKNvDRKYDQFKQDPRIPPLFSATNSDYKGSGSLD 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26353972 717 YGFLTPPRLNRVSNHIYSEALLTSNIVPMYQ-SFQVIWHYLHDTLLQRYAHERNGINVVSGPVFDFDYDGRYDSleilKQ 795
Cdd:cd00091  79 RGHLAPAADPVWSQDAQDATFYLTNMAPQVQgFNQGNWAYLEDYLRDLAASEGKDVYVVTGPLFLPDLDGDGGS----YL 154

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26353972 796 NSRVIRSQEILIPTHFFIVLTSCKQLSEtplecsaLESSAYILPHRPDNIESCthgkrESSWVEELLTLHRARVTDvelI 875
Cdd:cd00091 155 STQVINNGKVAVPTHFWKVIIDEKAPGN-------LSVGAFVLPNNNPHDTLE-----FILCVEKTFQVPVASVEK---A 219

                       250       260
                ....*....|....*....|..
gi 26353972 876 TGLSFYQDRQESVSELLRLKTH 897
Cdd:cd00091 220 TGLSFFCNVPDSVSAVLELKKK 241
AtaC COG1524
c-di-AMP phosphodiesterase AtaC or nucleotide pyrophosphatase, AlkP superfamily [Signal ...
 192-561 1.30e-66

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


Pssm-ID: 441133 [Multi-domain]  Cd Length: 370  Bit Score: 227.32  E-value: 1.30e-66
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26353972 192 PPTLLFSLDGFRAEYLHTwgGLLPVISKLKNCGTYTKNMRPMYPTKTFPNHYSIVTGLYPESHGIIDNKMYDP---KMNA 268
Cdd:COG1524  24 KKVVLILVDGLRADLLER--AHAPNLAALAARGVYARPLTSVFPSTTAPAHTTLLTGLYPGEHGIVGNGWYDPelgRVVN 101

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26353972 269 SFSLKSKEKFNPLWYKGQPIWVTANHQEVKSGTYFWPGSDVE--IDGILPdiyKVYNGSVPF----EERILAVLEWLQLP 342
Cdd:COG1524 102 SLSWVEDGFGSNSLLPVPTIFERARAAGLTTAAVFWPSFEGSglIDAARP---YPYDGRKPLlgnpAADRWIAAAALELL 178

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26353972 343 SHERPHFYTLYLEEPDSSGHSHGPVSSEVIKALQKVDRLVGMLMDGLKDLGLDKCLNLILISDHGMeqGSCKKYVYLNKy 422
Cdd:COG1524 179 REGRPDLLLVYLPDLDYAGHRYGPDSPEYRAALREVDAALGRLLDALKARGLYEGTLVIVTADHGM--VDVPPDIDLNR- 255

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26353972 423 LGDVNNVKVVYGPAARLRPTDVpetyysfNYEALAKNLscrepNQHFRPYLKPFLpKRLHFAkSDRIEPLTFYLDPQWql 502
Cdd:COG1524 256 LRLAGLLAVRAGESAHLYLKDG-------ADAEVRALL-----GLPARVLTREEL-AAGHFG-PHRIGDLVLVAKPGW-- 319

                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 26353972 503 alnPSERKYCGSgfHGSDNlFSNMQALFIGYGPAFKHGaevdsFENIEVYNLMCDLLGL 561
Cdd:COG1524 320 ---ALDAPLKGS--HGGLP-DEEMRVPLLASGPGFRPG-----VRNVDVAPTIARLLGL 367
NUC1 COG1864
DNA/RNA endonuclease G, NUC1 [Nucleotide transport and metabolism];
653-897 2.56e-13

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


Pssm-ID: 441469  Cd Length: 238  Bit Score: 70.32  E-value: 2.56e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26353972 653 LLQQQQFLTGYSLDLLMPLWASY----TFLRNDQFSRDDFsnclYQDLRIPLS-PVHKCSYykSNSKLSYGFLTP---PR 724
Cdd:COG1864  27 LLCYTGYSLSYNESRRTPNWVAYnldgSWLGKSLKRSDDF----RPDPRLPSGyRATLADY--TGSGYDRGHLAPsadRT 100

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26353972 725 LNRVSNhiySEALLTSNIVPMYQSF-QVIWHYLHDTLLQrYAHERNGINVVSGPVFDfdydgrydsleilKQNSRVIRSQ 803
Cdd:COG1864 101 FSKEAN---SETFLMTNISPQAPDFnQGIWARLENYVRD-LARKGGEVYVVTGPVFD-------------DGDLKTIGSG 163

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26353972 804 EILIPTHFF-IVLTsckqlseTPLECSALESSAYILPHRPDniescthgkRESSWVEELLTlhrarVTDVELITGLSFYQ 882
Cdd:COG1864 164 GVAVPTAFWkVVVD-------PDKNTGTLRAIAFLLPNTAL---------SSGPLRTYQVS-----VDEIEKLTGLDFFP 222

                       250
                ....*....|....*
gi 26353972 883 DRQESVSELLRLKTH 897
Cdd:COG1864 223 NLPDDLEAALEAKVD 237
Somatomedin_B pfam01033
Somatomedin B domain;
129-169 1.38e-11

Somatomedin B domain;


Pssm-ID: 460034  Cd Length: 40  Bit Score: 59.62  E-value: 1.38e-11
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 26353972   129 WTCnKFRCGEKRLSRFVCSCADDCKTHNDCCINYSSVCQDK 169
Cdd:pfam01033   1 ESC-KGRCGESFDRGRLCQCDDDCVKYGDCCPDYESLCLGE 40
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 26353972     86 EVKSCKGRCFERTFSN--CRCDAACVSLGNCCLDFQETCVEPT 126
Cdd:smart00201   1 AIGSCKGRCGESFNEGnaCRCDALCLSYGDCCTDYESVCKKEV 43
SO smart00201
Somatomedin B -like domains; Somatomedin-B is a peptide, proteolytically excised from ...
 127-170 1.27e-10

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: 57.00  E-value: 1.27e-10
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 26353972    127 HIWTCnKFRCGEKRLSRFVCSCADDCKTHNDCCINYSSVCQDKK 170
Cdd:smart00201   1 AIGSC-KGRCGESFNEGNACRCDALCLSYGDCCTDYESVCKKEV 43
Somatomedin_B pfam01033
Somatomedin B domain;
89-125 2.86e-10

Somatomedin B domain;


Pssm-ID: 460034  Cd Length: 40  Bit Score: 56.16  E-value: 2.86e-10
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 26353972    89 SCKGRCFERTFSN--CRCDAACVSLGNCCLDFQETCVEP 125
Cdd:pfam01033   2 SCKGRCGESFDRGrlCQCDDDCVKYGDCCPDYESLCLGE 40
Endonuclease_NS pfam01223
DNA/RNA non-specific endonuclease;
655-880 2.30e-08

DNA/RNA non-specific endonuclease;


Pssm-ID: 460120  Cd Length: 220  Bit Score: 55.52  E-value: 2.30e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26353972   655 QQQQFLTGYSL----DLLMPLWASY-----TFLRNDQFSRDDFsnclYQDLRIPLSPVHKCSYYKSNSKLSYGFLTPPrl 725
Cdd:pfam01223  16 DVVLFYKYYSLcydrRTRRALWVAHhltgaSLAGSKGRRRPGF----KQDPRIPGAYFRTLYTDYTGSGFDRGHLAPA-- 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26353972   726 nrvSNHIYSEA--LLT---SNIVPMYQSF-QVIWHYLHDtLLQRYAHERNG-INVVSGPVFDFDYDGrydsleilkqnsr 798
Cdd:pfam01223  90 ---ADFKFSAGanAATfnfTNIAPQWAGFnQGNWAYLEN-YVRDLAARHNNsVYVYTGPLYVPNLLD------------- 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26353972   799 virSQEILIPTHFFIVLtsckqLSETPLECSALESSAYILPHRPdniescthGKRESSWVEELLTlhrarVTDVELITGL 878
Cdd:pfam01223 153 ---KNKVAVPTHFWKVI-----LSEDGDGGGGLNAPAFVLPNKY--------ILDDGPLRTFQVP-----VDELERLTGL 211


                  ..
gi 26353972   879 SF 880
Cdd:pfam01223 212 DF 213
PTZ00259 PTZ00259
endonuclease G; Provisional
 598-883 1.32e-06

endonuclease G; Provisional


Pssm-ID: 240335 [Multi-domain]  Cd Length: 434  Bit Score: 51.79  E-value: 1.32e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26353972  598 IKSTSNDLGCTCDPWIVPIKDFEKQLNLTTEDDDIYHMTVPYGRP---RILLKQHHVcllqqqqflTGYSLDLLMPLW-A 673
Cdd:PTZ00259  62 VKSVVSGNALKKVTELPPPYPSEQASTARADTLPFCKEYPSFGLPsteNLRLYEGYV---------SSLNYERRIPNWvA 132

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26353972  674 SYTFLRNDQFSRD----DFSNC-LYQDLRIPLSPVHKCSYYKSnSKLSYGFLTPPRLNRVSNHIYSEA-LLTSNIVPmyQ 747
Cdd:PTZ00259 133 EYIPYRGISVEAGekkaNRADCvFYADPTVPEAFRAENKDYTG-SGYSRGHLAAAGFHKASQTAMDDTfLLSANIVP--Q 209

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26353972  748 SF---QVIWHYLHD-TLLQRYAHErNGINVVSGPVFDFDYDGRYDSLEILKQNSR-------------------VIRSQE 804
Cdd:PTZ00259 210 DLtnnAGDWLRLENlTRKLAREYE-VGVYVVSGPLFVPRYMREKLRKWRLAEPSEihkpdspadktpkkvvtyeVIGDNN 288

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 26353972  805 ILIPTHFFIVLtsckqLSETPLECSAlESSAYILPHRPdnIEScthgkresswvEELLTLHRARVTDVELITGLSFYQD 883
Cdd:PTZ00259 289 VAVPTHLFKVI-----LAEKNDGPPH-EVAAFLMPNEP--ISK-----------EKPLTAYQVPLEEIEKLTGLQFFPK 348
 
Name Accession Description Interval E-value
Phosphodiest pfam01663
Type I phosphodiesterase / nucleotide pyrophosphatase; This family consists of ...
 194-520 2.01e-112

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: 348.26  E-value: 2.01e-112
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26353972   194 TLLFSLDGFRAEYLHTWGgLLPVISKLKNCGTYTKNMRPMYPTKTFPNHYSIVTGLYPESHGIIDNKMYDPKMNASFSLK 273
Cdd:pfam01663   1 LLVISLDGFRADYLDRFE-LTPNLAALAKEGVSAPNLTPVFPTLTFPNHYTLVTGLYPGSHGIVGNTFYDPKTGEYLVFV 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26353972   274 SKEKFNPLWYKGQPIWVTANHQEVKSGTYFWPGSDVEID---GILPDIYK-VYNGSVPFEERILAVL--EWLQLPS---- 343
Cdd:pfam01663  80 ISDPEDPRWWQGEPIWDTAAKAGVRAAALFWPGSEVDYStyyGTPPRYLKdDYNNSVPFEDRVDTAVlqTWLDLPFadva 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26353972   344 HERPHFYTLYLEEPDSSGHSHGPVSSEVIKALQKVDRLVGMLMDGLKDLGLDKCLNLILISDHGMEQGSCKKYVYLNKYL 423
Cdd:pfam01663 160 AERPDLLLVYLEEPDYAGHRYGPDSPEVEDALRRVDRAIGDLLEALDERGLFEDTNVIVVSDHGMTPVSDDKVIFLNDYL 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26353972   424 GDVNNVKVV-YGPAARLRP-----TDVPETYYSFNYEALAKNLSCR--EPNQHFRPYLKPFLPKRLHFakSDRIEPLTFY 495
Cdd:pfam01663 240 REKGLLHLVdGGPVVAIYPkarelGHVPPGEVEEVYAELKEKLLGLriQDGEHLAVYLKEEIPGRLHY--NPRIPDLVLV 317

                         330       340
                  ....*....|....*....|....*.
gi 26353972   496 LDPQWQLALNPSERKYC-GSGFHGSD 520
Cdd:pfam01663 318 ADPGWYITGKDGGDKEAaIHGTHGYD 343
Enpp cd16018
Ectonucleotide pyrophosphatase/phosphodiesterase, also called autotaxin; Ecto-nucleotide ...
 192-560 2.71e-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: 337.25  E-value: 2.71e-109
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26353972 192 PPTLLFSLDGFRAEYLhTWGGLLPVISKLKNCGTYTKNMRPMYPTKTFPNHYSIVTGLYPESHGIIDNKMYDPKMNASFS 271
Cdd:cd16018   1 PPLIVISIDGFRWDYL-DRAGLTPNLKRLAEEGVRAKYVKPVFPTLTFPNHYSIVTGLYPESHGIVGNYFYDPKTNEEFS 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26353972 272 lKSKEKFNPLWYKGQPIWVTANHQEVKSGTYFWPGSDVEIDGILPD------IYKVYNGSVPFEERILAVLEWLQLpshE 345
Cdd:cd16018  80 -DSDWVWDPWWIGGEPIWVTAEKAGLKTASYFWPGSEVAIIGYNPTpiplggYWQPYNDSFPFEERVDTILEWLDL---E 155

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26353972 346 RPHFYTLYLEEPDSSGHSHGPVSSEVIKALQKVDRLVGMLMDGLKDLGLDKCLNLILISDHGMeqgsckkyvylnkylgd 425
Cdd:cd16018 156 RPDLILLYFEEPDSAGHKYGPDSPEVNEALKRVDRRLGYLIEALKERGLLDDTNIIVVSDHGM----------------- 218

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26353972 426 vnnvkvvygpaarlrpTDVpetyysfnyealaknlscrepnqhfrpylkpflpkrlhfaksdriepltfyldpqwqlaln 505
Cdd:cd16018 219 ----------------TDV------------------------------------------------------------- 221

                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|....*
gi 26353972 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 3.84e-80

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: 258.06  E-value: 3.84e-80
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26353972    656 QQQFLTGYSLDLLMPLWASYTFLRNDQFSR-DDFSNCLYQDLRIPLSPVHKCSYYKsNSKLSYGFLTPPRLNRVSNHIYS 734
Cdd:smart00477   1 RNQYVLGYNRSTRMPNWVAYHITGELLTSGaERKSDCFKPDTRIPEKFQAKLSDYK-GSGYDRGHLAPAADHKFSSEAMA 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26353972    735 EALLTSNIVPMYQSF-QVIWHYLHDTLLQRYAHERNGINVVSGPVFDFDYDGRYDSLEILKQnsrVIRSQEILIPTHFFI 813
Cdd:smart00477  80 DTFYLSNIVPQYPDFnRGAWAYLEDYLRKLTASERNGVYVVSGPLFLPNYDGKGDKLEVKYQ---VIGSKNVAIPTHFFK 156

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 26353972    814 VLTSCKQLsetplecSALESSAYILPHRPDNIESCthgkresswveelLTLHRARVTDVELITGLSFYQDRQES 887
Cdd:smart00477 157 VITAEKAD-------SYLEVAAFILPNDPINDESP-------------LTNFRVPVDEIERLTGLDFFRNLDPA 210
NUC cd00091
DNA/RNA non-specific endonuclease; prokaryotic and eukaryotic double- and single-stranded DNA ...
 638-897 1.67e-68

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: 227.64  E-value: 1.67e-68
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26353972 638 PYGRPRILLKQhhvCLLQQQQFLTGYSLDLLMPLWASYTFLRNDQFSR-DDFSNCLYQDLRIPLSPVHKCSYYKSNSKLS 716
Cdd:cd00091   2 QYGRPGVLADT---EVLSYTHYVLSYNRATRLPLWVAEHIDKEDLGKNvDRKYDQFKQDPRIPPLFSATNSDYKGSGSLD 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26353972 717 YGFLTPPRLNRVSNHIYSEALLTSNIVPMYQ-SFQVIWHYLHDTLLQRYAHERNGINVVSGPVFDFDYDGRYDSleilKQ 795
Cdd:cd00091  79 RGHLAPAADPVWSQDAQDATFYLTNMAPQVQgFNQGNWAYLEDYLRDLAASEGKDVYVVTGPLFLPDLDGDGGS----YL 154

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26353972 796 NSRVIRSQEILIPTHFFIVLTSCKQLSEtplecsaLESSAYILPHRPDNIESCthgkrESSWVEELLTLHRARVTDvelI 875
Cdd:cd00091 155 STQVINNGKVAVPTHFWKVIIDEKAPGN-------LSVGAFVLPNNNPHDTLE-----FILCVEKTFQVPVASVEK---A 219

                       250       260
                ....*....|....*....|..
gi 26353972 876 TGLSFYQDRQESVSELLRLKTH 897
Cdd:cd00091 220 TGLSFFCNVPDSVSAVLELKKK 241
AtaC COG1524
c-di-AMP phosphodiesterase AtaC or nucleotide pyrophosphatase, AlkP superfamily [Signal ...
 192-561 1.30e-66

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


Pssm-ID: 441133 [Multi-domain]  Cd Length: 370  Bit Score: 227.32  E-value: 1.30e-66
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26353972 192 PPTLLFSLDGFRAEYLHTwgGLLPVISKLKNCGTYTKNMRPMYPTKTFPNHYSIVTGLYPESHGIIDNKMYDP---KMNA 268
Cdd:COG1524  24 KKVVLILVDGLRADLLER--AHAPNLAALAARGVYARPLTSVFPSTTAPAHTTLLTGLYPGEHGIVGNGWYDPelgRVVN 101

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26353972 269 SFSLKSKEKFNPLWYKGQPIWVTANHQEVKSGTYFWPGSDVE--IDGILPdiyKVYNGSVPF----EERILAVLEWLQLP 342
Cdd:COG1524 102 SLSWVEDGFGSNSLLPVPTIFERARAAGLTTAAVFWPSFEGSglIDAARP---YPYDGRKPLlgnpAADRWIAAAALELL 178

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26353972 343 SHERPHFYTLYLEEPDSSGHSHGPVSSEVIKALQKVDRLVGMLMDGLKDLGLDKCLNLILISDHGMeqGSCKKYVYLNKy 422
Cdd:COG1524 179 REGRPDLLLVYLPDLDYAGHRYGPDSPEYRAALREVDAALGRLLDALKARGLYEGTLVIVTADHGM--VDVPPDIDLNR- 255

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26353972 423 LGDVNNVKVVYGPAARLRPTDVpetyysfNYEALAKNLscrepNQHFRPYLKPFLpKRLHFAkSDRIEPLTFYLDPQWql 502
Cdd:COG1524 256 LRLAGLLAVRAGESAHLYLKDG-------ADAEVRALL-----GLPARVLTREEL-AAGHFG-PHRIGDLVLVAKPGW-- 319

                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 26353972 503 alnPSERKYCGSgfHGSDNlFSNMQALFIGYGPAFKHGaevdsFENIEVYNLMCDLLGL 561
Cdd:COG1524 320 ---ALDAPLKGS--HGGLP-DEEMRVPLLASGPGFRPG-----VRNVDVAPTIARLLGL 367
ALP_like cd00016
alkaline phosphatases and sulfatases; This family includes alkaline phosphatases and ...
 192-447 1.25e-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: 109.43  E-value: 1.25e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26353972 192 PPTLLFSLDGFRAEYLHTWGG---LLPVISKLKNCGTYTkNMRPMYP-TKTFPNHYSIVTGLYPESHGIIDNKMYDPKMN 267
Cdd:cd00016   1 KHVVLIVLDGLGADDLGKAGNpapTTPNLKRLASEGATF-NFRSVSPpTSSAPNHAALLTGAYPTLHGYTGNGSADPELP 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26353972 268 asfslkskEKFNPLWYKGQPIWVTANHQEVKSGTYFwpgsdveidgilpdiykvyngsvpfeerILAVLEWLQLpshERP 347
Cdd:cd00016  80 --------SRAAGKDEDGPTIPELLKQAGYRTGVIG----------------------------LLKAIDETSK---EKP 120

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26353972 348 HFYTLYLEEPDSSGHSHGPVSSEVIKALQKVDRLVGMLMDGLKDLGLDKCLNLILISDHGMEQGSC----KKYVYLNKYL 423
Cdd:cd00016 121 FVLFLHFDGPDGPGHAYGPNTPEYYDAVEEIDERIGKVLDALKKAGDADDTVIIVTADHGGIDKGHggdpKADGKADKSH 200

                       250       260
                ....*....|....*....|....
gi 26353972 424 GDVNNVKVVYGPAARLRPTDVPET 447
Cdd:cd00016 201 TGMRVPFIAYGPGVKKGGVKHELI 224
Endonuclease_NS smart00892
DNA/RNA non-specific endonuclease; A family of bacterial and eukaryotic endonucleases share ...
 658-883 1.16e-24

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: 102.49  E-value: 1.16e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26353972    658 QFLTGYSLDLLMPLWASYTFLR--NDQFSRDDFSNCLYQD-LRIPLSPVHKCSYYKsNSKLSYGFLTPPRLNRVSNHIYS 734
Cdd:smart00892   3 HYALCYDERRRLPLWVAYHLTGstRQGKNTGRKRPWFKPDgWHLPAIFQAVNSDYT-GSGYDRGHLAPAADHGVSQEAMA 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26353972    735 EALLTSNIVPMYQSF-QVIWHYLHDTLLQRYAHERNGINVVSGPVFDFDYDGRydsleilkqnsrvirsqEILIPTHFFI 813
Cdd:smart00892  82 ATFYLTNIVPQTAGFnQGNWNRLENYVRKLLAKNKDTVYVVTGPIYLPTLPDN-----------------NVAVPSHFWK 144

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26353972    814 VLTSCKQLSEtplecsALESSAYILPHRPDNiescthgkresswVEELLTLHRARVTDVELITGLSFYQD 883
Cdd:smart00892 145 VILSEDGSNG------GLAAIAFNLPNAPIN-------------EDYPLCEFQVPVDNIERLTGLDFFCG 195
NUC1 COG1864
DNA/RNA endonuclease G, NUC1 [Nucleotide transport and metabolism];
653-897 2.56e-13

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


Pssm-ID: 441469  Cd Length: 238  Bit Score: 70.32  E-value: 2.56e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26353972 653 LLQQQQFLTGYSLDLLMPLWASY----TFLRNDQFSRDDFsnclYQDLRIPLS-PVHKCSYykSNSKLSYGFLTP---PR 724
Cdd:COG1864  27 LLCYTGYSLSYNESRRTPNWVAYnldgSWLGKSLKRSDDF----RPDPRLPSGyRATLADY--TGSGYDRGHLAPsadRT 100

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26353972 725 LNRVSNhiySEALLTSNIVPMYQSF-QVIWHYLHDTLLQrYAHERNGINVVSGPVFDfdydgrydsleilKQNSRVIRSQ 803
Cdd:COG1864 101 FSKEAN---SETFLMTNISPQAPDFnQGIWARLENYVRD-LARKGGEVYVVTGPVFD-------------DGDLKTIGSG 163

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26353972 804 EILIPTHFF-IVLTsckqlseTPLECSALESSAYILPHRPDniescthgkRESSWVEELLTlhrarVTDVELITGLSFYQ 882
Cdd:COG1864 164 GVAVPTAFWkVVVD-------PDKNTGTLRAIAFLLPNTAL---------SSGPLRTYQVS-----VDEIEKLTGLDFFP 222

                       250
                ....*....|....*
gi 26353972 883 DRQESVSELLRLKTH 897
Cdd:COG1864 223 NLPDDLEAALEAKVD 237
Somatomedin_B pfam01033
Somatomedin B domain;
129-169 1.38e-11

Somatomedin B domain;


Pssm-ID: 460034  Cd Length: 40  Bit Score: 59.62  E-value: 1.38e-11
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 26353972   129 WTCnKFRCGEKRLSRFVCSCADDCKTHNDCCINYSSVCQDK 169
Cdd:pfam01033   1 ESC-KGRCGESFDRGRLCQCDDDCVKYGDCCPDYESLCLGE 40
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 26353972     86 EVKSCKGRCFERTFSN--CRCDAACVSLGNCCLDFQETCVEPT 126
Cdd:smart00201   1 AIGSCKGRCGESFNEGnaCRCDALCLSYGDCCTDYESVCKKEV 43
SO smart00201
Somatomedin B -like domains; Somatomedin-B is a peptide, proteolytically excised from ...
 127-170 1.27e-10

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: 57.00  E-value: 1.27e-10
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 26353972    127 HIWTCnKFRCGEKRLSRFVCSCADDCKTHNDCCINYSSVCQDKK 170
Cdd:smart00201   1 AIGSC-KGRCGESFNEGNACRCDALCLSYGDCCTDYESVCKKEV 43
Somatomedin_B pfam01033
Somatomedin B domain;
89-125 2.86e-10

Somatomedin B domain;


Pssm-ID: 460034  Cd Length: 40  Bit Score: 56.16  E-value: 2.86e-10
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 26353972    89 SCKGRCFERTFSN--CRCDAACVSLGNCCLDFQETCVEP 125
Cdd:pfam01033   2 SCKGRCGESFDRGrlCQCDDDCVKYGDCCPDYESLCLGE 40
Endonuclease_NS pfam01223
DNA/RNA non-specific endonuclease;
655-880 2.30e-08

DNA/RNA non-specific endonuclease;


Pssm-ID: 460120  Cd Length: 220  Bit Score: 55.52  E-value: 2.30e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26353972   655 QQQQFLTGYSL----DLLMPLWASY-----TFLRNDQFSRDDFsnclYQDLRIPLSPVHKCSYYKSNSKLSYGFLTPPrl 725
Cdd:pfam01223  16 DVVLFYKYYSLcydrRTRRALWVAHhltgaSLAGSKGRRRPGF----KQDPRIPGAYFRTLYTDYTGSGFDRGHLAPA-- 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26353972   726 nrvSNHIYSEA--LLT---SNIVPMYQSF-QVIWHYLHDtLLQRYAHERNG-INVVSGPVFDFDYDGrydsleilkqnsr 798
Cdd:pfam01223  90 ---ADFKFSAGanAATfnfTNIAPQWAGFnQGNWAYLEN-YVRDLAARHNNsVYVYTGPLYVPNLLD------------- 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26353972   799 virSQEILIPTHFFIVLtsckqLSETPLECSALESSAYILPHRPdniescthGKRESSWVEELLTlhrarVTDVELITGL 878
Cdd:pfam01223 153 ---KNKVAVPTHFWKVI-----LSEDGDGGGGLNAPAFVLPNKY--------ILDDGPLRTFQVP-----VDELERLTGL 211


                  ..
gi 26353972   879 SF 880
Cdd:pfam01223 212 DF 213
sulfatase_like cd16148
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ...
 192-411 4.13e-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: 55.63  E-value: 4.13e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26353972 192 PPTLLFSLDGFRAEYLHTWGGLL---PVISKL-------KNCgtYTKNMRpmyptkTFPNHYSIVTGLYPESHGIIDNKM 261
Cdd:cd16148   1 MNVILIVIDSLRADHLGCYGYDRvttPNLDRLaaegvvfDNH--YSGSNP------TLPSRFSLFTGLYPFYHGVWGGPL 72

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26353972 262 ydpkmnasfslkskEKFNPLWY-----KGqpiWVTA---NHQEVKSGTYFWPGSDVEIDGILPDIYKVYNGSVPFEERIL 333
Cdd:cd16148  73 --------------EPDDPTLAeilrkAG---YYTAavsSNPHLFGGPGFDRGFDTFEDFRGQEGDPGEEGDERAERVTD 135

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26353972 334 AVLEWLQLPSHERPHFYTLYLEEPdssghsHGP------VSsevikalqKVDRLVGMLMDGLKDLGL-DKCLnLILISDH 406
Cdd:cd16148 136 RALEWLDRNADDDPFFLFLHYFDP------HEPylydaeVR--------YVDEQIGRLLDKLKELGLlEDTL-VIVTSDH 200


                ....*
gi 26353972 407 GMEQG 411
Cdd:cd16148 201 GEEFG 205
PTZ00259 PTZ00259
endonuclease G; Provisional
 598-883 1.32e-06

endonuclease G; Provisional


Pssm-ID: 240335 [Multi-domain]  Cd Length: 434  Bit Score: 51.79  E-value: 1.32e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26353972  598 IKSTSNDLGCTCDPWIVPIKDFEKQLNLTTEDDDIYHMTVPYGRP---RILLKQHHVcllqqqqflTGYSLDLLMPLW-A 673
Cdd:PTZ00259  62 VKSVVSGNALKKVTELPPPYPSEQASTARADTLPFCKEYPSFGLPsteNLRLYEGYV---------SSLNYERRIPNWvA 132

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26353972  674 SYTFLRNDQFSRD----DFSNC-LYQDLRIPLSPVHKCSYYKSnSKLSYGFLTPPRLNRVSNHIYSEA-LLTSNIVPmyQ 747
Cdd:PTZ00259 133 EYIPYRGISVEAGekkaNRADCvFYADPTVPEAFRAENKDYTG-SGYSRGHLAAAGFHKASQTAMDDTfLLSANIVP--Q 209

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26353972  748 SF---QVIWHYLHD-TLLQRYAHErNGINVVSGPVFDFDYDGRYDSLEILKQNSR-------------------VIRSQE 804
Cdd:PTZ00259 210 DLtnnAGDWLRLENlTRKLAREYE-VGVYVVSGPLFVPRYMREKLRKWRLAEPSEihkpdspadktpkkvvtyeVIGDNN 288

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 26353972  805 ILIPTHFFIVLtsckqLSETPLECSAlESSAYILPHRPdnIEScthgkresswvEELLTLHRARVTDVELITGLSFYQD 883
Cdd:PTZ00259 289 VAVPTHLFKVI-----LAEKNDGPPH-EVAAFLMPNEP--ISK-----------EKPLTAYQVPLEEIEKLTGLQFFPK 348
AP-SPAP cd16016
SPAP is a subclass of alkaline phosphatase (AP); Alkaline phosphatases are non-specific ...
 200-265 3.78e-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: 47.14  E-value: 3.78e-05
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 26353972 200 DGFRAEYLH------TWGGLLpvisKLKNCGTYTKNMR-PMYPTKTFPNHYSIVTGLYPESHGIIDNKMYDPK 265
Cdd:cd16016  11 DQMRADYLYryrdrfGEGGFK----RLLNEGFVFENAHyNYAPTDTAPGHATIYTGTTPAIHGIIGNDWYDRE 79
GPI_EPT_1 cd16020
GPI ethanolamine phosphate transferase 1; PIG-N; Ethanolamine phosphate transferase is ...
 344-412 3.29e-04

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: 43.73  E-value: 3.29e-04
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26353972 344 HERPHFYTLYLEEPDSSGHSHGPVSSEVIKALQKVDRLVGMLMDGLKDLGLDKCLNLILISDHGM-EQGS 412
Cdd:cd16020 154 NQDGLVFFLHLLGLDTNGHAHKPYSKEYLENIRYVDKGIEKTYPLIEEYFNDGRTAYIFTSDHGMtDWGS 223
AslA COG3119
Arylsulfatase A or related enzyme, AlkP superfamily [Inorganic ion transport and metabolism];
378-411 6.87e-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: 6.87e-03
                        10        20        30
                ....*....|....*....|....*....|....*.
gi 26353972 378 VDRLVGMLMDGLKDLGLDKclNLILI--SDHGMEQG 411
Cdd:COG3119 209 VDDQVGRLLDALEELGLAD--NTIVVftSDNGPSLG 242
iduronate-2-sulfatase cd16030
iduronate-2-sulfatase; Iduronate 2-sulfatase is a sulfatase enzyme that catalyze the ...
 378-407 9.64e-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: 39.48  E-value: 9.64e-03
                        10        20        30
                ....*....|....*....|....*....|..
gi 26353972 378 VDRLVGMLMDGLKDLGLDKclNLI--LISDHG 407
Cdd:cd16030 270 VDAQVGRVLDALEELGLAD--NTIvvLWSDHG 299
 
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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